|
Name |
Accession |
Description |
Interval |
E-value |
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-252 |
3.08e-131 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 370.93 E-value: 3.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAVFESI 245
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLREI 242
|
....*..
gi 1561673794 246 YGRSLTA 252
Cdd:COG3638 243 YGGEAEE 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-246 |
1.01e-114 |
|
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: 329.14 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAVFESI 245
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 1561673794 246 Y 246
Cdd:cd03256 241 Y 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-247 |
6.71e-112 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 321.94 E-value: 6.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAVFESI 245
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
..
gi 1561673794 246 YG 247
Cdd:TIGR02315 242 YG 243
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-246 |
1.67e-69 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 214.88 E-value: 1.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 19 HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS-----SRGLRDLRGDIGMIFQGFN 93
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQregrlARDIRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 LAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILA 173
Cdd:PRK09984 97 LVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 174 DEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAVFESIY 246
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLY 249
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-247 |
1.38e-66 |
|
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: 207.20 E-value: 1.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrDLRGDI 85
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR---ELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLhssPmWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRY---P-HLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDA-DEAVFES 244
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVlTPELLEE 233
|
...
gi 1561673794 245 IYG 247
Cdd:COG1120 234 VYG 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-229 |
1.65e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.05 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:COG1136 5 LELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GD-IGMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:COG1136 85 RRhIGFVFQFFNLLPELTALENVAL------PL--LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLArRYGDRLIGLRDGKVV 229
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-228 |
2.44e-66 |
|
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: 205.42 E-value: 2.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT---ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GD-IGMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVEL------PL--LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLArRYGDRLIGLRDGKV 228
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-234 |
1.66e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 198.35 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVAL------PL--RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAeLGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHG 234
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-232 |
1.87e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 199.15 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGaWSAED-----TELgmqaLERVEIVGKAYEKASSLSGGQQQR 157
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVAL------PL--EIAG-VPKAEirkrvAEL----LELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-232 |
5.99e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 194.83 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVnTLSSRGLRDLRGDI 85
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGrlhssPMWrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLA-----PIK--VKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 166 QQPRVILADEPVASLDPP-TSHV--VMRDLqrinAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG1126 153 MEPKVMLFDEPTSALDPElVGEVldVMRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-229 |
2.30e-61 |
|
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: 193.18 E-value: 2.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGH---TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQGFNLAKRTSVLNNVMMgrlhssPmwrtlLGAWSAEDTELGMQALERVEIVG---KAYEKASSLSGGQQQRVA 159
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL------P-----LEIAGVPKAEIEERVLELLELVGledKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-228 |
1.06e-58 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 185.43 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVnTLSSRGLRDLRGDI 85
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGrlhssPMWrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLA-----PIK--VKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVV---MRDLqrinAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVldvMKDL----AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-250 |
2.01e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 178.36 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVpvttgtvtvgdRAVN---TLSSRG 77
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLL-----------PPTSgtvRLFGKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGDIGMIFQGFNLAKR--TSVLNNVMMGRLHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQ 155
Cdd:COG1121 70 PRRARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRP----SRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLrDGKVVFDGHGR 235
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
250
....*....|....*.
gi 1561673794 236 DA-DEAVFESIYGRSL 250
Cdd:COG1121 224 EVlTPENLSRAYGGPV 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-233 |
1.32e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 179.23 E-value: 1.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:PRK11153 2 IELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQGFNLAKRTSVLNNVMMgrlhssPMwrtLLGAWSAED-----TELgmqaLERVEIVGKAYEKASSLSGGQQQR 157
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL------PL---ELAGTPKAEikarvTEL----LELVGLSDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-237 |
1.97e-54 |
|
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: 175.21 E-value: 1.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRavnTLSSRGLRDLRGDI 85
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK---DITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQG-----FNlakrTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAI 160
Cdd:COG1122 78 GLVFQNpddqlFA----PTVEEDVAFGPEN--------LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDA 237
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-233 |
1.15e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 173.74 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlSSRGLRDLRGDI 85
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLR-------VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 166 QQPRVILADEPVASLDPPTSH---VVMRDLqrinAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHevlKVMQDL----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-227 |
1.79e-52 |
|
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: 168.52 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLsSRGLRDLRGDI 85
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIARALA 165
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG------------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGK 227
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-232 |
1.32e-51 |
|
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: 175.48 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTY----AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL 81
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQG----FNlaKRTSVLNNVMMG-RLHsspmwrtllGAWSAED-TELGMQALERVEIVGKAYEK-ASSLSGGQ 154
Cdd:COG1123 341 RRRVQMVFQDpyssLN--PRMTVGDIIAEPlRLH---------GLLSRAErRERVAELLERVGLPPDLADRyPHELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 155 QQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-232 |
1.87e-51 |
|
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: 166.07 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlrgdigmi 88
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 fqgfNLAKRTSVLNnvmmgrlhsspmwrtllgawsaedtelgmQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:cd03214 70 ----ELARKIAYVP-----------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-232 |
3.51e-50 |
|
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: 164.77 E-value: 3.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQG---F-NLakrtSVLNNVMMG-RLHsspmwrTLLGAwsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAI 160
Cdd:COG1127 85 GMLFQGgalFdSL----TVFENVAFPlREH------TDLSE--AEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-232 |
1.54e-49 |
|
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: 163.06 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMG-RLHsspmwrTLLGAWsaEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPlREH------TRLSEE--EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-232 |
3.48e-49 |
|
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: 161.16 E-value: 3.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgDRAVNTLSSRGLRDLRGDIGM 87
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP--------TSGSIRVFGKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQGFNLAK--RTSVLNNVMMGRLHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:cd03235 73 VPQRRSIDRdfPISVRDVVLMGLYGHKGLFRRL----SKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLrDGKVVFDG 232
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-227 |
8.57e-49 |
|
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: 160.49 E-value: 8.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVAL------PL--EVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAeLGITVVVNLHFLDLARRYGDRLIGLRDGK 227
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-228 |
2.57e-48 |
|
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: 159.11 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhssPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF------AL--EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-255 |
4.62e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 4.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDI 85
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNV-MMGRLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLrFFARLYGLP---------RKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAVFES 244
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLED 225
|
250
....*....|.
gi 1561673794 245 IYgRSLTAEDV 255
Cdd:COG1131 226 VF-LELTGEEA 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-229 |
7.29e-47 |
|
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: 155.37 E-value: 7.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlRGDIGM 87
Cdd:cd03259 3 LKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQGFNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGlKLRGVP---------KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-229 |
3.00e-46 |
|
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: 154.20 E-value: 3.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQGFNlakrtSVLNNVM-MGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEK-ASSLSGGQQQRVAI 160
Cdd:cd03257 82 KEIQMVFQDPM-----SSLNPRMtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-229 |
3.12e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.79 E-value: 3.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVN---TLSSRGLRDL 81
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQGFNLAKRTSVLNNvmmgrLHSSPMWrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEN-----LIEAPCK--VLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 162 RALAQQPRVILADEPVASLDPP-TSHVV--MRDLqrinAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEiTAQVVeiIREL----SQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-204 |
1.82e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDG--IAFDNVSVTYA---GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgDRAVN---T 72
Cdd:COG1116 1 MSAAApaLELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-----------EKPTSgevL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 73 LSSRGLRDLRGDIGMIFQGFNLAKRTSVLNNVMMGrLHsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSG 152
Cdd:COG1116 70 VDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALG-LE-------LRGVPKAERRERARELLELVGLAGFEDAYPHQLSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 153 GQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVV 204
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVL 193
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-232 |
3.61e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 152.99 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQgF---NLAKRTsVLNNVMMGrlhssPMwrtLLGAWSAEDTELGMQALERVEIVGKAYEKAS-SLSGGQQQR 157
Cdd:TIGR04521 81 RKKVGLVFQ-FpehQLFEET-VYKDIAFG-----PK---NLGLSEEEAEERVKEALELVGLDEEYLERSPfELSGGQMRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-241 |
3.81e-44 |
|
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: 150.10 E-value: 3.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRG-DIGMIFQGFNLAKRTS 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVMMGrlhsspmwRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVAS 179
Cdd:cd03294 119 VLENVAFG--------LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 180 LDPptshVVMRDLQ----RINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD-----ADEAV 241
Cdd:cd03294 191 LDP----LIRREMQdellRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEiltnpANDYV 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-238 |
3.99e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSgdgIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVN---TLSSRG 77
Cdd:PRK11124 1 MS---IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGDIGMIFQGFNLAKRTSVLNNvmmgrLHSSPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQR 157
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHLTVQQN-----LIEAPC--RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPP-TSHVV--MRDLQrinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGhg 234
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEiTAQIVsiIRELA----ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-- 223
|
....
gi 1561673794 235 rDAD 238
Cdd:PRK11124 224 -DAS 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-229 |
4.41e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 148.48 E-value: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTV-----GDRAVNTLSSRGLRd 80
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevllDGKDIYDLDVDVLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAkRTSVLNNVMMG-RLHSSpmwrtllgAWSAEDTELGMQALERVEIVGKAYEK--ASSLSGGQQQR 157
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVAYGlRLHGI--------KLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElgITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-227 |
1.11e-43 |
|
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: 146.84 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGDIG 86
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQG-----FNlakrTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:cd03225 79 LVFQNpddqfFG----PTVEEEVAFGLEN--------LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGK 227
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-229 |
1.37e-43 |
|
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: 147.23 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgDRAVNTLSSRGLRDLR 82
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERP--------TSGEVLVDGEPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIvgKAYEKA--SSLSGGQQQRVAI 160
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGL--------ELQGVPKAEARERAEELLELVGL--SGFENAypHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGL--RDGKVV 229
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIV 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-236 |
1.19e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.59 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGD 84
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFnlakrTSVLNNVMMGRLHSSPMWRTLLGAwsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:COG1123 85 IGMVFQDP-----MTQLNPVTVGDQIAEALENLGLSR--AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-241 |
1.28e-42 |
|
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: 144.89 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRgLRDLRGdIGMI 88
Cdd:cd03219 4 RGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLG-IGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDT--ELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD--ADEAV 241
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEvrNNPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-232 |
5.54e-42 |
|
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: 144.03 E-value: 5.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDlRGdIGMI 88
Cdd:COG0411 8 RGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIAR-LG-IART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRL--HSSPMWRTLLGAWS-----AEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHarLGRGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-229 |
2.27e-41 |
|
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: 141.80 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGH---TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR 82
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GD-IGMIFQGFNLAKRTSVLNNVMMgrlhssPMWrtLLGAwsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:COG4181 89 ARhVGFVFQSFQLLPTLTALENVML------PLE--LAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVV 229
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
9-232 |
1.10e-40 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.68 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRgdiGMI 88
Cdd:PRK13548 6 RNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR---AVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ-- 166
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAP--------HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 167 ----QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-233 |
3.02e-40 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 139.48 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRG----D 84
Cdd:COG4559 5 ENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAvlpqH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFqGFnlakrtSVLNNVMMGRL-HSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:COG4559 84 SSLAF-PF------TVEEVVALGRApHGSS---------AAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 164 LAQ-------QPRVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:COG4559 148 LAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGT 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-223 |
3.13e-40 |
|
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: 138.13 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL-RGDIGMI 88
Cdd:TIGR03608 3 NISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRLHSSPMWRtllgawsaEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKK--------EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRyGDRLIGL 223
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-252 |
5.09e-40 |
|
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: 138.78 E-value: 5.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGH---TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlSSRGLRDLRGDI 85
Cdd:COG1124 5 RNLSVSYGQGGrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQgfnlaKRTSVLNNVM-MGRLHSSPMWRTLLGAWSAEDTELgmqaLERVEIVGK-AYEKASSLSGGQQQRVAIARA 163
Cdd:COG1124 82 QMVFQ-----DPYASLHPRHtVDRILAEPLRIHGLPDREERIAEL----LEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGhGRDADEAVFE 243
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL-TVADLLAGPK 231
|
....*....
gi 1561673794 244 SIYGRSLTA 252
Cdd:COG1124 232 HPYTRELLA 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
18-235 |
9.30e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.34 E-value: 9.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRG-----LRDLRGDIGMIFQGF 92
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 93 NLAKRTSVLNNVMMGRLhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVIL 172
Cdd:PRK11264 95 NLFPHRTVLENIIEGPV-------IVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 173 ADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.47e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.23 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrd 80
Cdd:COG3842 1 MAMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 lRGDIGMIFQGFNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVA 159
Cdd:COG3842 76 -KRNVGMVFQDYALFPHLTVAENVAFGlRMRGVP---------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-236 |
2.61e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 137.24 E-value: 2.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRG----------LRDLRGDIG 86
Cdd:COG4598 19 GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrrqLQRIRTRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMGRLHsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:COG4598 99 MVFQSFNLWSHMTVLENVIEAPVH-------VLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 167 QPRVILADEPVASLDPP-TSHV--VMRDLqrinAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:COG4598 172 EPEVMLFDEPTSALDPElVGEVlkVMRDL----AEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-232 |
5.02e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 136.79 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDraVNTLSSRGLRDLRGD 84
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQ-------GfnlakrTSVLNNVMMG----RLHSSPMWRTLLgawsaedtelgmQALERVEIVGKAYEKASSLSGG 153
Cdd:TIGR04520 79 VGMVFQnpdnqfvG------ATVEDDVAFGlenlGVPREEMRKRVD------------EALKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDG 232
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-233 |
1.22e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.48 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTL----------SSRGLRDLRGDIG 86
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMmgrlhSSPMwrTLLGAWSAEDTELGMQALERVEIVGKAYEK-ASSLSGGQQQRVAIARALA 165
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVM-----EAPI--QVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-232 |
5.85e-38 |
|
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: 140.74 E-value: 5.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGD 84
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTsVLNNVMMGRLHsspmwrtllgawsAEDTELgMQALERVEI--------------VGkayEKASSL 150
Cdd:COG2274 551 IGVVLQDVFLFSGT-IRENITLGDPD-------------ATDEEI-IEAARLAGLhdfiealpmgydtvVG---EGGSNL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYgDRLIGLRDGKVVF 230
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVE 689
|
..
gi 1561673794 231 DG 232
Cdd:COG2274 690 DG 691
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-233 |
1.74e-37 |
|
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: 138.35 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL 81
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIG---MIFQGfnlakrtSVLNNVMMGRLHSSP--MWRTL----LGAWSAE-----DTELGmqalerveivgkayEKA 147
Cdd:COG4988 413 IAWVPqnpYLFAG-------TIRENLRLGRPDASDeeLEAALeaagLDEFVAAlpdglDTPLG--------------EGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYgDRLIGLRDGK 227
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGR 548
|
....*.
gi 1561673794 228 VVFDGH 233
Cdd:COG4988 549 IVEQGT 554
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-232 |
4.53e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 131.29 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlrgdigmi 88
Cdd:PRK11231 6 ENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 fqgfNLAKRTSVLNNVMM-------------GRlhsSPmWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQ 155
Cdd:PRK11231 73 ----QLARRLALLPQHHLtpegitvrelvayGR---SP-WLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDppTSHVV--MRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLD--INHQVelMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-247 |
7.78e-37 |
|
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: 130.36 E-value: 7.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDI 85
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMM-GRLHsspmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYfAELY---------GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG--------HGRD 236
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGsldelreeIGEE 226
|
250
....*....|.
gi 1561673794 237 ADEAVFESIYG 247
Cdd:COG4555 227 NLEDAFVALIG 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-232 |
9.54e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.87 E-value: 9.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYagGHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrglrDLRGdI 85
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AERP-V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGrLHSSpmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLG-LRPG-------LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 166 QQPRVILADEPVASLDPptshvVMRD-----LQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG3840 146 RKRPILLLDEPFSALDP-----ALRQemldlVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-227 |
1.92e-36 |
|
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: 126.59 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDlrgDIGM 87
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR---RIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQgfnlakrtsvlnnvmmgrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIARALAQQ 167
Cdd:cd00267 78 VPQ-----------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGK 227
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-247 |
3.27e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 129.05 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlrgdi 85
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSR--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 gmifqgfNLAKRTSVL--NNVMMGRL------------HSSpmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASSLS 151
Cdd:COG4604 72 -------ELAKRLAILrqENHINSRLtvrelvafgrfpYSK-------GRLTAEDREIIDEAIAYLDLEDLADRYLDELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 152 GGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFD 231
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
250
....*....|....*..
