|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-227 |
5.96e-122 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 346.26 E-value: 5.96e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKkGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:COG1136 1 MSPLLELRNLTKSYGT-GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG1136 80 LARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKEI 227
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-223 |
3.93e-109 |
|
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: 313.27 E-value: 3.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKkGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:cd03255 1 IELKNLSKTYGG-GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-223 |
5.60e-78 |
|
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: 235.02 E-value: 5.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:COG4181 8 IIELRGLTKTVGT-GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAinpkvdKIAKRL----GIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR------ARARALlervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-223 |
1.36e-75 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 228.40 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:COG2884 1 MIRFENVSKRYPGGRE----ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:COG2884 77 LR-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELvDRMPKRVLELEDGRL 215
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-223 |
2.95e-74 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 224.92 E-value: 2.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:TIGR02211 1 LLKCENLGKRY-QEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:TIGR02211 80 LRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-230 |
7.61e-74 |
|
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: 223.89 E-value: 7.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmadf 84
Cdd:cd03293 1 LEVRNVSKTYGGGGG-AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgqEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03293 74 ---DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFI--KDGKIGKEIKKD 230
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLsaRPGRIVAEVEVD 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-248 |
1.07e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 224.97 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSE---VVQVQDITKTYGKKGeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLn 77
Cdd:COG1116 1 MSAaapALELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 knqmadfrGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAA 157
Cdd:COG1116 79 --------GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKD--GKIGKEIK------ 228
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSArpGRIVEEIDvdlprp 230
|
250 260
....*....|....*....|....*
gi 489748581 229 --KDGKSREEFY---QEIIAELGRR 248
Cdd:COG1116 231 rdRELRTSPEFAalrAEILDLLREE 255
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-223 |
1.39e-73 |
|
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: 223.17 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:cd03259 1 LELKGLSKTYGSV-----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03259 72 RN--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-205 |
5.94e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 225.73 E-value: 5.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:COG1135 2 IELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
5.27e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 218.43 E-value: 5.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:COG3842 2 AMPALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfRGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG3842 77 ----RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEAlALADRIAVMNDGRI 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-204 |
8.76e-70 |
|
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: 213.98 E-value: 8.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:cd03258 80 AR-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTH 204
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
4.63e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 216.09 E-value: 4.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVvQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknq 80
Cdd:COG3839 1 MASL-ELENVSKSYGGV-----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG3839 71 PPKDRN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAmTLADRIAVMNDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
4.56e-68 |
|
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: 218.23 E-value: 4.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQD----FNllENLTNRENIALPLSLQNVKTSA-INPKVDKIAKRLGID-HILNKYPAEISGGQKQRVAAA 157
Cdd:COG1123 340 LR-RRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAeRRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
1.53e-65 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 203.75 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:COG3638 2 MLELRNLSKRYP--GGTP--ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQeIGFIFQDFNLLENLTnrenialplSLQNVKTSAIN------------PKVDKIA-----KRLGIDHILNKYPAEI 146
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLS---------VLTNVLAGRLGrtstwrsllglfPPEDRERalealERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 147 SGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP-YSASYASRILFIKDGKI 223
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRV 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-223 |
2.32e-65 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 202.17 E-value: 2.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:TIGR02982 1 VISIRNLNHYYGH-GSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQeIGFIFQDFNLLENLTNRENIALPLSLQ-NVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:TIGR02982 80 LRRR-IGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
1.95e-64 |
|
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: 200.59 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDR-----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRgQEIGFIFQDFNLLENLTNRENIALPLS-LQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLADGKI 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-204 |
4.39e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 203.11 E-value: 4.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:PRK11153 80 AR-RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTH 204
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-218 |
6.59e-64 |
|
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: 198.22 E-value: 6.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRG 86
Cdd:TIGR03608 1 LKNISKKFGDK-----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAI 166
Cdd:TIGR03608 76 EKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489748581 167 LYGDEPTGALDSKSATELLETMKGLNEKDKVsILMVTHDPYSASYASRILFI 218
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHDPEVAKQADRVIEL 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-223 |
7.43e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 199.06 E-value: 7.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQMAD 83