gi 1561673794 232 GHGRD-ADEAVFESIYG 247
Cdd:COG4604 218 GTPEEiITPEVLSDIYD 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-229 |
4.61e-36 |
|
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: 128.19 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGDI 85
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhsSPmwrTLLGaWSAEDTE------LGMQALERVEIVGKaYekASSLSGGQQQRVA 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-----VP---KLLK-WPKEKIReradelLALVGLDPAEFADR-Y--PHELSGGQQQRVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-231 |
5.05e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.64 E-value: 5.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 3 GDGIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTtgtvtvgdrAVNTLSSRG-LRDL 81
Cdd:PRK11247 10 GTPLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS---------AGELLAGTApLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQGFNLAKRTSVLNNVMMGrlhsspmwrtLLGAWSAEdtelGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:PRK11247 80 REDTRLMFQDARLLPWKKVIDNVGLG----------LKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTsHVVMRDL-QRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFD 231
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALT-RIEMQDLiESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-178 |
6.66e-36 |
|
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: 125.07 E-value: 6.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAvntLSSRGLRDLRGDIGMIFQGFNLAKRTSVL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 NNVMMGRLHSSPMwrtllGAWSAEDTElgmQALERVEIVGKAYEKA----SSLSGGQQQRVAIARALAQQPRVILADEPV 177
Cdd:pfam00005 78 ENLRLGLLLKGLS-----KREKDARAE---EALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 1561673794 178 A 178
Cdd:pfam00005 150 A 150
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-232 |
7.00e-36 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 128.18 E-value: 7.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGD---RAVNTLSSR-GLRDLRGDI 85
Cdd:TIGR00972 6 NLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKvlfDGQDIYDKKiDVVELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRtSVLNNVMMG-RLHsspmwrtllGAWS-AEDTELGMQALERV----EIVGKAYEKASSLSGGQQQRVA 159
Cdd:TIGR00972 85 GMVFQKPNPFPM-SIYDNIAYGpRLH---------GIKDkKELDEIVEESLKKAalwdEVKDRLHDSALGLSGGQQQRLC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVV---MRDLQRinaelGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIeelIQELKK-----KYTIVIVTHNMQQAARISDRTAFFYDGELVEYG 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-229 |
3.27e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 127.90 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGDI 85
Cdd:COG1125 2 IEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhsSPMwrtLLGaWSAEDT-----ELgmqaLERV----EIVGKAYekASSLSGGQQQ 156
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIAT-----VPR---LLG-WDKERIrarvdEL----LELVgldpEEYRDRY--PHELSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG1125 144 RVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
21-227 |
7.20e-35 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 124.45 E-value: 7.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS-SRGLRDLRGDIGMIFQGFNLAKRTS 99
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSySQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVMMgrlhssPM-WRtllGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVA 178
Cdd:NF038007 100 IFDNVAL------PLkYR---GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTG 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1561673794 179 SLDPPTSHVVMRDLQRINAElGITVVVNLHFlDLARRYGDRLIGLRDGK 227
Cdd:NF038007 171 NLDSKNARAVLQQLKYINQK-GTTIIMVTHS-DEASTYGNRIINMKDGK 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-235 |
1.05e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.22 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhssPMwrtLLGAWSAEDTELGMQ-ALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAI------PL---IIAGASGDDIRRRVSaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-219 |
1.31e-34 |
|
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: 126.32 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTY---AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTV---TVGDRAVNTLSSRGLRDLR 82
Cdd:COG0444 5 RNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSgeiLFDGEDLLKLSEKELRKIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 G-DIGMIFQGfnlakRTSVLNNVM-MGRLHSSPMwRTLLGAWSAEDTELGMQALERVEI-----VGKAY--EkassLSGG 153
Cdd:COG0444 85 GrEIQMIFQD-----PMTSLNPVMtVGDQIAEPL-RIHGGLSKAEARERAIELLERVGLpdperRLDRYphE----LSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDR 219
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-236 |
1.31e-34 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgdI 85
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR---V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRlhsSPMwRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGR---TPH-RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 166 QQPRVILADEPVASLDppTSHVVMR-DLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-228 |
1.64e-34 |
|
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: 124.37 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlSSRGLRDlRGd 84
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQE-RN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMGrLHSSPMWRTllgAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFG-LRVKPRSER---PPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-229 |
2.22e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.73 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlRGDI 85
Cdd:COG3839 4 LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPlKLRKVP---------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 165 AQQPRVILADEPVASLDPPtSHVVMR-DLQRINAELGITVVVNLHflDL--ARRYGDRLIGLRDGKVV 229
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAK-LRVEMRaEIKRLHRRLGTTTIYVTH--DQveAMTLADRIAVMNDGRIQ 213
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
2.68e-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: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRD 80
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LrgdIGMIFQG---FNlakrTSVLNNVMMGRLHSSP--MWRTL----LGAWSAE-----DTELGmqalerveivgkayEK 146
Cdd:COG4987 410 R---IAVVPQRphlFD----TTLRENLRLARPDATDeeLWAALervgLGDWLAAlpdglDTWLG--------------EG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 147 ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYgDRLIGLRDG 226
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDG 545
|
....*.
gi 1561673794 227 KVVFDG 232
Cdd:COG4987 546 RIVEQG 551
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-236 |
2.85e-34 |
|
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: 123.50 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTL--SSRGlrdlrg 83
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLppHKRP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 dIGMIFQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:cd03300 74 -VNTVFQNYALFPHLTVFENIAFGL--------RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-229 |
2.99e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.51 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIR-------------TINGlvpvttgtvtvgdRAVN 71
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNlllrfydptsgriLIDG-------------VDIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 72 TLSsrgLRDLRGDIGMIFQGFNLAKRTsVLNNVMMGRLHsspmwrtllgawsAEDTELgMQALERVEI------------ 139
Cdd:COG1132 406 DLT---LESLRRQIGVVPQDTFLFSGT-IRENIRYGRPD-------------ATDEEV-EEAAKAAQAhefiealpdgyd 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 140 --VGkayEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYg 217
Cdd:COG1132 468 tvVG---ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA- 541
|
250
....*....|..
gi 1561673794 218 DRLIGLRDGKVV 229
Cdd:COG1132 542 DRILVLDDGRIV 553
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-232 |
3.15e-34 |
|
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: 122.93 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglRDLRGDIGMI 88
Cdd:cd03224 4 ENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRLHSSPmwrtllgawsaedtELGMQALERVeivgkaYE-----------KASSLSGGQQQR 157
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR--------------AKRKARLERV------YElfprlkerrkqLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-227 |
3.99e-34 |
|
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: 120.95 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGD 84
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTsVLNNVmmgrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIARAL 164
Cdd:cd03228 78 IAYVPQDPFLFSGT-IRENI---------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYgDRLIGLRDGK 227
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-229 |
9.96e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 125.60 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR-GDIGMIFQGFNL- 94
Cdd:COG4175 38 GQTvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRrKKMSMVFQHFALl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTsVLNNVMMGrLHsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:COG4175 118 PHRT-VLENVAFG-LE-------IQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 175 EPVASLDPptshVVMRDLQ----RINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4175 189 EAFSALDP----LIRREMQdellELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-228 |
3.91e-33 |
|
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: 118.65 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvTVGDR---AVNTLS-SRGLRDL 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--------LKPDSgeiKVLGKDiKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQGFNLAKRTSVLNNVMmgrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIA 161
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLK--------------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-229 |
4.18e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.33 E-value: 4.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSgdgIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlsSRGLRD 80
Cdd:COG1118 1 MS---IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT--NLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRgdIGMIFQGFNLAKRTSVLNNVMMGrLHSSPMWRtllgawsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAI 160
Cdd:COG1118 75 RR--VGFVFQHYALFPHMTVAENIAFG-LRVRPPSK-------AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 161 ARALAQQPRVILADEPVASLDpptSHV---VMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALD---AKVrkeLRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-228 |
5.44e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.15 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGDI 85
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQgfnlakrtsvlnnvmmgrlhSSPMW---------RTLLGAWSAEDTELGMQALERVEIVGKAYEK-ASSLSGGQQ 155
Cdd:COG4619 77 AYVPQ--------------------EPALWggtvrdnlpFPFQLRERKFDRERALELLERLGLPPDILDKpVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-245 |
1.11e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 120.72 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 15 YAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtLSSRGLRDLRGDIGMIFQG-FN 93
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQDpDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 LAKRTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILA 173
Cdd:PRK13636 94 QLFSASVYQDVSFGAVN--------LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 174 DEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD--ADEAVFESI 245
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEvfAEKEMLRKV 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-232 |
3.93e-32 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 117.21 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYagGHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTING--LVPVTTGTVTVGDRAVNTLSSRglrdlrg 83
Cdd:cd03298 1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfeTPQSGRVLINGVDVTAAPPADR------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQGFNLAKRTSVLNNVMMGRlhsSPMWRTllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:cd03298 71 PVSMLFQENNLFAHLTVEQNVGLGL---SPGLKL-----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-232 |
5.70e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRavnTLSSRGLR 79
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 DLRGDIGMIFQG-FNLAKRTSVLNNVMMGrLHSSPMWRTllgawsaEDTELGMQALERVEIVGKAYEKASSLSGGQQQRV 158
Cdd:PRK13635 78 DVRRQVGMVFQNpDNQFVGATVQDDVAFG-LENIGVPRE-------EMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDG 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-228 |
7.92e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 7.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGG--HT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRG-D 84
Cdd:PRK11629 9 DNLCKRYQEGsvQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMGRLhsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLL--------IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYgDRLIGLRDGKV 228
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-229 |
9.96e-32 |
|
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: 116.20 E-value: 9.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlRGDIGMI 88
Cdd:cd03301 4 ENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQ 167
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGlKLRKVP---------KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 168 PRVILADEPVASLDPPTsHVVMR-DLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03301 149 PKVFLMDEPLSNLDAKL-RVQMRaELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-255 |
1.02e-31 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 119.96 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL-RGDIGMIFQGFNLA 95
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:TIGR01186 84 PHMTILQNTSLGP--------ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 176 PVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD-----ADEAVFESIYG--- 247
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEilrnpANEYVEEFIGKvdl 235
|
....*....
gi 1561673794 248 -RSLTAEDV 255
Cdd:TIGR01186 236 sQVFDAERI 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
9-241 |
4.57e-31 |
|
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: 115.08 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSS-----RGlrdlrg 83
Cdd:COG0410 7 ENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriarLG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 dIGMIFQGFNLAKRTSVLNNVMMgrlhsspmwrtllGAWSAEDTELGMQALERVeivgkaYE-----------KASSLSG 152
Cdd:COG0410 80 -IGYVPEGRRIFPSLTVEENLLL-------------GAYARRDRAEVRADLERV------YElfprlkerrrqRAGTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 153 GQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVV---NLHFldlARRYGDRLIGLRDGKVV 229
Cdd:COG0410 140 GEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLveqNARF---ALEIADRAYVLERGRIV 215
|
250
....*....|....
gi 1561673794 230 FDGHGRD--ADEAV 241
Cdd:COG0410 216 LEGTAAEllADPEV 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-232 |
4.79e-31 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 114.31 E-value: 4.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIP---AGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtlSSRGLRDL---RGDIGMIFQGFNLA 95
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSRKKINLppqQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGrlhsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:cd03297 88 PHLNVRENLAFG----------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 176 PVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-182 |
5.36e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.52 E-value: 5.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTV----------GDRAVNtlss 75
Cdd:COG1117 12 IEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEgeilldgediYDPDVD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 76 rgLRDLRGDIGMIFQGFN-LAKrtSVLNNVMMG-RLHsspmwrtllGAWSAEDT-ELGMQALERV----EIVGKAYEKAS 148
Cdd:COG1117 87 --VVELRRRVGMVFQKPNpFPK--SIYDNVAYGlRLH---------GIKSKSELdEIVEESLRKAalwdEVKDRLKKSAL 153
|
170 180 190
....*....|....*....|....*....|....
gi 1561673794 149 SLSGGQQQRVAIARALAQQPRVILADEPVASLDP 182
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-228 |
1.61e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.34 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSgdgIAFDNVSVTYagGHTA-LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLR 79
Cdd:PRK10851 1 MS---IEIANIKKSF--GRTQvLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 dlrgdIGMIFQGFNLAKRTSVLNNVMMG-----RlHSSPMwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQ 154
Cdd:PRK10851 76 -----VGFVFQHYALFRHMTVFDNIAFGltvlpR-RERPN--------AAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 155 QQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-259 |
1.74e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRgdIGMIF 89
Cdd:COG1129 9 GISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG--IAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFNLAKRTSVLNNVMMGRLHSSPM---WRTLlgawsAEDTElgmQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:COG1129 86 QELNLVPNLSVAENIFLGREPRRGGlidWRAM-----RRRAR---ELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 167 QPRVILADEPVASLDPP-TSHV--VMRDLQrinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEA-VF 242
Cdd:COG1129 158 DARVLILDEPTASLTEReVERLfrIIRRLK----AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDeLV 233
|
250 260
....*....|....*....|....*..
gi 1561673794 243 ESIYGRSLT----------AEDVLEAK 259
Cdd:COG1129 234 RLMVGRELEdlfpkraaapGEVVLEVE 260
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-229 |
1.75e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 111.37 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRgdI 85
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQgfnlakrtsvlnnvmmgrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIARALA 165
Cdd:cd03216 78 AMVYQ-----------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDPP-TSHV--VMRDLQrinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03216 99 RNARLLILDEPTAALTPAeVERLfkVIRRLR----AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-232 |
4.42e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 4.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtlsSRGLRDLRGDI 85
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQG-----FNlakrTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAI 160
Cdd:PRK13647 82 GLVFQDpddqvFS----STVWDDVAFGPVN--------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-232 |
7.16e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtLSSRGLRDLRGDIGMIF 89
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFN---LAKRtsVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:PRK13639 85 QNPDdqlFAPT--VEEDVAFGPLN--------LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-236 |
7.49e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDraVNTLSSRGLRD 80
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQG-FNLAKRTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIvgKAYEKASS--LSGGQQQR 157
Cdd:PRK13633 83 IRNKAGMVFQNpDNQIVATIVEEDVAFGPEN--------LGIPPEEIRERVDESLKKVGM--YEYRRHAPhlLSGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDGHGRD 236
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKE 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-232 |
8.65e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 111.81 E-value: 8.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDravNTLSSRGLRDLRGD 84
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRtSVLNNVMMGRlHSSPMWRTLLGAWSAEDTELGMQALERVE-IVGkayEKASSLSGGQQQRVAIARA 163
Cdd:cd03252 78 VGVVLQENVLFNR-SIRDNIALAD-PGMSMERVIEAAKLAGAHDFISELPEGYDtIVG---EQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDG 232
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-213 |
1.03e-29 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 110.21 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 15 YAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtLSSRGLRDLRGDIGMIFQG--- 91
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLLERRQRVGLVFQDpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 92 --FNlakrTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPR 169
Cdd:TIGR01166 80 qlFA----ADVDQDVAFGPLN--------LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1561673794 170 VILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLA 213
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-254 |
2.07e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 111.62 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrDLRGDIGMI 88
Cdd:PRK10253 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRLHSSPMWRTllgaWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTR----WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD-ADEAVFESIYG 247
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEiVTAELIERIYG 242
|
....*...
gi 1561673794 248 -RSLTAED 254
Cdd:PRK10253 243 lRCMIIDD 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
2.80e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.65 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAV-NTLSSRGLRD 80
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQgF---NLAKRTsVLNNVMMGrlhssPMwrtLLGAwSAEDTELgmQALERVEIVGKAYEKAS----SLSGG 153
Cdd:PRK13634 83 LRKKVGIVFQ-FpehQLFEET-VEKDICFG-----PM---NFGV-SEEDAKQ--KAREMIELVGLPEELLArspfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
...
gi 1561673794 234 GRD 236
Cdd:PRK13634 230 PRE 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-240 |
3.38e-29 |
|
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: 109.92 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglRDLRGDIGMI 88
Cdd:TIGR03410 4 SNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGrlhsspmwrtllgawsaedtelgMQALERVE--IVGKAYE-----------KASSLSGGQQ 155
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-----------------------LAALPRRSrkIPDEIYElfpvlkemlgrRGGDLSGGQQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:TIGR03410 138 QQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGD 217
|
....*
gi 1561673794 236 DADEA 240
Cdd:TIGR03410 218 ELDED 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-232 |
3.40e-29 |
|
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: 110.56 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGtvtvgdravNTLS----SRG---L 78
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG---------NDVRlfgeRRGgedV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 79 RDLRGDIGMI--FQGFNLAKRTSVLNNVMMGRLHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQ 156
Cdd:COG1119 74 WELRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYREP----TDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-236 |
4.17e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVtyagghtaLDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVN--TLSSRGLRDLRG 83
Cdd:PRK14247 11 VSFGQVEV--------LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDgqDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQGFNLAKRTSVLNNVMMG----RLHSSpmwrtllgawSAEDTELGMQALERV----EIVGKAYEKASSLSGGQQ 155
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGlklnRLVKS----------KKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVnlHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT--HFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
.
gi 1561673794 236 D 236
Cdd:PRK14247 231 E 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-247 |
5.54e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtlsSRGLRDLRGD 84
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQG-FNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIAR 162
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVKYDVAFGlENHAVP---------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDGHGRDadeaVF 242
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTE----IF 230
|
....*
gi 1561673794 243 ESIYG 247
Cdd:PRK13648 231 DHAEE 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-243 |
5.90e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT----ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNT-LSSRGLRD 80
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQgFNLAK--RTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKAS-SLSGGQQQR 157
Cdd:PRK13641 83 LRKKVSLVFQ-FPEAQlfENTVLKDVEFGPKN--------FGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVM---RDLQRInaelGITVVVNLHFLDLARRYGDRLIGLRDGKVVfdghG 234
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMqlfKDYQKA----GHTVILVTHNMDDVAEYADDVLVLEHGKLI----K 225
|
....*....