Cdd:COG1126 1 MIEIENLHKSFGDL-----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIAL-PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:COG1126 75 LR-RKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEmGFAREVADRVVFMDGGRI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-223 |
3.91e-63 |
|
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: 196.32 E-value: 3.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:cd03301 1 VELENVTKRFGNV-----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03301 72 --RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-223 |
1.00e-62 |
|
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: 195.80 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnQMAD 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSV-KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR-RLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQD----FNLLenLTNRENIALPLSLQ--NVKTSAINPKVDKIAKRLGID-HILNKYPAEISGGQKQRVAA 156
Cdd:cd03257 79 IRRKEIQMVFQDpmssLNPR--MTIGEQIAEPLRIHgkLSKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-223 |
8.56e-62 |
|
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: 194.25 E-value: 8.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnKNQMADF 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQD----FNllENLTNRENIALPLSLQNVKtsAINPKVDKIAKRLGID-HILNKYPAEISGGQKQRVAAARA 159
Cdd:COG1124 78 RRR-VQMVFQDpyasLH--PRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-223 |
2.38e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.59 E-value: 2.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMadf 84
Cdd:COG1131 1 IEVRGLTKRYGDK-----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:COG1131 73 --RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAeRLCDRVAIIDKGRI 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-222 |
4.31e-61 |
|
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: 190.09 E-value: 4.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnQMADF 84
Cdd:cd03229 1 LELKNVSKRYGQK-----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED-ELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLslqnvktsainpkvdkiakrlgidhilnkypaeiSGGQKQRVAAARALVHEP 164
Cdd:cd03229 75 R-RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGK 222
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-223 |
6.43e-61 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 191.55 E-value: 6.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknqmaDF 84
Cdd:TIGR00968 1 IEIANISKRFGS-----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRV------HA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:TIGR00968 70 RDRKIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAmEVADRIVVMSNGKI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-240 |
9.82e-61 |
|
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: 190.62 E-value: 9.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYgkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnKNQMADF 84
Cdd:COG1122 1 IELENLSFSY----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:COG1122 74 R-RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDP-YSASYASRILFIKDGKigkeIKKDGKSREEFYQE 240
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLdLVAELADRVIVLDDGR----IVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-222 |
1.06e-60 |
|
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: 189.99 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfR 85
Cdd:cd03225 1 ELKNLSFSYPDGARP---ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQDFNL-LENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03225 74 RRKVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDP-YSASYASRILFIKDGK 222
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
2.14e-60 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 193.82 E-value: 2.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSevVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnknq 80
Cdd:COG1118 1 MS--IEVRNISKRFG-----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 mADFRGQE--IGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAAR 158
Cdd:COG1118 68 -TNLPPRErrVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 159 ALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRI 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-222 |
5.13e-60 |
|
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: 188.61 E-value: 5.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:TIGR02673 1 MIEFHNVSKAYPG----GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:TIGR02673 77 LR-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNeKDKVSILMVTHDP-YSASYASRILFIKDGK 222
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-223 |
6.12e-60 |
|
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: 192.94 E-value: 6.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnQ 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFG-----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPP-Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFrgqeiGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:TIGR03265 75 KRDY-----GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVI 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-223 |
7.01e-60 |
|
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: 188.12 E-value: 7.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlNKNQMADF 84
Cdd:cd03262 1 IEIKNLHKSFGDF-----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIAL-PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:cd03262 75 R-QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-223 |
3.46e-59 |
|
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: 186.94 E-value: 3.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:cd03261 1 IELRGLTKSFGGR-----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLsLQNVKTSA--INPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:cd03261 76 R-RRMGMLFQSGALFDSLTVFENVAFPL-REHTRLSEeeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-236 |
7.06e-58 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 194.17 E-value: 7.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK10535 1 MTALLELKDIRRSY-PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:PRK10535 80 LAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYASRILFIKDGKI----GKEIKKDGKSREE 236
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIvrnpPAQEKVNVAGGTE 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-223 |
8.78e-58 |
|
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: 183.59 E-value: 8.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03300 72 --RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-245 |
3.46e-57 |
|
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: 182.00 E-value: 3.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKGekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFR 85
Cdd:cd03256 2 EVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQeIGFIFQDFNLLENLTnrenialplSLQNVKTSAIN------------PKVDKIA-----KRLGIDHILNKYPAEISG 148
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLS---------VLENVLSGRLGrrstwrslfglfPKEEKQRalaalERVGLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 149 GQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP-YSASYASRILFIKDGkigkEI 227
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDG----RI 223
|
250
....*....|....*...