gi 1561673794 235 RDADEAVFE 243
Cdd:PRK13641 226 HASPKEIFS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-231 |
9.98e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.44 E-value: 9.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTA---LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGD-I 85
Cdd:PRK10535 9 DIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSspmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK10535 89 GFIFQRYHLLSHLTAAQNVEVPAVYA--------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDLARRyGDRLIGLRDGKVVFD 231
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-213 |
1.15e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQG-FnlakrtS 99
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpY------A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVM-MGRLHSSPMwrTLLGAWSAEDTElgmqalERV----EIVGKAYEKASS----LSGGQQQRVAIARALAQQPRV 170
Cdd:COG4608 107 SLNPRMtVGDIIAEPL--RIHGLASKAERR------ERVaellELVGLRPEHADRypheFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 171 ILADEPVASLDpptshV--------VMRDLQRinaELGITVVVNLHflDLA 213
Cdd:COG4608 179 IVCDEPVSALD-----VsiqaqvlnLLEDLQD---ELGLTYLFISH--DLS 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-245 |
2.18e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSgdgIAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDraVN-TLSS 75
Cdd:PRK13637 1 MS---IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDiTDKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 76 RGLRDLRGDIGMIFQ--GFNLAKRTsVLNNVMMGrlhssPMWRTLlgawsaEDTELGMQALERVEIVGKAYE--KASS-- 149
Cdd:PRK13637 76 VKLSDIRKKVGLVFQypEYQLFEET-IEKDIAFG-----PINLGL------SEEEIENRVKRAMNIVGLDYEdyKDKSpf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 -LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:PRK13637 144 eLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
250
....*....|....*..
gi 1561673794 229 VFDGHGRDadeaVFESI 245
Cdd:PRK13637 224 ELQGTPRE----VFKEV 236
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-232 |
2.37e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 109.40 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDIGMIFQGFNL-A 95
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV----VREPRKVRRSIGIVPQYASVdE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGRLHSSPMWRTllgawSAEDTELgmqaLERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEA-----EERAEEL----LELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 176 PVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALK-EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
17-229 |
2.55e-28 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 110.51 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrGLRDLrgdiGMIFQGFNLAK 96
Cdd:TIGR03265 15 GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPP-QKRDY----GIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVLNNVMMGrLHSSPMWRtllgawsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:TIGR03265 90 NLTVADNIAYG-LKNRGMGR-------AEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 177 VASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-236 |
2.68e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.81 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlRGDI 85
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMG-RLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGlRMQKTP---------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-232 |
2.86e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 113.04 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrDLRGD 84
Cdd:TIGR03375 464 IEFRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPA---DLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IG------MIFQGfnlakrtSVLNNVMMGRLHsspmwrtllgawsAEDTELgMQALER------VEIVGKAY-----EKA 147
Cdd:TIGR03375 541 IGyvpqdpRLFYG-------TLRDNIALGAPY-------------ADDEEI-LRAAELagvtefVRRHPDGLdmqigERG 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLH---FLDLArrygDRLIGLR 224
Cdd:TIGR03375 600 RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHrtsLLDLV----DRIIVMD 673
|
....*...
gi 1561673794 225 DGKVVFDG 232
Cdd:TIGR03375 674 NGRIVADG 681
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
18-228 |
3.83e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.20 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtlSSRGLRDL---RGDIGMIFQGFNL 94
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLppeKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNVMMGrlhsspMWRTllgawSAEDTELGMQALERVEIVGKAYEK-ASSLSGGQQQRVAIARALAQQPRVILA 173
Cdd:TIGR02142 87 FPHLSVRGNLRYG------MKRA-----RPSERRISFERVIELLGIGHLLGRlPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 174 DEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-232 |
4.94e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 106.93 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgdI 85
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTsVLNNVMMGRLhSSPMWRTLLGAWSAEDTELGMQALERVE-IVGkayEKASSLSGGQQQRVAIARAL 164
Cdd:cd03254 80 GVVLQDTFLFSGT-IMENIRLGRP-NATDEEVIEAAKEAGAHDFIMKLPNGYDtVLG---ENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDG 232
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-229 |
8.54e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.47 E-value: 8.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG--------HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRG 77
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGDIGMIFQ----GFNLAKRtsvlnnvmMGRLHSSPMwRTLLgawSAEDTELGMQALERVEIVGKAYEKAS----S 149
Cdd:PRK10419 84 RKAFRRDIQMVFQdsisAVNPRKT--------VREIIREPL-RHLL---SLDKAERLARASEMLRAVDLDDSVLDkrppQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-229 |
1.57e-27 |
|
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: 105.88 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgDRAVNTLSSRGLRDL---RGDIGMIFQGFNLAKRT 98
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP--------DSGKILLNGKDITNLppeKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVLNNVMMGrlhsspmwrtllgawsaedteLGMQALERVEIVGKAYE-------------KASSLSGGQQQRVAIARALA 165
Cdd:cd03299 87 TVYKNIAYG---------------------LKKRKVDKKEIERKVLEiaemlgidhllnrKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-229 |
2.73e-27 |
|
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: 109.77 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTY----------AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvPVTTGTVTVGDRAVNTLSSRGL 78
Cdd:COG4172 279 RDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 79 RDLRGDIGMIFQ---GfNLAKRTSVLNNVMMG-RLHSSPMWRtllgawsAEDTELGMQALERVEIVGKAYEK-ASSLSGG 153
Cdd:COG4172 358 RPLRRRMQVVFQdpfG-SLSPRMTVGQIIAEGlRVHGPGLSA-------AERRARVAEALEEVGLDPAARHRyPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-245 |
2.81e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS-SRGLR 79
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 DLRGDIGMIFQgF---NLAKRTsVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKAS-SLSGGQQ 155
Cdd:PRK13649 82 QIRKKVGLVFQ-FpesQLFEET-VLKDVAFGPQN--------FGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
250
....*....|
gi 1561673794 236 DadeaVFESI 245
Cdd:PRK13649 231 D----IFQDV 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-232 |
4.06e-27 |
|
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: 104.20 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHtALDGVTLDIPAGqMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDI 85
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNV-MMGRLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLdYIAWLKGIP---------SKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAElgITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-232 |
5.03e-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: 104.21 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGD 84
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTsVLNNVMMGRLHsspmwrtllgawsAEDTELgMQALER------VEIVGKAY-----EKASSLSGG 153
Cdd:cd03245 80 IGYVPQDVTLFYGT-LRDNITLGAPL-------------ADDERI-LRAAELagvtdfVNKHPNGLdlqigERGRGLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLH---FLDLArrygDRLIGLRDGKVVF 230
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHrpsLLDLV----DRIIVMDSGRIVA 218
|
..
gi 1561673794 231 DG 232
Cdd:cd03245 219 DG 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-229 |
6.40e-27 |
|
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: 108.62 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTV----GDRAVNTLSSRGLRDL 81
Cdd:COG4172 10 EDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGsilfDGQDLLGLSERELRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RG-DIGMIFQgfnlAKRTSvLNNVM-----MG---RLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAyEKASS--- 149
Cdd:COG4172 90 RGnRIAMIFQ----EPMTS-LNPLHtigkqIAevlRLH--------RGLSGAAARARALELLERVGIPDPE-RRLDAyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 -LSGGQQQRVAIARALAQQPRVILADEPVASLDpptshVV--------MRDLQRinaELGITVVVNLHFLDLARRYGDRL 220
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALD-----VTvqaqildlLKDLQR---ELGMALLLITHDLGVVRRFADRV 227
|
....*....
gi 1561673794 221 IGLRDGKVV 229
Cdd:COG4172 228 AVMRQGEIV 236
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
9-218 |
9.04e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.48 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTvtvgdRAVNTLSSRGLR--------- 79
Cdd:PRK14243 14 ENLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-----RVEGKVTFHGKNlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 DLRGDIGMIFQGFNLAKRtSVLNNVMMGrlhsspmwrTLLGAWSAEDTELGMQALERV----EIVGKAYEKASSLSGGQQ 155
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPK-SIYDNIAYG---------ARINGYKGDMDELVERSLRQAalwdEVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPptshVVMRDLQRINAELG--ITVVVNLHFLDLARRYGD 218
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDP----ISTLRIEELMHELKeqYTIIIVTHNMQQAARVSD 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-229 |
9.58e-27 |
|
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: 103.77 E-value: 9.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG--GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRG 83
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQG---FNlakrTSVLNNVmmgrlhsspmwrtLLGAWSAEDTELgMQALERVEI--------------VGkayEK 146
Cdd:cd03249 78 QIGLVSQEpvlFD----GTIAENI-------------RYGKPDATDEEV-EEAAKKANIhdfimslpdgydtlVG---ER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 147 ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRinAELGITVVVNLHFLdLARRYGDRLIGLRDG 226
Cdd:cd03249 137 GSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRL-STIRNADLIAVLQNG 213
|
...
gi 1561673794 227 KVV 229
Cdd:cd03249 214 QVV 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-232 |
1.23e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.74 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlssrglrDLRGDI 85
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVM-MGRLHSspMWRTLLGAWSAEdtelgmqALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVyLAQLKG--LKKEEARRRIDE-------WLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
18-229 |
1.24e-26 |
|
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: 105.95 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntLSSRGLRDL---RGDIGMIFQGFNL 94
Cdd:COG4148 12 GGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNVMMGrlhsspMWRTLLGAwSAEDTE-----LGMQAL-ERveivgkayeKASSLSGGQQQRVAIARALAQQP 168
Cdd:COG4148 89 FPHLSVRGNLLYG------RKRAPRAE-RRISFDevvelLGIGHLlDR---------RPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-221 |
1.57e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPvttgtvtvgdravnTLSSRGLRDLRGDIGMIFQGFNLAK 96
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR--------------PTSGTVRRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 R--TSVLNNVMMGRLHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:NF040873 69 SlpLTVRDLVAMGRWARRGLWRRL----TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1561673794 175 EPVASLDpPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLI 221
Cdd:NF040873 145 EPTTGLD-AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-223 |
1.86e-26 |
|
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: 107.37 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI 85
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 G---MIFQGfnlakrtSVLNNVMMGRLHSSP--MWRTLLGAWSAEDTELGMQALERVeiVGkayEKASSLSGGQQQRVAI 160
Cdd:TIGR02857 402 PqhpFLFAG-------TIAENIRLARPDASDaeIREALERAGLDEFVAALPQGLDTP--IG---EGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYgDRLIGL 223
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-232 |
1.97e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 103.08 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIR-------------TINGlvpvttgtvtvGD-RAVn 71
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRllfrfydvssgsiLIDG-----------QDiREV- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 72 TLSSrglrdLRGDIGMIFQG---FNlakrTSVLNNVMMGRLHSSPmwrtllgawsaEDTELGMQAL---ERVEIVGKAY- 144
Cdd:cd03253 69 TLDS-----LRRAIGVVPQDtvlFN----DTIGYNIRYGRPDATD-----------EEVIEAAKAAqihDKIMRFPDGYd 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 145 ----EKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGDRL 220
Cdd:cd03253 129 tivgERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKI 205
|
250
....*....|..
gi 1561673794 221 IGLRDGKVVFDG 232
Cdd:cd03253 206 IVLKDGRIVERG 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-232 |
2.68e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.93 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDgIAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAV--NTLSS 75
Cdd:PRK13645 4 SKD-IILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 76 RGLRDLRGDIGMIFQ--GFNLAKRTsVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIvGKAYEKAS--SLS 151
Cdd:PRK13645 83 KEVKRLRKEIGLVFQfpEYQLFQET-IEKDIAFGPVN--------LGENKQEAYKKVPELLKLVQL-PEDYVKRSpfELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 152 GGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFD 231
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
.
gi 1561673794 232 G 232
Cdd:PRK13645 233 G 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-232 |
3.08e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.65 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravntlssrglrdLRGDIGMI 88
Cdd:COG4152 5 KGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-------------------------LAPDSGEV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 -FQGFNLA-----------------KRTSVLNNVM-MGRLHsspmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASS 149
Cdd:COG4152 59 lWDGEPLDpedrrrigylpeerglyPKMKVGEQLVyLARLK---------GLSKAEAKRRADEWLERLGLGDRANKKVEE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
...
gi 1561673794 230 FDG 232
Cdd:COG4152 209 LSG 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-232 |
4.40e-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: 101.92 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGD 84
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQG---FNlakrTSVLNNVMMGRlHSSPMWRTLLGAWSAEDTELGMQALERVE-IVGkayEKASSLSGGQQQRVAI 160
Cdd:cd03251 78 IGLVSQDvflFN----DTVAENIAYGR-PGATREEVEEAARAANAHEFIMELPEGYDtVIG---ERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDG 232
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-247 |
4.62e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.56 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAGgHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDl 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPG-RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 rgDIGMIFQGFNLAKRTSVLNNVMMGRLHsspmWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIA 161
Cdd:PRK10575 86 --KVAYLPQQLPAAEGMTVRELVAIGRYP----WHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEA- 240
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGe 239
|
....*..
gi 1561673794 241 VFESIYG 247
Cdd:PRK10575 240 TLEQIYG 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
6.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 6.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGL------------------VPVTTGTVTVGDRAVNTLSSRGLR-- 79
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkKKTKEKEKVLEKLVIQKTRFKKIKki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 -DLRGDIGMIFQ--GFNLAKRTsVLNNVMMGRLHsspmwrtlLGAWSAEDTELgmqALERVEIVG--KAYEKAS--SLSG 152
Cdd:PRK13651 101 kEIRRRVGVVFQfaEYQLFEQT-IEKDIIFGPVS--------MGVSKEEAKKR---AAKYIELVGldESYLQRSpfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 153 GQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-210 |
7.60e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 102.27 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLrd 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 lrgdIGMIFQGFNLAKRTSVL--NNVMMGRLHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRV 158
Cdd:PRK15056 80 ----VAYVPQSEEVDWSFPVLveDVVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFL 210
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNL 202
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-232 |
8.62e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 103.34 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 37 VVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrglrDLRGdIGMIFQGFNLAKRTSVLNNVMMG-RLHSSPmw 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP----HLRH-INMVFQSYALFPHMTVEENVAFGlKMRKVP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 116 rtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRI 195
Cdd:TIGR01187 74 -------RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1561673794 196 NAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:TIGR01187 147 QEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-229 |
1.88e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.57 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 26 TLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLR-GDIGMIFQGFNLAKRTSVLNNV 104
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 105 MMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPT 184
Cdd:PRK10070 128 AFGM--------ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561673794 185 SHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-229 |
1.92e-25 |
|
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: 99.64 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRavntlsSRGLRDLRGDIGMI 88
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQ--GFNLAkRTSVLNNVMMGrlhsspmwrTLLGAWSAEDTElgmQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:cd03226 77 MQdvDYQLF-TDSVREELLLG---------LKELDAGNEQAE---TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 167 QPRVILADEPVASLDPPTshvvMR---DLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKN----MErvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-232 |
1.95e-25 |
|
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: 99.75 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDIGMIFQGFNLAK 96
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVLNNV-MMGRLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:cd03265 87 ELTGWENLyIHARLYGVP---------GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 176 PVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-236 |
2.13e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.39 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAV-NTLSSRGLRD 80
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQgFNLAK--RTSVLNNVMMGRLH--------SSPMWRTLLgawsaedtELGmqaLERvEIVGKAyekASSL 150
Cdd:PRK13646 83 VRKRIGMVFQ-FPESQlfEDTVEREIIFGPKNfkmnldevKNYAHRLLM--------DLG---FSR-DVMSQS---PFQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVF 230
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
....*.
gi 1561673794 231 DGHGRD 236
Cdd:PRK13646 227 QTSPKE 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-241 |
3.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG----GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS-SRGLRD 80
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQgFNLAK--RTSVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKAS-SLSGGQQQR 157
Cdd:PRK13643 82 VRKKVGVVFQ-FPESQlfEETVLKDVAFGPQN--------FGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDA 237
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
....
gi 1561673794 238 DEAV 241
Cdd:PRK13643 232 FQEV 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-210 |
5.90e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.21 E-value: 5.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrglRDLRGD 84
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ---DEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKrTSVLNNVMMGRLHSSP--MWRTL----LGAWSAE-----DTELGmqalerveivgkayEKASSLSGG 153
Cdd:TIGR02868 411 VSVCAQDAHLFD-TTVRENLRLARPDATDeeLWAALervgLADWLRAlpdglDTVLG--------------EGGARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLqrINAELGITVVVNLHFL 210
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-229 |
8.51e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.08 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTIN---GLVPVTTGTVTVGDRAVNTLSSR-GLRDLRGDI 85
Cdd:PRK14239 10 DLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVTITGSIVYNGHNIYSPRtDTVDLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNlAKRTSVLNNVMMG-RLHSspmwrtllgawsAEDTELGMQALERV--------EIVGKAYEKASSLSGGQQQ 156
Cdd:PRK14239 89 GMVFQQPN-PFPMSIYENVVYGlRLKG------------IKDKQVLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVnlHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-233 |
9.11e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.55 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQGfNLAKrtsv 100
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQD-PLAS---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 101 LNNVM-MGRLHSSPMwRTLLGAWSAEDTElgmqalERVeivgKAYEKASSL------------SGGQQQRVAIARALAQQ 167
Cdd:PRK15079 111 LNPRMtIGEIIAEPL-RTYHPKLSRQEVK------DRV----KAMMLKVGLlpnlinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIglrdgkVVFDGH 233
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL------VMYLGH 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-232 |
1.40e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGgHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL---RGDIG 86
Cdd:PRK14271 26 NLTLGFAG-KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlefRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNlAKRTSVLNNVMMG-RLHSSPMWRTLLGAWSAEDTELGMQALERVEIVGKAYEkassLSGGQQQRVAIARALA 165
Cdd:PRK14271 105 MLFQRPN-PFPMSIMDNVLAGvRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR----LSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELgiTVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-228 |
1.54e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.93 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRG-DIGMIFQGFNLAKRT 98
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVLNNVMMGRLhsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVA 178
Cdd:PRK10584 104 NALENVELPAL--------LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1561673794 179 SLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYgDRLIGLRDGKV 228
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-240 |
4.61e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.49 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRgdI 85
Cdd:COG3845 6 LELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG--I 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRlhsspmwrtllgawsaEDTELGM----QALERVEIVGKAY-------EKASSLSGGQ 154
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGL----------------EPTKGGRldrkAARARIRELSERYgldvdpdAKVEDLSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 155 QQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHG 234
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
....*.