gi 489748581 228 KKDGKSrEEFYQEIIAEL 245
Cdd:cd03256 224 VFDGPP-AELTDEVLDEI 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
3.87e-57 |
|
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: 189.73 E-value: 3.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPT---TGNVYINGRDITGLN 77
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDV---PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 knqmADFRGQEIGFIFQDF-NLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:COG1123 78 ----EALRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP-YSASYASRILFIKDGKI 223
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-223 |
5.40e-57 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 180.68 E-value: 5.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:cd03292 1 IEFINVTKTYPN----GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03292 77 R-RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNeKDKVSILMVTHDP-YSASYASRILFIKDGKI 223
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-227 |
7.31e-57 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 181.17 E-value: 7.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK11629 5 LLQCDNLCKRY-QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKEI 227
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-223 |
8.55e-57 |
|
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: 181.40 E-value: 8.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAd 83
Cdd:COG1120 1 MLEAENLSVGYGGR-----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 frgQEIGFIFQDFNLLENLTNRENIAL-------PLSLQNVKTSAInpkVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:COG1120 75 ---RRIAYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAArYADRLVLLKDGRI 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-223 |
1.91e-56 |
|
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: 180.23 E-value: 1.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknqmaDF 84
Cdd:cd03296 3 IEVRNVSKRFG-----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKT----SAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:cd03296 72 QERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-246 |
1.43e-53 |
|
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: 173.12 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmaDFR 85
Cdd:COG4555 3 EVENLSKKYGKV-----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR----EAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 gQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKVsILMVTHDPYS-ASYASRILFIKDGKI----GKEIKKDGKSREEFYQE 240
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEvEALCDRVVILHKGKVvaqgSLDELREEIGEENLEDA 231
|
....*.
gi 489748581 241 IIAELG 246
Cdd:COG4555 232 FVALIG 237
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
25-223 |
2.25e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 2.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRgQEIGFIFQDFNLLENlTN 104
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR-RQVAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNVKTSaiNPKVDKIAKRLGIDH-ILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATE 183
Cdd:COG4619 91 RDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489748581 184 LLETMKGLNEKDKVSILMVTHDPY-SASYASRILFIKDGKI 223
Cdd:COG4619 169 VEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-223 |
7.09e-53 |
|
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: 168.73 E-value: 7.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnKNQMADF 84
Cdd:cd03230 1 IEVRNLSKRYGKK-----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALplslqnvktsainpkvdkiakrlgidhilnkypaeiSGGQKQRVAAARALVHEP 164
Cdd:cd03230 72 K-RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-235 |
7.75e-53 |
|
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: 170.94 E-value: 7.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:TIGR02315 1 MLEVENLSKVYPN----GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALP-LSLQNVKTSAIN--PKVDK-----IAKRLGIDHILNKYPAEISGGQKQRVA 155
Cdd:TIGR02315 77 LR-RRIGMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLLGrfSEEDKeralsALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGkigkEIKKDGKSR 234
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAG----EIVFDGAPS 231
|
.
gi 489748581 235 E 235
Cdd:TIGR02315 232 E 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-223 |
8.06e-53 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 172.06 E-value: 8.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKG-------------------ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGN 65
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKgkskeeilkktgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 66 VYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAE 145
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 146 ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-244 |
1.19e-52 |
|
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: 170.21 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfrgQEIGFIFQDFNLLENLTN 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 185 LETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIgkeIKKdGKSREEFYQ---EIIAE 244
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKL---IQV-GKPEEVFKKpknEFVAE 228
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-223 |
3.44e-52 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 172.57 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYgkkgeKQYQaLKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:NF040840 2 IRIENLSKDW-----KEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:NF040840 72 RG--IAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-223 |
4.07e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 168.78 E-value: 4.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGkkgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfR 85
Cdd:COG3840 3 RLDDLTYRYG-------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALPLSlQNVK-TSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:COG3840 72 P--VSMLFQENNLFPHLTVAQNIGLGLR-PGLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAaRIADRVLLVADGRI 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-205 |
5.58e-52 |
|
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: 171.39 E-value: 5.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQP---TTGNVYINGRDITGLNKNQ 80
Cdd:COG0444 1 LLEVRNLKVYF-PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQEIGFIFQD-FNLLeN--LTNRENIALPLSL-QNVKTSAINPKVDKIAKRLGID---HILNKYPAEISGGQKQR 153
Cdd:COG0444 80 LRKIRGREIQMIFQDpMTSL-NpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDsksAT---ELLETMKGLNEKDKVSILMVTHD 205
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALD---VTiqaQILNLLKDLQRELGLAILFITHD 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-226 |
3.62e-51 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 166.49 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK10584 6 IVEVHHLKKSVGQ-GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-247 |
1.01e-50 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 169.11 E-value: 1.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSevVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnq 80
Cdd:PRK10851 1 MS--IEIANIKKSFGRT-----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfRGQEIGFIFQDFNLLENLTNRENIALPLSL----QNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:PRK10851 72 ----RDRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIG-----KEIKKD 230
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNIEqagtpDQVWRE 227
|
250
....*....|....*..
gi 489748581 231 GKSReeFYQEIIAELGR 247
Cdd:PRK10851 228 PATR--FVLEFMGEVNR 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-223 |
1.73e-50 |
|
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: 165.17 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKkGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdf 84
Cdd:cd03295 1 IEFENVTKRYGG-GKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGID--HILNKYPAEISGGQKQRVAAARALVH 162
Cdd:cd03295 75 --RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEI 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-237 |
8.09e-50 |
|
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: 164.55 E-value: 8.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQ--DFNLLENlTNRENIAL-PLSLqNVKTSAINPKVDKIAKRLGIDH-ILNKYPAEISGGQKQRVAAARAL 160
Cdd:TIGR04521 81 R-KKVGLVFQfpEHQLFEE-TVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKigkeIKKDGKSREEF 237
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGK----IVLDGTPREVF 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-246 |
1.18e-49 |
|
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: 163.76 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItgLNKNQMADF 84
Cdd:TIGR04520 1 IEVENVSFSYP---ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQ--DfNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:TIGR04520 76 R-KKVGMVFQnpD-NQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKigkeIKKDGKSREEFYQ-EI 241
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGK----IVAEGTPREIFSQvEL 229
|
....*
gi 489748581 242 IAELG 246
Cdd:TIGR04520 230 LKEIG 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-222 |
7.06e-49 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 158.70 E-value: 7.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:cd03228 1 IEFKNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDFNLLeNLTNRENIalplslqnvktsainpkvdkiakrlgidhilnkypaeISGGQKQRVAAARALVHEP 164
Cdd:cd03228 75 RKN-IAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTHDPYSASYASRILFIKDGK 222
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-223 |
1.64e-47 |
|
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: 156.69 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVaRGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLENLTNREN 107