gi 1561673794 235 RDADEA 240
Cdd:COG3845 226 AETSEE 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-228 |
4.69e-24 |
|
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: 94.98 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrGLRDLRGD 84
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKrTSVLNNVmmgrlhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIARAL 164
Cdd:cd03246 78 VGYLPQDDELFS-GSIAENI---------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRyGDRLIGLRDGKV 228
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-257 |
5.41e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGG----HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS--SRGlrdlrG 83
Cdd:COG1101 6 NLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeyKRA-----K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQ----GfnLAKRTSVLNNVMMGRLHSSPmwRTLLGAWSAEDTELGMQALERVEIvG---KAYEKASSLSGGQQQ 156
Cdd:COG1101 81 YIGRVFQdpmmG--TAPSMTIEENLALAYRRGKR--RGLRRGLTKKRRELFRELLATLGL-GlenRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
250 260
....*....|....*....|.
gi 1561673794 237 AdeavfesiygRSLTAEDVLE 257
Cdd:COG1101 236 K----------KKLTVEDLLE 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-202 |
7.11e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRgLRdlrgD 84
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DR----D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMGrLHSSPMWRTLLG---AWSAEDTELGmQALERveivgkayeKASSLSGGQQQRVAIA 161
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEervAEAARILELE-PLLDR---------KPRELSGGQRQRVAMG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1561673794 162 RALAQQPRVILADEPVASLDPPTsHVVMR-DLQRINAELGIT 202
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKL-RVQMRlEIQRLHRRLKTT 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
17-229 |
8.70e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVnTLSSRGLRDlrgdIGMIFQGFNLAK 96
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRD----ICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:PRK11432 92 HMSLGENVGYGL--------KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 177 VASLDPPTSHVV---MRDLQRinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11432 164 LSNLDANLRRSMrekIRELQQ---QFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-245 |
3.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 95.06 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDravNTLSSRGLRDLRGD 84
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQG-FNLAKRTSVLNNVMMG----RLHSSPMWRTLLGAwsaeDTELGMQ-ALERveivgkayeKASSLSGGQQQRV 158
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDIAFGlenkKVPPKKMKDIIDDL----AKKVGMEdYLDK---------EPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVV---MRDLQRINAELGITVVVNLHFLDLArrygDRLIGLRDGKVVFDGHGR 235
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIkkiMVDLRKTRKKTLISITHDMDEAILA----DKVIVFSEGKLIAQGKPK 227
|
250
....*....|..
gi 1561673794 236 D--ADEAVFESI 245
Cdd:PRK13632 228 EilNNKEILEKA 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-229 |
4.16e-23 |
|
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: 97.95 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLV--PVTTGTVTVGDRAVNtLSSRGLrDLRGD----IGMIFQGFNL 94
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLepTSGEVNVRVGDEWVD-MTKPGP-DGRGRakryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNvmmgrlhsspmwrtLLGAWSAE-DTELG-MQALERVEIVGKAYEKASS--------LSGGQQQRVAIARAL 164
Cdd:TIGR03269 377 YPHRTVLDN--------------LTEAIGLElPDELArMKAVITLKMVGFDEEKAEEildkypdeLSEGERHRVALAQVL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-182 |
4.62e-23 |
|
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: 93.31 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtlssRGLRDLRGDI 85
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgrlhsspmWRTLLGAwsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRF--------WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170
....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDP 182
Cdd:COG4133 148 SPAPLWLLDEPFTALDA 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-233 |
4.66e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravntLSSRG--------LRD 80
Cdd:PRK11174 353 EDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-----------------LPYQGslkingieLRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 L-----RGDIGMIFQGFNLAKRTsVLNNVMMGRLHSSP--MWRTLLGAWSAEDTELGMQALERVeiVGkayEKASSLSGG 153
Cdd:PRK11174 416 LdpeswRKHLSWVGQNPQLPHGT-LRDNVLLGNPDASDeqLQQALENAWVSEFLPLLPQGLDTP--IG---DQAAGLSVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRinAELGITVVVNLHFLDLARRYgDRLIGLRDGKVVFDGH 233
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-236 |
5.66e-23 |
|
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: 97.48 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGD 84
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTsVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEI-VGkayEKASSLSGGQQQRVAIARA 163
Cdd:TIGR02203 408 VALVSQDVVLFNDT-IANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTpIG---ENGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGDRLIGLRDGKVVFDGHGRD 236
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNE 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-208 |
6.05e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.45 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQGFNLAK 96
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVLNNVMMG-RLHS---SPMWRTLLgawsaedtelgMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVIL 172
Cdd:PRK11831 98 DMNVFDNVAYPlREHTqlpAPLLHSTV-----------MMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1561673794 173 ADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLH 208
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSH 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-229 |
6.64e-23 |
|
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: 97.20 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIR-------------TINGlvpvttgtvtvGD- 67
Cdd:COG5265 354 GGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARllfrfydvtsgriLIDG-----------QDi 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 68 RAVnTLSSrglrdLRGDIGMIFQG---FNlakrTSVLNNVMMGRlhsspmwrtllgaWSAEDTELgMQALERVEI----- 139
Cdd:COG5265 423 RDV-TQAS-----LRAAIGIVPQDtvlFN----DTIAYNIAYGR-------------PDASEEEV-EAAARAAQIhdfie 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 140 ---------VGkayEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFL 210
Cdd:COG5265 479 slpdgydtrVG---ERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRL 553
|
250
....*....|....*....
gi 1561673794 211 DLARRyGDRLIGLRDGKVV 229
Cdd:COG5265 554 STIVD-ADEILVLEAGRIV 571
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-232 |
7.09e-23 |
|
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: 92.67 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravntlssrglrdLRGDIGMI- 88
Cdd:cd03268 5 DLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL-------------------------IKPDSGEIt 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNvmMGRLHSSPmwrTLLGAWSAED------TELG------MQALERVEIVGKAYEKASSLSGGQQQ 156
Cdd:cd03268 59 FDGKSYQKNIEALRR--IGALIEAP---GFYPNLTAREnlrllaRLLGirkkriDEVLDVVGLKDSAKKKVKGFSLGMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHvVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIK-ELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-208 |
1.20e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.10 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTL--SSRGlrdlrgdIGM 87
Cdd:PRK11000 8 NVTKAYGDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVppAERG-------VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQ 167
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGL--------KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1561673794 168 PRVILADEPVASLDPPTsHVVMR-DLQRINAELGITVVVNLH 208
Cdd:PRK11000 152 PSVFLLDEPLSNLDAAL-RVQMRiEISRLHKRLGRTMIYVTH 192
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-181 |
1.38e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrglrdlrgDI 85
Cdd:COG4525 7 RHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA--------DR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGL--------RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170
....*....|....*.
gi 1561673794 166 QQPRVILADEPVASLD 181
Cdd:COG4525 151 ADPRFLLMDEPFGALD 166
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-232 |
1.99e-22 |
|
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: 92.05 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 7 AFDNVSVTYAgghtALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRDLRGDIG 86
Cdd:cd03266 10 RFRDVKKTVQ----AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVM-MGRLHSSPmwrtllgawsaedtelGMQALERVEIVGKAYE-------KASSLSGGQQQRV 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEyFAGLYGLK----------------GDELTARLEELADRLGmeelldrRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 159 AIARALAQQPRVILADEPVASLDpPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-229 |
2.05e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.56 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgDRAVNTLSSRGLRDLRGD---------IGMI 88
Cdd:PRK11144 11 GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRP--------QKGRIVLNGRVLFDAEKGiclppekrrIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGrlhsspMWRTLLGAWSAEDTELGMQA-LERVEIvgkayekasSLSGGQQQRVAIARALAQQ 167
Cdd:PRK11144 82 FQDARLFPHYKVRGNLRYG------MAKSMVAQFDKIVALLGIEPlLDRYPG---------SLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11144 147 PELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-232 |
2.62e-22 |
|
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: 91.41 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlssrGLRDLRGDIGMI 88
Cdd:cd03263 5 NLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVM-MGRLHSSPmwrtllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQ 167
Cdd:cd03263 81 PQFDALFDELTVREHLRfYARLKGLP---------KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAELgiTVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-236 |
3.27e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLR 79
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 DLRGDIGMIFQG-FNLAKRTSVLNNVMMGrLHSSPMWRTllgawsaEDTELGMQALERVEIVGKAYEKASSLSGGQQQRV 158
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRP-------EMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLArRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-208 |
5.30e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVG----------DRAVNtls 74
Cdd:PRK14258 7 AIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqniyERRVN--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 75 srgLRDLRGDIGMIFQGFNLAKrTSVLNNVMMG-RLHSspmWRTLLGAWSAEDTELGMQALERvEIVGKAYEKASSLSGG 153
Cdd:PRK14258 83 ---LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGvKIVG---WRPKLEIDDIVESALKDADLWD-EIKHKIHKSALDLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQ--RINAELGITVVV-NLH 208
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVShNLH 212
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
20-229 |
6.21e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.44 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlSSRGLRDLRgdIGMIFQGFNlakrTS 99
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYKYRCKH--IRMIFQDPN----TS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 vLN-NVMMGRLHSSPMWR-TLLGAwsAEDTELGMQALERVEIVGK-AYEKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:COG4167 100 -LNpRLNIGQILEEPLRLnTDLTA--EEREERIFATLRLVGLLPEhANFYPHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 177 VASLDPPT-SHVV--MRDLQRinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4167 177 LAALDMSVrSQIInlMLELQE---KLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-226 |
8.79e-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: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTvgdravntLSSRGLRDLRGDIGMIFQGFNLAKRTSVL 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI--------LEGKQITEPGPDRMVVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 NNVMMGrlhsspMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:TIGR01184 73 ENIALA------VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561673794 182 PPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDG 226
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
1.47e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.45 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGD----------RAVNTLSSRGLRD---LRGDIG 86
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKIKNfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQ--GFNLAKRTsVLNNVMMGRLHsspmwrtlLGAWSAEDTELGMQALERVEIvGKAYEKAS--SLSGGQQQRVAIAR 162
Cdd:PRK13631 120 MVFQfpEYQLFKDT-IEKDIMFGPVA--------LGVKKSEAKKLAKFYLNKMGL-DDSYLERSpfGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-232 |
4.06e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlsSRGLRD 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAKRTSVLNNVMM-GRLHsspmwrtllgAWSAEDTELGMQAL-ERVEIVGKAYEKASSLSGGQQQRV 158
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLVfGRYF----------GMSTREIEAVIPSLlEFARLESKADARVSDLSGGMKRRL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAeLGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-244 |
4.42e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTaLDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGD-----RAVNTLSSRGLRdLRGD 84
Cdd:PRK14267 9 NLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlfgRNIYSPDVDPIE-VRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMG-RLHSspmwrtlLGAWSAEDTELGMQALERV----EIVGKAYEKASSLSGGQQQRVA 159
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAIGvKLNG-------LVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELgiTVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDade 239
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK--- 234
|
....*
gi 1561673794 240 aVFES 244
Cdd:PRK14267 235 -VFEN 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-241 |
6.66e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglRDLRGDI 85
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSspmwrtllgawsaeDTELGMQALERV-EIVGKAYEK----ASSLSGGQQQRVAI 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFA--------------ERDQFQERIKWVyELFPRLHERriqrAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD--AD 238
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAllAN 227
|
...
gi 1561673794 239 EAV 241
Cdd:PRK11614 228 EAV 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-255 |
9.97e-21 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 88.35 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgdigmifQGFNLAKR 97
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLAAI--------DAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 98 TSVLNN-------------VMMGRLhssPMWRTLlGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK13547 85 RAVLPQaaqpafafsareiVLLGRY---PHARRA-GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 165 AQ---------QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGR 235
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|.
gi 1561673794 236 DA-DEAVFESIYGRSLTAEDV 255
Cdd:PRK13547 241 DVlTPAHIARCYGFAVRLVDA 261
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-232 |
1.37e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDgvtLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVT--VGDRAVNTLSSRglrdlrg 83
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD---LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlnGQDHTTTPPSRR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQGFNLAKRTSVLNNVMMGrLHssPMWRTllgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:PRK10771 72 PVSMLFQENNLFSHLTVAQNIGLG-LN--PGLKL-----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-232 |
1.44e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVgdRAVNTLSSRGLRDLRGDI 85
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGfnlaKRTSVLNNVMMGRLHSSPMWRTLLgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK13644 80 GIVFQN----PETQFVGRTVEEDLAFGPENLCLP---PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINaELGITVVVNLHFLDlARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-229 |
1.74e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.87 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQgfN----LAK 96
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQ--NpygsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVlnnvmmGRLHSSPMW-RTLLGAwsAEDTElgmQALERVEIVGKAYEKASS----LSGGQQQRVAIARALAQQPRVI 171
Cdd:PRK11308 108 RKKV------GQILEEPLLiNTSLSA--AERRE---KALAMMAKVGLRPEHYDRyphmFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 172 LADEPVASLDPPTSHVV---MRDLQRinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11308 177 VADEPVSALDVSVQAQVlnlMMDLQQ---ELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-208 |
1.91e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrglrdlrgDIGMI 88
Cdd:PRK11248 5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA--------ERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL--------QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLH 208
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-261 |
1.93e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrglRD 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAKRTSVLNNVMM-GRLhsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVA 159
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVfGRY---------FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 160 IARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADE 239
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
250 260
....*....|....*....|....*...
gi 1561673794 240 A-----VFEsIYGRSLTA-EDVLEAKAE 261
Cdd:PRK13537 228 SeigcdVIE-IYGPDPVAlRDELAPLAE 254
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-232 |
2.25e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 87.19 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTALDgVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGL------RDLRG 83
Cdd:TIGR02323 8 GLSKSYGGGKGCRD-VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLseaerrRLMRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQ------------GFNLAKRTSVLNNVMMGRLhsspmwRTLLGAWsaedtelgmqaLERVEI-VGKAYEKASSL 150
Cdd:TIGR02323 87 EWGFVHQnprdglrmrvsaGANIGERLMAIGARHYGNI------RATAQDW-----------LEEVEIdPTRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVF 230
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
..
gi 1561673794 231 DG 232
Cdd:TIGR02323 230 SG 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-232 |
3.43e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNtLSSRGLRDLRGDIGMIFQGFNLAKRTSVL 101
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 NNVMMGRLHSspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PRK13638 96 DSDIAFSLRN-------LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 182 PPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-232 |
3.80e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 85.30 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVT-----YAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVtvgDRAVNTlSSRGLRD 80
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSG---EVLING-RPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQgfnlakrtsvlNNVMMGRLhsspmwrtllgawSAEDTeLGMQALERveivgkayekasSLSGGQQQRVAI 160
Cdd:cd03213 80 FRKIIGYVPQ-----------DDILHPTL-------------TVRET-LMFAAKLR------------GLSGGERKRVSI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLH---------FldlarrygDRLIGLRDGKVVFD 231
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHqpsseifelF--------DKLLLLSQGRVIYF 193
|
.
gi 1561673794 232 G 232
Cdd:cd03213 194 G 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-241 |
3.80e-20 |
|
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: 89.09 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAV--------------- 70
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVAlcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 71 -------NTLSSRGL----------RDLRGDIGMIFQ-GFNLAKRTSVLNNVMMGrLHSspmwrtlLGAWSAEDTELGMQ 132
Cdd:TIGR03269 80 epcpvcgGTLEPEEVdfwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNVLEA-LEE-------IGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 133 ALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDL 212
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*....
gi 1561673794 213 ARRYGDRLIGLRDGKVVFDGhgrDADEAV 241
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEG---TPDEVV 257
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-229 |
4.26e-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: 85.62 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYA-GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrGLRDLRGD 84
Cdd:cd03244 3 IEFKNVSLRYRpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMI------FQG---FNLAkrtsvlnnvmmgrlhssPmwrtlLGAWSaeDTELgMQALERV---EIVGKAYEK------ 146
Cdd:cd03244 80 ISIIpqdpvlFSGtirSNLD-----------------P-----FGEYS--DEEL-WQALERVglkEFVESLPGGldtvve 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 147 --ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQriNAELGITVVVNLHFLDLARRYgDRLIGLR 224
Cdd:cd03244 135 egGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDS-DRILVLD 211
|
....*
gi 1561673794 225 DGKVV 229
Cdd:cd03244 212 KGRVV 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-236 |
7.77e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgDI 85
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--GI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSaEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWR-EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRD 236
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
6-228 |
1.04e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 84.53 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaggHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrdlRGDI 85
Cdd:TIGR01277 1 LALDKVRYEY---EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY-----QRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGrLHSSPmwrtllgAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:TIGR01277 73 SMLFQENNLFAHLTVRQNIGLG-LHPGL-------KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:TIGR01277 145 RPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-228 |
4.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAvntLSSRGLRDLRGDIGMIFQG-FNLAKRTSV 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 101 LNNVMMGrLHSSPMWRTLLGAWSAEDTEL-GMQALERVEivgkayekASSLSGGQQQRVAIARALAQQPRVILADEPVAS 179
Cdd:PRK13650 100 EDDVAFG-LENKGIPHEEMKERVNEALELvGMQDFKERE--------PARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1561673794 180 LDPPTSHVVMRDLQRINAELGITVVVNLHFLDLArRYGDRLIGLRDGKV 228
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-229 |
4.15e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 85.66 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHtALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVtvgdravnTLSSRGLRDL---RGDIG 86
Cdd:PRK11607 24 NLTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI--------MLDGVDLSHVppyQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMGrLHSSPMWRtllgawsAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG-LKQDKLPK-------AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-204 |
4.30e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 3 GDGIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPvttgtvtvgdravntlSSRGLRDLR 82
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP----------------YGSGRIARP 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFqgfnLAKRTSVLnnvmMGRLhsspmwRTLL----GAWSAEDTELgMQALERV---EIVGKAYEKAS---SLSG 152
Cdd:COG4178 424 AGARVLF----LPQRPYLP----LGTL------REALlypaTAEAFSDAEL-REALEAVglgHLAERLDEEADwdqVLSL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 153 GQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMrdlQRINAEL-GITVV 204
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY---QLLREELpGTTVI 538
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-229 |
5.63e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 7 AFDNVSVTYAGGHtALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGlrDLRGDIG 86
Cdd:PRK11288 6 SFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMGRLHSSPMW--RTLLGAWSAEdtelgmqALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLPHKGGIvnRRLLNYEARE-------QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-257 |
6.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRavnTLSSRGLRDLRGDIGMIFQGFNlakrtsvl 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQNPD-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 nnvmmgrlhsspmwRTLLGAWSAEDTELGM--QALERVEIVGKAYE-------------KASSLSGGQQQRVAIARALAQ 166
Cdd:PRK13642 92 --------------NQFVGATVEDDVAFGMenQGIPREEMIKRVDEallavnmldfktrEPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDGKVVfdghgrdaDEAVFESIY 246
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII--------KEAAPSELF 228
|
250
....*....|.
gi 1561673794 247 GrslTAEDVLE 257
Cdd:PRK13642 229 A---TSEDMVE 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
10-232 |
6.89e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 6.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlSSRGLRDLRGDIGMIF 89
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QG-----FNlakrTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQAL-ERVeivgkayekASSLSGGQQQRVAIARA 163
Cdd:PRK13652 85 QNpddqiFS----PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELrDRV---------PHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-252 |
7.37e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQG--FNLAKRT 98
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVLNNVMMG-RLHsspmwRTLLGAWSAEDTElgmQALERVEIVGK-AYEKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:PRK10261 419 TVGDSIMEPlRVH-----GLLPGKAAAARVA---WLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 177 VASLDPPTSHVV---MRDLQRinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRdadeAVFES---IYGRSL 250
Cdd:PRK10261 491 VSALDVSIRGQIinlLLDLQR---DFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR----AVFENpqhPYTRKL 563
|
..
gi 1561673794 251 TA 252
Cdd:PRK10261 564 MA 565
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-229 |
7.74e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.05 E-value: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHtALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTT-----GTVTVGDRAVNTLSSRGLRDL-R 82
Cdd:PRK11701 10 RGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgevhyRMRDGQLRDLYALSEAERRRLlR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGMIFQ------------GFNLAKRTSVLNNVMMGRLhsspmwRTLLGAWsaedtelgmqaLERVEI-VGKAYEKASS 149
Cdd:PRK11701 89 TEWGFVHQhprdglrmqvsaGGNIGERLMAVGARHYGDI------RATAGDW-----------LERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-229 |
8.46e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.17 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 15 YAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAV----NTLSSRGLRdLRGDIGMIFQ 90
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkDIFQIDAIK-LRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 91 GFNLAKRTSVLNNVMMG-RLHSSPMWRtllgawsaEDTELGMQALERVEIVGKAYEK----ASSLSGGQQQRVAIARALA 165
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPlKSHGIKEKR--------EIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVnlHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS--HNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-241 |
9.09e-19 |
|
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: 82.21 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGlRDLRGdIGMI 88
Cdd:cd03218 4 ENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLG-IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMMGRlhsspmwrTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:cd03218 81 PQEASIFRKLTVEENILAVL--------EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 169 RVILADEPVASLDPptshVVMRDLQRINAEL---GITVVVNLH----FLDLArrygDRLIGLRDGKVVFDGHGRD--ADE 239
Cdd:cd03218 153 KFLLLDEPFAGVDP----IAVQDIQKIIKILkdrGIGVLITDHnvreTLSIT----DRAYIIYEGKVLAEGTPEEiaANE 224
|
..
gi 1561673794 240 AV 241
Cdd:cd03218 225 LV 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-210 |
1.19e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.15 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSGDGIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRD 80
Cdd:PRK10790 336 LQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 lrgDIGMIFQG-FNLAKrtSVLNNVMMGR-LHSSPMWrtllgawsaedtelgmQALERVEIVGKAY-----------EKA 147
Cdd:PRK10790 416 ---GVAMVQQDpVVLAD--TFLANVTLGRdISEEQVW----------------QALETVQLAELARslpdglytplgEQG 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElgITVVVNLHFL 210
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRL 535
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-226 |
1.29e-18 |
|
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: 81.71 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTING--LVPVTTGTVTVGDRAVN--TLSSRGLRDLR-GDIGMIFQGFNLA 95
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGSILVRHDGGWVDlaQASPREILALRrRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMmgrlhsspmwRTLLgawsaedtELGMQALErveivgkAYEKASSL------------------SGGQQQR 157
Cdd:COG4778 106 PRVSALDVVA----------EPLL--------ERGVDREE-------ARARARELlarlnlperlwdlppatfSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDG 226
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-227 |
1.57e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGdRAVNTLSSRGLRDL-RGDIGMIFQGFNLA 95
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEII-FEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGRlHSSPMWRTLLGAWSAEDTELgmqaLERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:PRK13549 95 KELSVLENIFLGN-EITPGGIMDYDAMYLRAQKL----LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 176 PVASL-DPPTSHV--VMRDLQRinaeLGITVVVNLHFLDLARRYGDRLIGLRDGK 227
Cdd:PRK13549 170 PTASLtESETAVLldIIRDLKA----HGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-227 |
2.09e-18 |
|
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: 80.59 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT----ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravNTLSSRGLRDL 81
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG----------------ELEKLSGSVSV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQG---FNlakrTSVLNNVMMGRLHSSPMWRTLLGAWSAE-DTELgMQALERVEIvGkayEKASSLSGGQQQR 157
Cdd:cd03250 65 PGSIAYVSQEpwiQN----GTIRENILFGKPFDEERYEKVIKACALEpDLEI-LPDGDLTEI-G---EKGINLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVV---NLHFLDLArrygDRLIGLRDGK 227
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILvthQLQLLPHA----DQIVVLDNGR 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-181 |
3.40e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgdiGMI 88
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL----GVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 F-----QGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSA--EDTElgmQALERVEIVGKAYE-KASSLSGGQQQRVAI 160
Cdd:COG3845 337 YipedrLGRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAirAFAE---ELIEEFDVRTPGPDtPARSLSGGNQQKVIL 413
|
170 180
....*....|....*....|.
gi 1561673794 161 ARALAQQPRVILADEPVASLD 181
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-233 |
6.81e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIR-------------TINGLvpvttgtvtvgdravnT 72
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINllqrvfdpqsgriLIDGT----------------D 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 73 LSSRGLRDLRGDIGMIFQGFNLAKRtSVLNNVMMGRLhsspmwrtllgawSAEDTELgMQALERVE-------------- 138
Cdd:PRK13657 399 IRTVTRASLRRNIAVVFQDAGLFNR-SIEDNIRVGRP-------------DATDEEM-RAAAERAQahdfierkpdgydt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 139 IVGkayEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRyGD 218
Cdd:PRK13657 464 VVG---ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-AD 537
|
250
....*....|....*
gi 1561673794 219 RLIGLRDGKVVFDGH 233
Cdd:PRK13657 538 RILVFDNGRVVESGS 552
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-252 |
7.31e-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: 82.57 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGdRAVNTLSSRGLRDL-RGDIGMIFQGFNLA 95
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIY-WSGSPLKASNIRDTeRAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELgMQALeRVEIVGKAyEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPGGRMAYNAMYLRAKNL-LREL-QLDADNVT-RPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 176 PVASLDPPTSHV---VMRDLQRinaeLGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEA-VFESIYGRSLT 251
Cdd:TIGR02633 168 PSSSLTEKETEIlldIIRDLKA----HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDdIITMMVGREIT 243
|
.
gi 1561673794 252 A 252
Cdd:TIGR02633 244 S 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-184 |
1.20e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtVGDRAVNT-----LSSRGLR 79
Cdd:COG4136 1 MLSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG----------TLSPAFSAsgevlLNGRRLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 DL----RGdIGMIFQGFNLAKRTSVLNNVMMGrlhsspMWRTLLGAwsaEDTELGMQALERVEIVGKAYEKASSLSGGQQ 155
Cdd:COG4136 70 ALpaeqRR-IGILFQDDLLFPHLSVGENLAFA------LPPTIGRA---QRRARVEQALEEAGLAGFADRDPATLSGGQR 139
|
170 180
....*....|....*....|....*....
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPT 184
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-176 |
1.49e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPvttgtvtvgdravntlSSRGLRDLRGD--I 85
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE----------------PDSGEVSIPKGlrI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTL--------------------------LGAWSAEdTELGmQALERVEI 139
Cdd:COG0488 64 GYLPQEPPLDDDLTVLDTVLDGDAELRALEAELeeleaklaepdedlerlaelqeefeaLGGWEAE-ARAE-EILSGLGF 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 1561673794 140 VGKAYEKA-SSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-229 |
1.82e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG---HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGD-----RAVNTLSSRG 77
Cdd:PRK15134 6 LAIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDirfhgESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGD-IGMIFQG--------FNLAKRTS-VLNnvmmgrLHSSpMWRtllgawSAEDTELgMQALERVEIVGKAYEKA 147
Cdd:PRK15134 86 LRGVRGNkIAMIFQEpmvslnplHTLEKQLYeVLS------LHRG-MRR------EAARGEI-LNCLDRVGIRQAAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 148 S---SLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLR 224
Cdd:PRK15134 152 DyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
....*
gi 1561673794 225 DGKVV 229
Cdd:PRK15134 232 NGRCV 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-181 |
2.53e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgDRAVNTLSSRGLRD---- 80
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI--------DEGEILLDGHDLRDytla 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 -LRGDIGMIFQGFNLAKRTsVLNNVMMGRLhsspmwrtllGAWSAEDTE------LGMQALERVE-----IVGkayEKAS 148
Cdd:PRK11176 414 sLRNQVALVSQNVHLFNDT-IANNIAYART----------EQYSREQIEeaarmaYAMDFINKMDngldtVIG---ENGV 479
|
170 180 190
....*....|....*....|....*....|...
gi 1561673794 149 SLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-234 |
4.57e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 19 HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVgDRAVNTLSSRglRDLRGDIGMIfQGFNLAKRt 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-DVPDNQFGRE--ASLIDAIGRK-GDFKDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 sVLNNVmmgRLHSSPMWRTllgawsaedtelgmqalerveivgkayeKASSLSGGQQQRVAIARALAQQPRVILADEPVA 178
Cdd:COG2401 118 -LLNAV---GLSDAVLWLR----------------------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 179 SLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARrygdrliGLRDGKVVFDGHG 234
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYDVID-------DLQPDLLIFVGYG 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-232 |
5.75e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 5.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgdiGMI--FQGFNL 94
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM----GVVrtFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNVMMGR-----------LHSSPMWRTLlgawSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:PRK11300 92 FREMTVIENLLVAQhqqlktglfsgLLKTPAFRRA----ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHvvmrDLQRINAEL----GITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETK----ELDELIAELrnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-232 |
7.51e-17 |
|
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: 77.37 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRdlrgDIGMIFQG-----FNL 94
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR----RIGVVFGQktqlwWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNVMMGRLHSSPMWRTLlgawsAEDTELgmqaLERVEIVgkaYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRL-----DELSEL----LDLEELL---DTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 175 EPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-228 |
9.02e-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: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG--GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrg 83
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 dIGMIFQGFNLAKRtSVLNNVMMGrLHSSPMWRTLLGAWSAE-DTELGMQALERVEIVGkayEKASSLSGGQQQRVAIAR 162
Cdd:cd03248 90 -VSLVGQEPVLFAR-SLQDNIAYG-LQSCSFECVKEAAQKAHaHSFISELASGYDTEVG---EKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELgiTVVVNLHFLDLARRyGDRLIGLRDGKV 228
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-232 |
9.20e-17 |
|
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: 75.81 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG-GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTInglvpvttgtvtvgdravntlssrgLRDLRGD 84
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL-------------------------TGDLKPQ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMI-FQGFNLAKRTSVLNNvMMGRLHSSP-MWRTLLGawsaedTELGMQalerveivgkayekassLSGGQQQRVAIAR 162
Cdd:cd03247 56 QGEItLDGVPVSDLEKALSS-LISVLNQRPyLFDTTLR------NNLGRR-----------------FSGGERQRLALAR 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLqrINAELGITVVVNLHFLdLARRYGDRLIGLRDGKVVFDG 232
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-232 |
1.03e-16 |
|
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: 79.02 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTA-LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRG- 83
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 ---DIGmIFQG--------FNLAKRTSVLNNVMMGRLHSspMWRTL-LGAwsaeDTELGmqalerveivgkayEKASSLS 151
Cdd:COG4618 411 lpqDVE-LFDGtiaeniarFGDADPEKVVAAAKLAGVHE--MILRLpDGY----DTRIG--------------EGGARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 152 GGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLH---FLDLArrygDRLIGLRDGKV 228
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHrpsLLAAV----DKLLVLRDGRV 544
|
....
gi 1561673794 229 VFDG 232
Cdd:COG4618 545 QAFG 548
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-229 |
1.72e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVG----DRAVNTLSSRGLRDLRG-DIGMIFQgfnla 95
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmrfdDIDLLRLSPRERRKLVGhNVSMIFQ----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLN-NVMMGR--LHSSPMWrTLLGAWSAEDTELGMQALERVEIVG-KAYEKASS-----LSGGQQQRVAIARALAQ 166
Cdd:PRK15093 97 EPQSCLDpSERVGRqlMQNIPGW-TYKGRWWQRFGWRKRRAIELLHRVGiKDHKDAMRsfpyeLTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 167 QPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-232 |
3.89e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKST----LIRTINglvpvTTGTVTVGDRAVNTLSSRGLRDLRGDIGMIFQGF 92
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 93 N--LAKRTSVLNNVMMG-RLHsspmwRTLLGAwsAEDTELGMQALERVEIVGKA-YEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGlRVH-----QPTLSA--AQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-247 |
7.03e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 7.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVgDRAVNTLSSRGLRDLRGdigmifqgfNLAKRTSVL 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLN-GRPLSDWSAAELARHRA---------YLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 nnVMMG-----RLHSSPmwrtllGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQ-------QPR 169
Cdd:COG4138 82 --FAMPvfqylALHQPA------GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 170 VILADEPVASLDppTSHVVMRD--LQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDA-DEAVFESIY 246
Cdd:COG4138 154 LLLLDEPMNSLD--VAQQAALDrlLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVmTPENLSEVF 230
|
.
gi 1561673794 247 G 247
Cdd:COG4138 231 G 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-182 |
1.13e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrglRDLRGDiGMIFQGF--NL 94
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHE-NILYLGHlpGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 95 AKRTSVLNNvmmgrLHsspMWRTLLGAwsaEDTELgMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:TIGR01189 85 KPELSALEN-----LH---FWAAIHGG---AQRTI-EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*...