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IA--LPLSLQNVKTSainpKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELL 185
Cdd:cd03297 96 LAfgLKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 489748581 186 ETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-223 |
1.95e-47 |
|
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: 166.93 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:COG2274 474 IELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDFNLLENlTNRENIAL---PLSLQnvktsainpKVDKIAKRLGIDHILNKYP-----------AEISGGQ 150
Cdd:COG2274 548 RRQ-IGVVLQDVFLFSG-TIRENITLgdpDATDE---------EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 151 KQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-223 |
3.65e-47 |
|
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: 154.52 E-value: 3.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfr 85
Cdd:cd03214 1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 gQEIGFIFQdfnllenltnreniALplslqnvktsainpkvdkiaKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:cd03214 73 -RKIAYVPQ--------------AL--------------------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAArYADRVILLKDGRI 176
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-173 |
1.57e-46 |
|
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: 152.03 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnknQMADFRGQEIGFIFQDFNLLENLTN 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD----DERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 105 RENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILN----KYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-205 |
3.41e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 154.63 E-value: 3.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVvQVQDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnknq 80
Cdd:COG4525 1 MSML-TVRHVSVRYPGGGQPQ-PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG4525 74 ----PGADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 161 VHEPAILYGDEPTGALDS---KSATELLETMKGLNEKdkvSILMVTHD 205
Cdd:COG4525 150 AADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGK---GVFLITHS 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-240 |
8.71e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 156.65 E-value: 8.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmad 83
Cdd:PRK09452 14 LVELRGISKSFDGK-----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 frgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:PRK09452 86 ---RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKigkeIKKDGKSReEFYQE 240
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGR----IEQDGTPR-EIYEE 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-223 |
3.09e-45 |
|
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: 150.72 E-value: 3.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 32 VARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnknqMADFRGQEIGFIFQDFNLLENLTNRENIALP 111
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT------AAPPADRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 112 LSlQNVKTSAIN-PKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKG 190
Cdd:cd03298 95 LS-PGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 489748581 191 LNEKDKVSILMVTHDPY-SASYASRILFIKDGKI 223
Cdd:cd03298 174 LHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-223 |
3.74e-45 |
|
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: 150.60 E-value: 3.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglNKNQMADF 84
Cdd:cd03266 2 ITADALTKRFRDV-KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVeRLCDRVVVLHRGRV 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-223 |
6.11e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 150.63 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlNKNQMAD 83
Cdd:PRK09493 1 MIEFKNVSKHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIAL-PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK09493 75 IR-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEiGFAEKVASRLIFIDKGRI 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-225 |
1.37e-44 |
|
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: 149.54 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrgqeigfIFQDFNLLENLTN 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLS--LQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSAT 182
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489748581 183 ELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDG---KIGK 225
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNGpaaNIGQ 198
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-223 |
1.38e-44 |
|
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: 149.24 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 29 SFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfrgQEIGFIFQDFNLLENLTNRENI 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 109 ALPLSlQNVKTSAI-NPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLET 187
Cdd:TIGR01277 92 GLGLH-PGLKLNAEqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 489748581 188 MKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-223 |
2.04e-44 |
|
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: 148.81 E-value: 2.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnkNQMADF 84
Cdd:cd03263 1 LQIRNLTKTYKKG---TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03263 74 R-QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGlnEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-223 |