gi 1561673794 175 EPVASLDP 182
Cdd:TIGR01189 153 EPTTALDK 160
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-250 |
2.29e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 18 GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDlrGDIGMIFQGFNLAKR 97
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 98 TSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELgmqaLERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPV 177
Cdd:PRK10762 94 LTIAENIFLGREFVNRFGRIDWKKMYAEADKL----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 178 ASL-DPPTSHV--VMRDLQrinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADE-AVFESIYGRSL 250
Cdd:PRK10762 170 DALtDTETESLfrVIRELK----SQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEdSLIEMMVGRKL 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-232 |
3.88e-15 |
|
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: 72.30 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgDRAVNTLSSRGL-------RDL-RGDIGMIFQGFN 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-----------VEGGGTTSGQILfngqprkPDQfQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 LAKRTSV-----LNNVMMGRLHSSPMWRTLLgawsAEDTELGMQALERVeivgkAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:cd03234 92 LLPGLTVretltYTAILRLPRKSSDAIRKKR----VEDVLLRDLALTRI-----GGNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLH--FLDLARRYgDRLIGLRDGKVVFDG 232
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIHqpRSDLFRLF-DRILLLSSGEIVYSG 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-233 |
5.93e-15 |
|
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: 71.29 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrGLRDLRGD 84
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLakrtsvlnnvMMGRLhsspmwRTLLGAWSAEDTELGMQALerveivgKAYEKASSLSGGQQQRVAIARAL 164
Cdd:cd03369 84 LTIIPQDPTL----------FSGTI------RSNLDPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVvmrdLQRINAEL--GITVVVNLHFLDLARRYgDRLIGLRDGKVVFDGH 233
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDAL----IQKTIREEftNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-236 |
7.36e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 73.92 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglrDLRGD 84
Cdd:TIGR01842 317 LSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE---TFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMGRLHSSpmwRTLLGAWSAE-------------DTELGmqalerveivgkayEKASSLS 151
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADP---EKIIEAAKLAgvhelilrlpdgyDTVIG--------------PGGATLS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 152 GGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLH---FLDLArrygDRLIGLRDGKV 228
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHrpsLLGCV----DKILVLQDGRI 531
|
....*...
gi 1561673794 229 VFDGHGRD 236
Cdd:TIGR01842 532 ARFGERDE 539
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
10-242 |
2.00e-14 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 70.12 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlssrglRDLRgDIGMIF 89
Cdd:TIGR03740 5 NLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR------KDLH-KIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFNLAKRTSVLNNVmmgRLHSspmwrTLLGAWSAEDTELgmqaLERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPR 169
Cdd:TIGR03740 77 ESPPLYENLTARENL---KVHT-----TLLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 170 VILADEPVASLDPPTSHvVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG--HGRDADEAVF 242
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQ-ELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGkiNKSENLEKLF 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-232 |
2.84e-14 |
|
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: 72.35 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDN-VSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlssrGLRDLRG 83
Cdd:TIGR01257 928 GVCVKNlVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQGFNLAKRTSVLNNVmmgrlhsspMWRTLLGAWSAEDTELGMQA-LERVEIVGKAYEKASSLSGGQQQRVAIAR 162
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHI---------LFYAQLKGRSWEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-204 |
2.94e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.72 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTtgtvtvgdravntlssrglrdlRGDI 85
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG----------------------SGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQgfnlakrtsvlNNVMM---------GRLHSSpmwrtLLGAWSAEdtelgmqalerveivgkayekassLSGGQQQ 156
Cdd:cd03223 59 GMPEG-----------EDLLFlpqrpylplGTLREQ-----LIYPWDDV------------------------LSGGEQQ 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQrinaELGITVV 204
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVI 142
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
3.15e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravntlssrglrDLRGDI 85
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-------------------------ELEPDS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQG--------------FNLAKrtSVLNNVM-----MGRLHSspmwRTLLGAW--SAEDtelgmqalerveivgkAY 144
Cdd:COG0488 370 GTVKLGetvkigyfdqhqeeLDPDK--TVLDELRdgapgGTEQEV----RGYLGRFlfSGDD----------------AF 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 145 EKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINaelGiTVVV---NLHFLDlarRYGDRLI 221
Cdd:COG0488 428 KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLvshDRYFLD---RVATRIL 500
|
250
....*....|..
gi 1561673794 222 GLRDGKVV-FDG 232
Cdd:COG0488 501 EFEDGGVReYPG 512
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-208 |
4.27e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGgHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGlRDLRGdIGMI 88
Cdd:PRK10895 7 KNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRG-IGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 89 FQGFNLAKRTSVLNNVMmgrlhSSPMWRTLLGAWSAEDTelGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK10895 84 PQEASIFRRLSVYDNLM-----AVLQIRDDLSAEQREDR--ANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1561673794 169 RVILADEPVASLDPptshVVMRDLQRINAEL---GITVVVNLH 208
Cdd:PRK10895 157 KFILLDEPFAGVDP----ISVIDIKRIIEHLrdsGLGVLITDH 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-181 |
6.03e-14 |
|
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: 68.67 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravntlssrgLRDLRGDIGMifQGFNLAK 96
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL----------------------SPPLAGRVLL--NGGPLDF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSVLNNVMMGRLHSSPMWRTL-----LGAWSAE-DTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRV 170
Cdd:cd03231 67 QRDSIARGLLYLGHAPGIKTTLsvlenLRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPL 146
|
170
....*....|.
gi 1561673794 171 ILADEPVASLD 181
Cdd:cd03231 147 WILDEPTTALD 157
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-205 |
6.52e-14 |
|
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: 67.84 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 11 VSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL--------R 82
Cdd:cd03215 5 LEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 GDIGmIFQGFnlakrtSVLNNVMMGRLhsspmwrtllgawsaedtelgmqalerveivgkayekassLSGGQQQRVAIAR 162
Cdd:cd03215 85 KREG-LVLDL------SVAENIALSSL----------------------------------------LSGGNQQKVVLAR 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTS---HVVMRDLqrinAELGITVVV 205
Cdd:cd03215 118 WLARDPRVLILDEPTRGVDVGAKaeiYRLIREL----ADAGKAVLL 159
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-232 |
7.37e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.91 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAG--GHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVtvgdravnTLSSRGLRD--- 80
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV--------LLDGVPLVQydh 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 --LRGDIGMIFQGFNLAKRtSVLNNVMMGrLHSSPMWRTLLGAWSAE------------DTELGmqalerveivgkayEK 146
Cdd:TIGR00958 551 hyLHRQVALVGQEPVLFSG-SVRENIAYG-LTDTPDEEIMAAAKAANahdfimefpngyDTEVG--------------EK 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 147 ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVvmrdLQRINAELGITVVVNLHFLDLARRyGDRLIGLRDG 226
Cdd:TIGR00958 615 GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL----LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKG 689
|
....*.
gi 1561673794 227 KVVFDG 232
Cdd:TIGR00958 690 SVVEMG 695
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-257 |
1.29e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttGTVTVGDRAVntlssrglrDLRGDIGMIFQG---FNlakrT 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG------ELSHAETSSV---------VIRGSVAYVPQVswiFN----A 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVLNNVMMG-RLHSSPMWRTLLGAWSAEDTELgMQALERVEIvgkaYEKASSLSGGQQQRVAIARALAQQPRVILADEPV 177
Cdd:PLN03232 694 TVRENILFGsDFESERYWRAIDVTALQHDLDL-LPGRDLTEI----GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 178 ASLDPPTSHVVMRDLQR--INAELGITVVVNLHFLDLArrygDRLIGLRDGKVvfdghgrdADEAVFESIYGRSLTAEDV 255
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKdeLKGKTRVLVTNQLHFLPLM----DRIILVSEGMI--------KEEGTFAELSKSGSLFKKL 836
|
..
gi 1561673794 256 LE 257
Cdd:PLN03232 837 ME 838
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-251 |
1.50e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGgHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRglRDLRGDIGMIF 89
Cdd:PRK10982 3 NISKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFNLAKRTSVLNNVMMGR-------LHSSPMWRtllgawsaeDTElgmQALERVEIVGKAYEKASSLSGGQQQRVAIAR 162
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRyptkgmfVDQDKMYR---------DTK---AIFDELDIDIDPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 163 ALAQQPRVILADEPVASL-DPPTSHV--VMRDLQrinaELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDAD- 238
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLtEKEVNHLftIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTm 223
|
250
....*....|...
gi 1561673794 239 EAVFESIYGRSLT 251
Cdd:PRK10982 224 DKIIAMMVGRSLT 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-233 |
1.97e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.47 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDlrgd 84
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ---- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 iGMIFqgfnLAKRTSVLNNVMMGRLhsspmwrtLLGAWSAEDTELgMQALERVEIvGKAYEKASSL-----------SGG 153
Cdd:PRK11160 415 -AISV----VSQRVHLFSATLRDNL--------LLAAPNASDEAL-IEVLQQVGL-EKLLEDDKGLnawlgeggrqlSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHfldlaRRYG----DRLIGLRDGKVV 229
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-----RLTGleqfDRICVMDNGQII 552
|
....
gi 1561673794 230 FDGH 233
Cdd:PRK11160 553 EQGT 556
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-253 |
2.52e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVnTLSSRGLRDLRgdIGMIFQGfnlaKRTSV 100
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQR--IRMIFQD----PSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 101 LNNVMMGRLHSSPMwrTLLGAWSAEDTELGM-QALERVEIV-GKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVA 178
Cdd:PRK15112 101 NPRQRISQILDFPL--RLNTDLEPEQREKQIiETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 179 SLDpptshVVMRDlQRINAEL------GITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHG--------RDADEAVFES 244
Cdd:PRK15112 179 SLD-----MSMRS-QLINLMLelqekqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTadvlasplHELTKRLIAG 252
|
....*....
gi 1561673794 245 IYGRSLTAE 253
Cdd:PRK15112 253 HFGEALTAD 261
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-187 |
4.76e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 3 GDGIAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtVGDRAvntlssRGLRDL 81
Cdd:TIGR00957 634 GNSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA----------EMDKV------EGHVHM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RGDIGMIFQGFNLaKRTSVLNNVMMGRLHSSPMWRTLLGAWSA-EDTELgMQALERVEIvgkaYEKASSLSGGQQQRVAI 160
Cdd:TIGR00957 698 KGSVAYVPQQAWI-QNDSLRENILFGKALNEKYYQQVLEACALlPDLEI-LPSGDRTEI----GEKGVNLSGGQKQRVSL 771
|
170 180
....*....|....*....|....*..
gi 1561673794 161 ARALAQQPRVILADEPVASLDpptSHV 187
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVD---AHV 795
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-229 |
4.83e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTvgDR----AVN--TLSSRGLRDLRG-DIGMIFQgfn 93
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTA--DRfrwnGIDllKLSPRERRKIIGrEIAMIFQ--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 laKRTSVLN-NVMMGR--LHSSPMWrTLLGAWSAEDTELGMQALERVEIVG-KAYEKASS-----LSGGQQQRVAIARAL 164
Cdd:COG4170 97 --EPSSCLDpSAKIGDqlIEAIPSW-TFKGKWWQRFKWRKKRAIELLHRVGiKDHKDIMNsypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 165 AQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-226 |
5.67e-13 |
|
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: 66.20 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 14 TYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDL-RGDIGMIFQGF 92
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 93 NLAKRTsVLNNVMMGRLHSSPMWRTLLGAWSAE-DTELgMQALERVEIvgkaYEKASSLSGGQQQRVAIARALAQQPRVI 171
Cdd:cd03290 89 WLLNAT-VEENITFGSPFNKQRYKAVTDACSLQpDIDL-LPFGDQTEI----GERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 172 LADEPVASLDPPTS-HVVMRDLQRINAELGITVVVNLHFLDLArRYGDRLIGLRDG 226
Cdd:cd03290 163 FLDDPFSALDIHLSdHLMQEGILKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-241 |
9.41e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 1 MSgDGIAFDNVSVTY---------------------AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvt 59
Cdd:COG1134 1 MS-SMIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 60 tgtvtvgdravnTLSSRGLRDLRG------DIGMIFQGfnlakRTSVLNNVMM-GRlhsspmwrtLLGAWSAEdtelgMQ 132
Cdd:COG1134 76 ------------LEPTSGRVEVNGrvsallELGAGFHP-----ELTGRENIYLnGR---------LLGLSRKE-----ID 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 133 ALERvEIV-----GKA-YEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVN 206
Cdd:COG1134 125 EKFD-EIVefaelGDFiDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|....*
gi 1561673794 207 lHFLDLARRYGDRLIGLRDGKVVFDGhgrDADEAV 241
Cdd:COG1134 204 -HSMGAVRRLCDRAIWLEKGRLVMDG---DPEEVI 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-261 |
1.68e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTtgtvtvgdravntlsSRGLRDLRGDIGMIFQG---FNlakrT 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPR---------------SDASVVIRGTVAYVPQVswiFN----A 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVLNNVMMGR-LHSSPMWRTLLGAWSAEDTELgMQALERVEIvgkaYEKASSLSGGQQQRVAIARALAQQPRVILADEPV 177
Cdd:PLN03130 694 TVRDNILFGSpFDPERYERAIDVTALQHDLDL-LPGGDLTEI----GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 178 ASLDpptSHVVMRDLQR-INAELG----ITVVVNLHFLDlarrYGDRLIGLRDGKVVFDGHGRD--ADEAVFESIYGRSL 250
Cdd:PLN03130 769 SALD---AHVGRQVFDKcIKDELRgktrVLVTNQLHFLS----QVDRIILVHEGMIKEEGTYEElsNNGPLFQKLMENAG 841
|
250
....*....|.
gi 1561673794 251 TAEDVLEAKAE 261
Cdd:PLN03130 842 KMEEYVEENGE 852
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-236 |
1.78e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYA---GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVG---DRAVNTLSSRGLRDLRG 83
Cdd:PRK09473 17 DLRVTFStpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSAtfnGREILNLPEKELNKLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 D-IGMIFQ----GFNLAKRTS-VLNNVMMgrLHSspmwrtllGAWSAEDTELGMQALERVEIvGKAYEKAS----SLSGG 153
Cdd:PRK09473 97 EqISMIFQdpmtSLNPYMRVGeQLMEVLM--LHK--------GMSKAEAFEESVRMLDAVKM-PEARKRMKmyphEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
...
gi 1561673794 234 GRD 236
Cdd:PRK09473 246 ARD 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-245 |
2.19e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVtvgdrAVNTLSSRGLRDLRGDIGMIFQGFNLAKRTS 99
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTG-----TILANNRKPTKQILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVMMGRLHSSPMWRTLLGAWSAEDT---ELGMQALERVeIVGKAYEKAssLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESvisELGLTKCENT-IIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 177 VASLDPPTSHVVMRDLQRInAELGITVVVNLHfLDLARRYG--DRLIGLRDGKVVFDGHGRDAdEAVFESI 245
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH-QPSSRVYQmfDSVLVLSEGRCLFFGKGSDA-MAYFESV 301
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-241 |
2.30e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTL-----SSRGL----- 78
Cdd:COG1137 7 ENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrARLGIgylpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 79 -----RDL--RGDIGMIFQGFNLAKRTsvlnnvMMGRLHSspmwrtLLGawsaedtELGMQALERVeivgkayeKASSLS 151
Cdd:COG1137 86 easifRKLtvEDNILAVLELRKLSKKE------REERLEE------LLE-------EFGITHLRKS--------KAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 152 GGQQQRVAIARALAQQPRVILADEPVASLDPptshVVMRDLQRINAEL---GITVVVNLH----FLDLArrygDRLIGLR 224
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDP----IAVADIQKIIRHLkerGIGVLITDHnvreTLGIC----DRAYIIS 210
|
250
....*....|....*....
gi 1561673794 225 DGKVVFDGHGRD--ADEAV 241
Cdd:COG1137 211 EGKVLAEGTPEEilNNPLV 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-232 |
2.53e-11 |
|
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: 61.78 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTY---------------------AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvt 64
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 65 vgdravnTLSSRGLRDLRGDIGMIFQ---GFNlaKRTSVLNNV-MMGRLHsspmwrtllgAWSAEDtelgMQALERvEIV 140
Cdd:cd03220 72 -------YPPDSGTVTVRGRVSSLLGlggGFN--PELTGRENIyLNGRLL----------GLSRKE----IDEKID-EII 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 141 -----GKAYEK-ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNlHFLDLAR 214
Cdd:cd03220 128 efselGDFIDLpVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVS-HDPSSIK 206
|
250
....*....|....*...
gi 1561673794 215 RYGDRLIGLRDGKVVFDG 232
Cdd:cd03220 207 RLCDRALVLEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-176 |
2.53e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLRgdIGMI-----FQGFNLA 95
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAG--IAYVpedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KrtSVLNNVMMGRLHSSPMWRTLLGAWSAEDTElgmQALERVEI-VGKAYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:COG1129 345 L--SIRENITLASLDRLSRGGLLDRRRERALAE---EYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
..
gi 1561673794 175 EP 176
Cdd:COG1129 420 EP 421
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-232 |
3.67e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTvgDRAVNTLSsRGLRDLRGDIGMIFQGFNLAKRTSVL 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSG--SVLLNGMP-IDAKEMRAISAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 NNVM------MGRLHSSPMWR-------TLLGAWSAEDTELGMQALERveivgkayekasSLSGGQQQRVAIARALAQQP 168
Cdd:TIGR00955 118 EHLMfqahlrMPRRVTKKEKRervdevlQALGLRKCANTRIGVPGRVK------------GLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHfLDLARRYG--DRLIGLRDGKVVFDG 232
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLG 249
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-184 |
4.20e-11 |
|
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: 59.38 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravntlssrglrDLRGDI 85
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-------------------------ELEPDE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGfnlakrtsvlNNVMMGRLHsspmwrtllgawsaedtelgmQalerveivgkayekassLSGGQQQRVAIARALA 165
Cdd:cd03221 55 GIVTWG----------STVKIGYFE---------------------Q-----------------LSGGEKMRLALAKLLL 86
|
170
....*....|....*....