5.12e-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: 148.10 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTL-----DQPTTGNVYINGRDITGLNKN 79
Cdd:cd03260 1 IELRDLNVYYGDK-----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADFRgqEIGFIFQDFNLLeNLTNRENIALPLSLQNVK-TSAINPKVDKIAKRLGI-DHILNKYPA-EISGGQKQRVAA 156
Cdd:cd03260 76 VLELRR--RVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTHDPYSASYAS-RILFIKDGKI 223
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVAdRTAFLLNGRL 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-205 |
5.81e-44 |
|
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: 147.97 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfR 85
Cdd:cd03219 2 EVRGLTKRFGG-----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALPLSLQNVKT----------SAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVA 155
Cdd:cd03219 76 G--IGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHD 205
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHD 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
5.84e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.31 E-value: 5.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnknq 80
Cdd:COG1121 3 MMPAIELENLTVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfRGQEIGFIFQDFNLlenltnreNIALPLSLQNV--------------KTSAINPKVDKIAKRLGIDHILNKYPAEI 146
Cdd:COG1121 73 ----ARRRIGYVPQRAEV--------DWDFPITVRDVvlmgrygrrglfrrPSRADREAVDEALERVGLEDLADRPIGEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 147 SGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSAS-YASRILFIKDGKIgk 225
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVReYFDRVLLLNRGLV-- 217
|
250 260
....*....|....*....|
gi 489748581 226 eikKDGKSREEFYQEIIAEL 245
Cdd:COG1121 218 ---AHGPPEEVLTPENLSRA 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
1.01e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.85 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSevVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDI---TGLN 77
Cdd:COG4161 1 MS--IQLKNINCFYG-----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMADFRgQEIGFIFQDFNLLENLTNREN-IALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:COG4161 74 EKAIRLLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEvEFARKVASQVVYMEKGRI 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-226 |
1.26e-43 |
|
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: 146.75 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnkNQMADF 84
Cdd:cd03265 1 IEVENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03265 72 R-RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIGKE 226
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAE 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-223 |
1.69e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 147.64 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDIT-------- 74
Cdd:COG4598 7 PALEVRDLHKSFG-----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 75 --GLNKNQMADFRGQeIGFIFQDFNLLENLTNREN-IALPLSLQNVktsainPKVDKIAK------RLGIDHILNKYPAE 145
Cdd:COG4598 82 lvPADRRQLQRIRTR-LGMVFQSFNLWSHMTVLENvIEAPVHVLGR------PKAEAIERaeallaKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 146 ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEmGFARDVSSHVVFLHQGRI 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-223 |
3.86e-43 |
|
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: 153.38 E-value: 3.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:COG4988 337 IELEDVSFSYPGGRP----ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD---PASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDFNLLeNLTNRENIALplslqnVKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQR 153
Cdd:COG4988 410 RRQ-IAWVPQNPYLF-AGTIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNeKDKvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGR-TVILITHRLALLAQADRILVLDDGRI 549
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-223 |
6.69e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.32 E-value: 6.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmADF 84
Cdd:COG1132 340 IEFENVSFSYP--GDRP--VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL---ESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDFNLLeNLTNRENIALPlslqnvKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQR 153
Cdd:COG1132 413 RRQ-IGVVPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNeKDKVSIlMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTI-VIAHRLSTIRNADRILVLDDGRI 552
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
7.99e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 7.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVqVQDITKTYgkKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTG-----NVYINGRDITG 75
Cdd:PRK11264 1 MSAIE-VKNLVKKF--HGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMADFRgQEIGFIFQDFNLLENLTNREN-IALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRV 154
Cdd:PRK11264 75 QQKGLIRQLR-QHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 155 AAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEmSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-237 |
1.32e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.95 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSevVQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNq 80
Cdd:PRK13637 1 MS--IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRgQEIGFIFQ--DFNLLENlTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDH--ILNKYPAEISGGQKQRVAA 156
Cdd:PRK13637 78 LSDIR-KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYS-ASYASRILFIKDGKigkeIKKDGKSRE 235
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGK----CELQGTPRE 231
|
..