gi 1561673794 166 QQPRVILADEPVASLDPPT 184
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLES 105
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-181 |
6.99e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.89 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSR------GLRDlrgdiGMifq 90
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachylGHRN-----AM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 91 gfnlaKRT-SVLNNVMmgrlhsspMWRTLLGAwsaedTELG-MQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK13539 85 -----KPAlTVAENLE--------FWAAFLGG-----EELDiAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170
....*....|...
gi 1561673794 169 RVILADEPVASLD 181
Cdd:PRK13539 147 PIWILDEPTAALD 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-232 |
1.02e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 21 ALDGVTLDIPAGQMVAVVGLSGAGKST-------LIRTINGLVPVTTGTVTVGDRAV---NTLSSRGLRDLRG-DIGMIF 89
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVielSEQSAAQMRHVRGaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QgfnlaKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALERVEIvGKAYEKAS----SLSGGQQQRVAIARALA 165
Cdd:PRK10261 111 Q-----EPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSryphQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 166 QQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-181 |
1.28e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravntlssrglrdLRGDIGMIF-QGFNLA 95
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-------------------------ARPDAGEVLwQGEPIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 K-RTSvlnnvmmgrLHSSPMW-------RTLLGAW----------SAEDTELGMQALERVEIVGKAYEKASSLSGGQQQR 157
Cdd:PRK13538 67 RqRDE---------YHQDLLYlghqpgiKTELTALenlrfyqrlhGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180
....*....|....*....|....*
gi 1561673794 158 VAIAR-ALAQQPRVILaDEPVASLD 181
Cdd:PRK13538 138 VALARlWLTRAPLWIL-DEPFTAID 161
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-232 |
1.34e-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: 58.87 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 19 HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTInglvpvttGTVTVGDRAVNTLSsrglrdlrgdigmifqgfnLAKRT 98
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--------LYASGKARLISFLP-------------------KFSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 SVlnnVMMGRLhsspmwRTLLgawsaeDTELGMQALERveivgkayeKASSLSGGQQQRVAIARALAQQPR--VILADEP 176
Cdd:cd03238 61 KL---IFIDQL------QFLI------DVGLGYLTLGQ---------KLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561673794 177 VASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLArRYGDRLI------GLRDGKVVFDG 232
Cdd:cd03238 117 STGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVL-SSADWIIdfgpgsGKSGGKVVFSG 176
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-241 |
1.37e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGgHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDLrgDIGMIF 89
Cdd:PRK15439 16 SISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--GIYLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFNLAKRTSVLNNVmmgrlhsspmwrtLLGAWSAEDTELGMQALerVEIVG---KAYEKASSLSGGQQQRVAIARALAQ 166
Cdd:PRK15439 93 QEPLLFPNLSVKENI-------------LFGLPKRQASMQKMKQL--LAALGcqlDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 167 QPRVILADEPVASLDPptsHVVMRDLQRINA--ELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGHGRDADEAV 241
Cdd:PRK15439 158 DSRILILDEPTASLTP---AETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-212 |
2.73e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdraVNTLSSRGLRDLRGDI 85
Cdd:PRK09544 5 VSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL--------------VAPDEGVIKRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKRTSVLNNVMMgRLHSspmwrtllGAWSAEDtelgMQALERVEIVGKAYEKASSLSGGQQQRVAIARALA 165
Cdd:PRK09544 70 GYVPQKLYLDTTLPLTVNRFL-RLRP--------GTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1561673794 166 QQPRVILADEPVASLDpPTSHVVMRDL-QRINAELGITVVVNLHFLDL 212
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD-VNGQVALYDLiDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-237 |
3.68e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlSSRGLRDLRGDI 85
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGFNLAKrtsvlnnvmmgrlhsspmwRTLLGAWSAEDTELGMQALERVEIVGKAYEKAS-----SLSGGQQQRVAI 160
Cdd:PRK10522 400 SAVFTDFHLFD-------------------QLLGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 161 ARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVV---NLHFLDLArrygDRLIGLRDGKVV-FDGHGRD 236
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAishDDHYFIHA----DRLLEMRNGQLSeLTGEERD 536
|
.
gi 1561673794 237 A 237
Cdd:PRK10522 537 A 537
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-236 |
5.68e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHT---ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLV----PVTTGTVTVGDRAVNTLSSRGLRDL 81
Cdd:PRK11022 7 DKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 82 RG-DIGMIFQG--FNLAKRTSVLNNVMMG-RLHSSPMWRTLLgawsaedtelgMQALERVEIVGKAyEKAS-------SL 150
Cdd:PRK11022 87 VGaEVAMIFQDpmTSLNPCYTVGFQIMEAiKVHQGGNKKTRR-----------QRAIDLLNQVGIP-DPASrldvyphQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVF 230
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
....*.
gi 1561673794 231 DGHGRD 236
Cdd:PRK11022 235 TGKAHD 240
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-210 |
8.01e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 19 HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSsrgLRDLRGDIGMIFQGFNLAKRT 98
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 99 sVLNNVMMGRLHSSP-----------MWRTLLGAWSAEDTELGmqalerveivgkayEKASSLSGGQQQRVAIARALAQQ 167
Cdd:PRK10789 405 -VANNIALGRPDATQqeiehvarlasVHDDILRLPQGYDTEVG--------------ERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFL 210
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRL 510
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-181 |
8.35e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTING-LVPVTTGTVTVGDRAVNTLSSRGLRDLRGDI------GMIF 89
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVydfvaeGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 QGFNLAKRTSVLNNVMmgrlhSSPMWRTL------------LGAWSAEDTElgMQALERVEIVGKAyeKASSLSGGQQQR 157
Cdd:PRK11147 94 QAEYLKRYHDISHLVE-----TDPSEKNLnelaklqeqldhHNLWQLENRI--NEVLAQLGLDPDA--ALSSLSGGWLRK 164
|
170 180
....*....|....*....|....
gi 1561673794 158 VAIARALAQQPRVILADEPVASLD 181
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
10-233 |
9.17e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTyagghTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVgDRAVNTLSSRGLRDLRGdigmif 89
Cdd:PRK03695 5 DVAVS-----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFA-GQPLEAWSAAELARHRA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 90 qgfNLAKRTSVLNNVmmgrlhssPMWRTLL-----GAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARAL 164
Cdd:PRK03695 73 ---YLSQQQTPPFAM--------PVFQYLTlhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 165 AQ-------QPRVILADEPVASLDPpTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDGH 233
Cdd:PRK03695 142 LQvwpdinpAGQLLLLDEPMNSLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-254 |
9.26e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGDIGMIFQG---FNLakrtSVLNNVMMGRLHSSPMWRTLLGAWSAEDtelgmqalERVEIVGKAYEK-----ASS 149
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEpmlFNM----SIYENIKFGKEDATREDVKRACKFAAID--------EFIESLPNKYDTnvgpyGKS 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRygdrliglRDGKVV 229
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR--------SDKIVV 1430
|
170 180
....*....|....*....|....*
gi 1561673794 230 FDGHGRDADEAVFESIYGRSLTAED 254
Cdd:PTZ00265 1431 FNNPDRTGSFVQAHGTHEELLSVQD 1455
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-190 |
9.37e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgDRA---VNTLSSRGLR--- 79
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHPqgySNDLTLFGRRrgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 80 -----DLRGDIGMIFQGFNLAKR--TSVLNNVMMGRLHSSPMWRtllgAWSAEDTELGMQALERVEIvGKAYEKAS--SL 150
Cdd:PRK10938 328 getiwDIKKHIGYVSSSLHLDYRvsTSVRNVILSGFFDSIGIYQ----AVSDRQQKLAQQWLDILGI-DKRTADAPfhSL 402
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMR 190
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRR 442
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-54 |
1.22e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1561673794 9 DNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTING 54
Cdd:NF033858 5 EGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-243 |
3.94e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.49 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 16 AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGLRDlrgDIGMIFQGFNLA 95
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ---QVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTsVLNNvmmgrlhsspmwrtLLGAWSAEDTELGMQA----LERVEIVGKAYEKA-SSLSGGQQQRVAIARALAQQPRV 170
Cdd:PRK10247 94 GDT-VYDN--------------LIFPWQIRNQQPDPAIflddLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 171 ILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDlARRYGDRLIGLRDgkvvfdgHGRDADEAVFE 243
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITLQP-------HAGEMQEARYE 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-211 |
5.60e-09 |
|
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: 55.63 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYA-GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLirtingLVPVTTGTVTVGDRAVNTLS--SRGLRDLRGDIG 86
Cdd:cd03289 7 DLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTL------LSAFLRLLNTEGDIQIDGVSwnSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTllgawsAEdtELGMQA--------LERVEIVGkayekASSLSGGQQQRV 158
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKV------AE--EVGLKSvieqfpgqLDFVLVDG-----GCVLSHGHKQLM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 159 AIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelGITVVVNLHFLD 211
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIE 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-211 |
1.03e-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: 55.33 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 9 DNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgDRAVN--TLSSRGLRdlrgdIG 86
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNgeARPQPGIK-----VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMG---------RLHSSPMwrtLLGAWSAEDTELG--MQALE-------------RVEIVGK 142
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGvaeikdaldRFNEISA---KYAEPDADFDKLAaeQAELQeiidaadawdldsQLEIAMD 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 143 AYE------KASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAelgiTVVVNLH---FLD 211
Cdd:TIGR03719 149 ALRcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTHdryFLD 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-193 |
1.41e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrGLRD 80
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAW---SAEDTELGMQAlerveivgKAYEKASSLSGGQQQR 157
Cdd:PLN03232 1308 LRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHikdVIDRNPFGLDA--------EVSEGGENFSVGQRQL 1379
|
170 180 190
....*....|....*....|....*....|....*.
gi 1561673794 158 VAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQ 193
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-205 |
1.49e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 147 ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINA-ELGITVVV 205
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIII 636
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
132-247 |
1.58e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 132 QALERVE-------IVGKAyeKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLqRINAELGITVV 204
Cdd:PLN03140 997 EVMELVEldnlkdaIVGLP--GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV-RNTVDTGRTVV 1073
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1561673794 205 VNLH--FLDLARRYGDRLIGLRDGKVVFDGH-GRDADEAV--FESIYG 247
Cdd:PLN03140 1074 CTIHqpSIDIFEAFDELLLMKRGGQVIYSGPlGRNSHKIIeyFEAIPG 1121
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-208 |
1.63e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYA-GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTIngLVPVTTGTVTVGDRAvnTLSSRGLRD 80
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL--LRLLSTEGEIQIDGV--SWNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTllgawsAEdtELGMQAL-----ERVEIVgkAYEKASSLSGGQQ 155
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKV------AE--EVGLKSVieqfpDKLDFV--LVDGGYVLSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 156 QRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElgITVVVNLH 208
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEH 1410
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-232 |
1.67e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 13 VTYAGGHTALDGVTLDIPAGQMVAVVGLSGAG--KSTLIRTINGLVPVTTGTvtvgdRAVNTLSSRglRDLRGDIGMiFQ 90
Cdd:NF000106 20 VKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPW-----RF*TWCANR--RALRRTIG*-HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 91 GFNLAKRTSVL---NNVMMGRLhsspmwrtlLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQ 167
Cdd:NF000106 92 PVR*GRRESFSgreNLYMIGR*---------LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 168 PRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDG 232
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-251 |
1.86e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdraV--------------NTLSSRGLRD-- 80
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG---------------VyphgsyegeilfdgEVCRFKDIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGdIGMIFQGFNLAKRTSVLNNVMMGRLHSSPM---W-RTLLGAwsaedTELgmqaLERVEIVGKAYEKASSLSGGQQQ 156
Cdd:NF040905 77 ALG-IVIIHQELALIPYLSIAENIFLGNERAKRGvidWnETNRRA-----REL----LAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVV--FDGHG 234
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIetLDCRA 225
|
250
....*....|....*...
gi 1561673794 235 RDADEA-VFESIYGRSLT 251
Cdd:NF040905 226 DEVTEDrIIRGMVGRDLE 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
145-261 |
3.43e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 145 EKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRiNAELGITVVVNLHFLDLARRyGDRLIGLR 224
Cdd:PTZ00243 778 EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFL-GALAGKTRVLATHQVHVVPR-ADYVVALG 855
|
90 100 110
....*....|....*....|....*....|....*...
gi 1561673794 225 DGKVVFDGHGRD-ADEAVFESIYGRSLTAEDVLEAKAE 261
Cdd:PTZ00243 856 DGRVEFSGSSADfMRTSLYATLAAELKENKDSKEGDAD 893
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-182 |
3.97e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 8 FDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVntlSSRGLRDLRGDIG 86
Cdd:PTZ00243 1311 FEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLlgawsaedtEL-GMQalERVE-----IVGKAYEKASSLSGGQQQRVAI 160
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVDPFLEASSAEVWAAL---------ELvGLR--ERVAsesegIDSRVLEGGSNYSVGQRQLMCM 1456
|
170 180
....*....|....*....|...
gi 1561673794 161 ARALAQQPR-VILADEPVASLDP 182
Cdd:PTZ00243 1457 ARALLKKGSgFILMDEATANIDP 1479
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-175 |
4.71e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 19 HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgdravnTLSSRGLRDLRGDIGMIFQGFNLAKRT 98
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV----------------TMPNKGTVDIKGSAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1561673794 99 SVLNNVMMGRLhsspmwrtLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADE 175
Cdd:PRK13545 101 TGIENIELKGL--------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-228 |
5.41e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLirTINGLVPVTTGTVTVGDRAVNtLSSRGLRDLRGD 84
Cdd:TIGR00957 1285 VEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGLN-IAKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 85 IGMIFQGFNLAKRTSVLNNVMMGRLHSSPMWrtllgaWSAEDTEL-GMQALERVEIVGKAYEKASSLSGGQQQRVAIARA 163
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSLRMNLDPFSQYSDEEVW------WALELAHLkTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1561673794 164 LAQQPRVILADEPVASLDPPTSHVVMRDLqRINAElGITVVVNLHFLDLARRYgDRLIGLRDGKV 228
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTI-RTQFE-DCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
144-232 |
7.74e-08 |
|
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: 52.86 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 144 YEK-ASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVV---NLHFLDLarrYGDR 219
Cdd:COG1245 449 LDKnVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVvdhDIYLIDY---ISDR 525
|
90
....*....|...
gi 1561673794 220 LIglrdgkvVFDG 232
Cdd:COG1245 526 LM-------VFEG 531
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-232 |
1.34e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 20 TALDGVTLDIPAGQMVAVVGLSGAGKSTLIR-------------TINGLVpvttgtvtvgdravntlSSRGLRDLRGDIG 86
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgilvptsgevRVLGYV-----------------PFKRRKEFARRIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 87 MIFqG------FNLAKRTSVLnnvMMGRLHSSPM--WRTLLgawsAEDTELgmqaLERVEIVGKAYEKassLSGGQQQRV 158
Cdd:COG4586 99 VVF-GqrsqlwWDLPAIDSFR---LLKAIYRIPDaeYKKRL----DELVEL----LDLGELLDTPVRQ---LSLGQRMRC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 159 AIARALAQQPRVILADEPVASLDpptshVVM----RD-LQRINAELGITVVVNLHFLD----LArrygDRLIGLRDGKVV 229
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLD-----VVSkeaiREfLKEYNRERGTTILLTSHDMDdieaLC----DRVIVIDHGRII 234
|
...
gi 1561673794 230 FDG 232
Cdd:COG4586 235 YDG 237
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-232 |
1.38e-07 |
|
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: 50.72 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 16 AGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGtvtvgdravntlssrglrdLRGDI---GMIFQGF 92
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-------------------VEGDIhynGIPYKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 93 -NLAKRTSVLNNvmMGRLHSSPM--WRTLlgawsaeDTELGMQALERVeivgkayekaSSLSGGQQQRVAIARALAQQPR 169
Cdd:cd03233 78 aEKYPGEIIYVS--EEDVHFPTLtvRETL-------DFALRCKGNEFV----------RGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 170 VILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLH-----FLDLArrygDRLIGLRDGKVVFDG 232
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqasdeIYDLF----DKVLVLYEGRQIYYG 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-211 |
1.62e-07 |
|
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: 51.86 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgdravntlssrglrdlrgDI 85
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP-------------------------DS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGfnlakRTSVLNNVMMGRLHSSP---MWRTLLGAwsAEDTELGmqaleRVEIVGKAY------------EKASSL 150
Cdd:TIGR03719 377 GTIEIG-----ETVKLAYVDQSRDALDPnktVWEEISGG--LDIIKLG-----KREIPSRAYvgrfnfkgsdqqKKVGQL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 151 SGGQQQRVAIARALAQQPRVILADEPVASLDPPTshvvMRDLQRINAELGITVVVNLH---FLD 211
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHdrwFLD 504
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-232 |
3.10e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 50.10 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAG-----QMVAVVGLSGAGKSTLIRTINGLVPVTTGTVtvgDRAVNTLSSRGlRDLRGDIGMIFQGFnLAK 96
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKP-QYIKADYEGTVRDL-LSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 RTSvlnnvmmgRLHSSPMWRTLLgawsaedtelgMQALERVEIVGKayeKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:cd03237 85 ITK--------DFYTHPYFKTEI-----------AKPLQIEQILDR---EVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1561673794 177 VASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIglrdgkvVFDG 232
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEG 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-211 |
3.35e-07 |
|
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: 51.17 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 4 DGIAFDNVSVTYAGGHT-ALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTlssrglrdlr 82
Cdd:TIGR01257 1936 DILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 83 gDIGMIFQGFNLAKRTSVLNNVMMGRLHSSpMWRTLLGAWSAEDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIAR 162
Cdd:TIGR01257 2006 -NISDVHQNMGYCPQFDAIDDLLTGREHLY-LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1561673794 163 ALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLHFLD 211
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSME 2131
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
150-232 |
8.58e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVV---NLHFLDLarrYGDRLIglrdg 226
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVvdhDIYMIDY---ISDRLM----- 525
|
....*.
gi 1561673794 227 kvVFDG 232
Cdd:PRK13409 526 --VFEG 529
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-232 |
9.30e-07 |
|
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: 48.01 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravntlssrglrdlRGDIGMIfQGfnlakrtsvl 101
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---------------------------RKTAGVI-TG---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 102 nNVMMGRLHSSPMWRTLLGAWSAEDTELGMQALeRVEIVGKAYEKAssLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:cd03232 65 -EILINGRPLDKNFQRSTGYVEQQDVHSPNLTV-REALRFSALLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1561673794 182 PPTSHVVMRDLQRInAELGITVVVNLH------FldlarRYGDRLIGL-RDGKVVFDG 232
Cdd:cd03232 141 SQAAYNIVRFLKKL-ADSGQAILCTIHqpsasiF-----EKFDRLLLLkRGGKTVYFG 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-240 |
9.79e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 25 VTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgDRAVN-TLSSRGLR-DLRGDIGMIFQGFNLAKR----- 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGA-----------TRRTAgQVYLDGKPiDIRSPRDAIRAGIMLCPEdrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 98 -----TSVLNNVMMG-RLHSSPMWRTLLGAWSAEDTELGMQALeRVEIVGkAYEKASSLSGGQQQRVAIARALAQQPRVI 171
Cdd:PRK11288 341 giipvHSVADNINISaRRHHLRAGCLINNRWEAENADRFIRSL-NIKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 172 LADEPVASLDPPTSHVVMRDLQRInAELGITVVVNLHflDLARRYG--DRLIGLRDGKVVFDGHGRDADEA 240
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRIAGELAREQATER 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-184 |
1.88e-06 |
|
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: 48.75 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 4 DGIAFDNVSVTyagGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravNTLSSRGLRDLRG 83
Cdd:TIGR01271 427 DGLFFSNFSLY---VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG----------------ELEPSEGKIKHSG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQgFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDtELGMQALERVEIVGkayEKASSLSGGQQQRVAIARA 163
Cdd:TIGR01271 488 RISFSPQ-TSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEE-DIALFPEKDKTVLG---EGGITLSGGQRARISLARA 562
|
170 180
....*....|....*....|.
gi 1561673794 164 LAQQPRVILADEPVASLDPPT 184
Cdd:TIGR01271 563 VYKDADLYLLDSPFTHLDVVT 583
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-181 |
2.45e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravntlssrglrDLRGDI 85
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-------------------------ELQPSS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GMIFQGfnlAK-RTSVLN--NVMMGRLHSSP---MWRTLLGAwsaedTELGMQA-LERVEIVGK-AYEKASSLSGGQQQR 157
Cdd:PLN03073 564 GTVFRS---AKvRMAVFSqhHVDGLDLSSNPllyMMRCFPGV-----PEQKLRAhLGSFGVTGNlALQPMYTLSGGQKSR 635
|
170 180
....*....|....*....|....
gi 1561673794 158 VAIARALAQQPRVILADEPVASLD 181
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLD 659
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
5-203 |
2.81e-06 |
|
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: 48.21 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 5 GIAFDNVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGL-VPVTTGTVTVGDRAVNTLSSR---GLRD 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwPVYGGRLTKPAKGKLFYVPQRpymTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDI-------GMIFQGFNLAKRTSVLNNVMMGRLhsspmwRTLLGAWSAedtelgMQALERVeivgkayekassLSGG 153
Cdd:TIGR00954 531 LRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHI------LEREGGWSA------VQDWMDV------------LSGG 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELgITV 203
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITL-FSV 635
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-181 |
6.40e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 10 NVSVTYAGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLvpvttgtvtvgDRAVN--TLSSRGLRdlrgdIGM 87
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFEgeARPAPGIK-----VGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQGFNLAKRTSVLNNVMMG---------RLHSSPMwrtLLGAWSAEDTELG--MQALE-------------RVEIVGKA 143
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGvaevkaaldRFNEIYA---AYAEPDADFDALAaeQGELQeiidaadawdldsQLEIAMDA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1561673794 144 Y------EKASSLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PRK11819 152 LrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-181 |
7.87e-06 |
|
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: 45.60 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 17 GGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVpvttgtvtvgdravntlssrGLRDLRGDIgmIFQGFNLak 96
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP--------------------KYEVTEGEI--LFKGEDI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 97 rtsvlnnvmmgrLHSSPMWRTLLGAWsaedteLGMQALERVEIVgkayeKAS--------SLSGGQQQRVAIARALAQQP 168
Cdd:cd03217 67 ------------TDLPPEERARLGIF------LAFQYPPEIPGV-----KNAdflryvneGFSGGEKKRNEILQLLLLEP 123
|
170
....*....|...
gi 1561673794 169 RVILADEPVASLD 181
Cdd:cd03217 124 DLAILDEPDSGLD 136
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-52 |
8.07e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.56 E-value: 8.07e-06
10 20 30
....*....|....*....|....*....|.
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTI 52
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNDI 651
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-55 |
1.16e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGL 55
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-181 |
1.42e-05 |
|
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: 45.23 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 4 DGIAFDNVSVTyagGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravNTLSSRGLRDLRG 83
Cdd:cd03291 38 NNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG----------------ELEPSEGKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 84 DIGMIFQgFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAWSAEDtELGMQALERVEIVGkayEKASSLSGGQQQRVAIARA 163
Cdd:cd03291 99 RISFSSQ-FSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEE-DITKFPEKDNTVLG---EGGITLSGGQRARISLARA 173
|
170
....*....|....*...
gi 1561673794 164 LAQQPRVILADEPVASLD 181
Cdd:cd03291 174 VYKDADLYLLDSPFGYLD 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-181 |
1.47e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 2 SGDGIAFDNVSVTYAGG-HTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLssrGLRD 80
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 81 LRGDIGMIFQGFNLAKRTSVLNNVMMGRLHSSPMWRTLLGAwSAEDT----ELGMQAlerveivgKAYEKASSLSGGQQQ 156
Cdd:PLN03130 1311 LRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERA-HLKDVirrnSLGLDA--------EVSEAGENFSVGQRQ 1381
|
170 180
....*....|....*....|....*
gi 1561673794 157 RVAIARALAQQPRVILADEPVASLD 181
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVD 1406
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-49 |
1.50e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 1.50e-05
10 20
....*....|....*....|....*...
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLI 49
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-232 |
1.78e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 6 IAFDNVSVTYaGGHTALDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdravntlssrGLRDLRGDI 85
Cdd:PRK10636 313 LKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG----------------------ELAPVSGEI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 86 GM---IFQGFNLAKRTSVLnnvmmgRLHSSPMWRTllgawsaedTELGMQALE---RVEIVG------KAYEKASSLSGG 153
Cdd:PRK10636 370 GLakgIKLGYFAQHQLEFL------RADESPLQHL---------ARLAPQELEqklRDYLGGfgfqgdKVTEETRRFSGG 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 154 QQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLqrINAElGITVVVNlHFLDLARRYGDRLIGLRDGKV-VFDG 232
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL--IDFE-GALVVVS-HDRHLLRSTTDDLYLVHDGKVePFDG 510
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-232 |
2.01e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIrtinglvpvttgtvtvGDRAVNTLSSR--GLRDLRGDIGMIfQGFNLAKRTS 99
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI----------------NDTLYPALARRlhLKKEQPGNHDRI-EGLEHIDKVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVMMGR-LHSSPMwrTLLGA----------------WSAEDTE-----------LGMQALERVEI------------ 139
Cdd:cd03271 74 VIDQSPIGRtPRSNPA--TYTGVfdeirelfcevckgkrYNRETLEvrykgksiadvLDMTVEEALEFfenipkiarklq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 140 ----VGKAYEK----ASSLSGGQQQRVAIARALAQQPR----VILaDEPVASLDPPTSHVVMRDLQRInAELGITVVVNL 207
Cdd:cd03271 152 tlcdVGLGYIKlgqpATTLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIE 229
|
250 260 270
....*....|....*....|....*....|.
gi 1561673794 208 HFLDLARRyGDRLI------GLRDGKVVFDG 232
Cdd:cd03271 230 HNLDVIKC-ADWIIdlgpegGDGGGQVVASG 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
150-181 |
2.15e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.15e-05
10 20 30
....*....|....*....|....*....|..
gi 1561673794 150 LSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-257 |
2.59e-05 |
|
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: 43.71 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 149 SLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIglrdgkv 228
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH------- 143
|
90 100
....*....|....*....|....*....
gi 1561673794 229 VFDGHgrdadeavfESIYGRSLTAEDVLE 257
Cdd:cd03222 144 VFEGE---------PGVYGIASQPKGTRE 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-49 |
2.90e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 2.90e-05
10 20
....*....|....*....|....*...
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLI 49
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-229 |
2.97e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.31 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 23 DGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVttgtvtvgdrAVNTLSSRGLRD--------LRG-DIGMIFQgfn 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA----------GVRQTAGRVLLDgkpvapcaLRGrKIATIMQ--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 lAKRtSVLNNVMMGRLHSSpmwRTLLGAWSAEDTELGMQALERV-----EIVGKAYekASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK10418 87 -NPR-SAFNPLHTMHTHAR---ETCLALGKPADDATLTAALEAVglenaARVLKLY--PFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561673794 169 RVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNLHFLDLARRYGDRLIGLRDGKVV 229
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-205 |
5.21e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 25 VTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSrgLRDLRGDIGMI---------FQGFNLA 95
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYItesrrdngfFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 96 KRTSVLNNVMMGRLHsspmwrtllGAW----SAEDTELGMQALERVEIVGKAYEK-ASSLSGGQQQRVAIARALAQQPRV 170
Cdd:PRK09700 360 QNMAISRSLKDGGYK---------GAMglfhEVDEQRTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190
....*....|....*....|....*....|....*...
gi 1561673794 171 ILADEPVASLDPPTS---HVVMRDLqrinAELGITVVV 205
Cdd:PRK09700 431 IIFDEPTRGIDVGAKaeiYKVMRQL----ADDGKVILM 464
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-181 |
5.79e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 25 VTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLS-----SRGL------RDLRGDIGMIFQGFN 93
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneaiNHGFalvteeRRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 94 lakrtSVLNNV-----MMGRLHSSPMwrtllgawsAEDTELGMQALeRVEIVGKaYEKASSLSGGQQQRVAIARALAQQP 168
Cdd:PRK10982 347 -----SLISNIrnyknKVGLLDNSRM---------KSDTQWVIDSM-RVKTPGH-RTQIGSLSGGNQQKVIIGRWLLTQP 410
|
170
....*....|...
gi 1561673794 169 RVILADEPVASLD 181
Cdd:PRK10982 411 EILMLDEPTRGID 423
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
135-212 |
6.95e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.12 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 135 ERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVV--NLHFLDL 212
Cdd:cd03236 125 DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVehDLAVLDY 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-228 |
7.68e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 25 VTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGDRAVNTLSSRGlrdlRGDIGMIF-----QGFNLAKRTS 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 100 VLNNVMMGRLHSSPMWrtllgawsaEDTELGMQALERV-EIVG----KAYEKASSLSGGQQQRVAIARALAQQPRVILAD 174
Cdd:PRK15439 358 LAWNVCALTHNRRGFW---------IKPARENAVLERYrRALNikfnHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 175 EPVASLDPPTSHVVMRDLQRInAELGITVVVNLHFLDLARRYGDRLIGLRDGKV 228
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-232 |
1.63e-04 |
|
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: 41.86 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLI----------RTINGLVPVTTGTVTVGDR----AVNTLS----------SRG 77
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAYARQFLGQMDKpdvdSIEGLSpaiaidqkttSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 78 LRDLRGDI-------GMIFQGFNLAKRTSVLNNVMMGRLhsspmwrtllgawsaedtelgmqALERveivgkayeKASSL 150
Cdd:cd03270 91 PRSTVGTVteiydylRLLFARVGIRERLGFLVDVGLGYL-----------------------TLSR---------SAPTL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 151 SGGQQQRVAIARALAQQPRVIL--ADEPVASLDPPTSHVVMRDLQRINAeLGITVVVNLHFLDLARRyGDRLI------G 222
Cdd:cd03270 139 SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIRA-ADHVIdigpgaG 216
|
250
....*....|
gi 1561673794 223 LRDGKVVFDG 232
Cdd:cd03270 217 VHGGEIVAQG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-258 |
2.16e-04 |
|
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: 42.12 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGLVPVTTGTVTVGD-RAVNTLSSrgLRDLRGDIGMIFQGfnlAKRTSV 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINgKPVDIRNP--AQAIRAGIAMVPED---RKRHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 101 LNNVMMGR---LHSSPMWRTLLGAWSAEDTELGMQALERVEI-VGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEP 176
Cdd:TIGR02633 351 VPILGVGKnitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 177 VASLDPPTSHVVMRDLQRINAElGITVVVNLHFLDLARRYGDRLIGLRDGKVVFDghgrdadeavfesIYGRSLTAEDVL 256
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD-------------FVNHALTQEQVL 496
|
..
gi 1561673794 257 EA 258
Cdd:TIGR02633 497 AA 498
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-181 |
2.39e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 41.21 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTLIRTINGlvpvttgtvtvgdRAVNTLSSrGLRDLRGD--------------IGM 87
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-------------HPKYEVTS-GSILLDGEdilelspderaragIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 88 IFQ------GFNLAK--RTSVlnNVMMGRLHSSPMWRTLLGAWSAEdteLGMQA--LERveivgkayEKASSLSGGQQQR 157
Cdd:COG0396 82 AFQypveipGVSVSNflRTAL--NARRGEELSAREFLKLLKEKMKE---LGLDEdfLDR--------YVNEGFSGGEKKR 148
|
170 180
....*....|....*....|....
gi 1561673794 158 VAIARALAQQPRVILADEPVASLD 181
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLD 172
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-236 |
3.03e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVI--LADEPVASLDPPTSHVVMRDLQRINAElGITVVVNLH---FLDLArrygDRLI- 221
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHdeqMISLA----DRIId 549
|
90 100
....*....|....*....|
gi 1561673794 222 -----GLRDGKVVFDGHGRD 236
Cdd:PRK00635 550 igpgaGIFGGEVLFNGSPRE 569
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-48 |
3.66e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 3.66e-04
10 20
....*....|....*....|....*..
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTL 48
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-213 |
4.79e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 4.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEpvasldpPTSHVVMRdlQRINA-----EL--GITVVVNLHflDLA 213
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDE-------PTSYLDIR--QRLNVarlirELaeGKYVLVVEH--DLA 272
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-226 |
7.68e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 32 GQMVAVVGLSGAGKSTLIRTInglvpvttgtvtvgdravntlsSRGLRDLRGDIGMIfqgfnlakrtsvlnnvmmgrlhs 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL----------------------ARELGPPGGGVIYI----------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 112 spmwrtllgawsaeDTELGMQALERVEIVGKAYEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVM-- 189
Cdd:smart00382 37 --------------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLll 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1561673794 190 ---RDLQRINAELGITVVVNLHFL-----DLARRYGDRLIGLRDG 226
Cdd:smart00382 103 eelRLLLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
148-181 |
1.11e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
148-213 |
1.26e-03 |
|
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: 39.77 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561673794 148 SSLSGGQQQRVAIARALAQQPRVILADEPVASLDpptshvvMRdlQRIN--------AELGITVVVNLHflDLA 213
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-------IY--QRLNvarlirelAEEGKYVLVVEH--DLA 273
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
11-49 |
1.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.50e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1561673794 11 VSVTYAGGHTaLDGVTLDIPAGQMVAVVGLSGAGKSTLI 49
Cdd:PRK00635 601 LTLSKATKHN-LKDLTISLPLGRLTVVTGVSGSGKSSLI 638
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-48 |
2.61e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.61e-03
10 20
....*....|....*....|....*..
gi 1561673794 22 LDGVTLDIPAGQMVAVVGLSGAGKSTL 48
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-48 |
2.72e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.72e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
145-181 |
3.74e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.74e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1561673794 145 EKASSLSGGQQQRVAIARALAQQPRVILADEPVASLD 181
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
139-244 |
8.44e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.52 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561673794 139 IVGKayEKASSLSGGQQQRVAIARALAQQPRVILADEPVASLDPPTSHVVMRDLQRINAELGITVVVNL-----HFLDLA 213
Cdd:PLN03140 328 IVGD--EMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLlqpapETFDLF 405
|
90 100 110
....*....|....*....|....*....|.
gi 1561673794 214 rrygDRLIGLRDGKVVFDGhGRDADEAVFES 244
Cdd:PLN03140 406 ----DDIILLSEGQIVYQG-PRDHILEFFES 431
|
|
| |