gi 489748581 236 EF 237
Cdd:PRK13637 232 VF 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-205 |
1.68e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.79 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKG------EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLN 77
Cdd:COG4608 7 LLEVRDLKKHFPVRGglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMADFRgQEIGFIFQD-FNLLeN--LTNRENIALPLSLQNVKTSA-INPKVDKIAKRLGI--DHiLNKYPAEISGGQK 151
Cdd:COG4608 87 GRELRPLR-RRMQMVFQDpYASL-NprMTVGDIIAEPLRIHGLASKAeRRERVAELLELVGLrpEH-ADRYPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 152 QRVAAARALVHEPAILYGDEPTGALD-SKSAtELLETMKGLNEKDKVSILMVTHD 205
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDvSIQA-QVLNLLEDLQDELGLTYLFISHD 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-223 |
2.00e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.95 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 9 DITKTYgkkgekQYQALKgISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfrgQE 88
Cdd:PRK10771 6 DITWLY------HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 89 IGFIFQDFNLLENLTNRENIALPLSlQNVK-TSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAIL 167
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLN-PGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTH---DpySASYASRILFIKDGKI 223
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRI 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
2.01e-40 |
|
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: 145.60 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKT-TLLNILSTLDQP---TTGNVYINGRDITGL 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTV-EAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 77 NKNQMADFRGQEIGFIFQD----FNLLenLTNRENIALPLSL-QNVKTSAINPKVDKIAKRLGIDH---ILNKYPAEISG 148
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEpmtsLNPL--HTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 149 GQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
2.02e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.99 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSevVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDI---TGLN 77
Cdd:PRK11124 1 MS--IQLNGINCFYG-----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMADFRgQEIGFIFQDFNLLENLTNREN-IALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:PRK11124 74 DKAIRELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVArKTASRVVYMENGHI 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-222 |
2.21e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.22 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfR 85
Cdd:cd00267 1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQdfnllenltnrenialplslqnvktsainpkvdkiakrlgidhilnkypaeISGGQKQRVAAARALVHEPA 165
Cdd:cd00267 72 RRRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYAS-RILFIKDGK 222
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-215 |
5.43e-40 |
|
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: 136.84 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnKNQMAD 83
Cdd:COG4133 2 MLEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINpkVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:COG4133 73 YR-RRLAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYASRI 215
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGG-AVLLTTHQPLELAAARVL 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
7.56e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 7.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgkKGEKQYqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitgLNKNQ 80
Cdd:PRK13635 2 KEEIIRVEHISFRY--PDAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQeIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK13635 76 VWDVRRQ-VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-223 |
1.35e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.54 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnKNQMADFRGQEIGFIFQDFNLLENL 102
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRL-KNREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSAT 182
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489748581 183 ELLETMKGLNeKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK10908 175 GILRLFEEFN-RVGVTVLMATHDiGLISRRSYRMLTLSDGHL 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-226 |
1.41e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 137.41 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEV-VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGL--- 76
Cdd:PRK10619 1 MSENkLNVIDLHKRYG-----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 77 -------NKNQMADFRGQeIGFIFQDFNLLENLTNRENI------ALPLSLQNVKTSAInpkvdKIAKRLGIDH-ILNKY 142
Cdd:PRK10619 76 dgqlkvaDKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAV-----KYLAKVGIDErAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 143 PAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHD-PYSASYASRILFIKDG 221
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEmGFARHVSSHVIFLHQG 228
|
....*
gi 489748581 222 KIGKE 226
Cdd:PRK10619 229 KIEEE 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-240 |
1.88e-39 |
|
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: 138.78 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 40 IMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnkNQMADFRGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKT 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT----NVPPHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 120 SAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSI 199
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489748581 200 LMVTHDPYSA-SYASRILFIKDGKigkeIKKDGKSrEEFYQE 240
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGK----IAQIGTP-EEIYEE 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-223 |
2.50e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 135.79 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRgQEIGFIFQDFNLLeNLT 103
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIAlpLSLQNVKTSAINpkvdKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:cd03245 94 LRDNIT--LGAPLADDERIL----RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489748581 173 TGALDSKSATELLETMKGLNEKDkvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-230 |
6.86e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 135.58 E-value: 6.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVyINGRditglnkNQMADFRg 86
Cdd:PRK11247 15 LNAVSKRYG-----ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-------APLAEAR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQDFNLLENLTNRENIALPLSlqnvktSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAI 166
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 167 LYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIGKEIKKD 230
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIGLDLTVD 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-216 |
1.21e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.76 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLN-ILSTLDQP--TTGNVYINGRDITGLNKNQmadfRGqeIGFIFQDFNLLEN 101
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQ----RR--IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 102 LTNRENIALplslqnvktsAINPKVDKIAKR---------LGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:COG4136 91 LSVGENLAF----------ALPPTIGRAQRRarveqaleeAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 173 TGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRIL 216
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-223 |
1.65e-38 |
|
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: 133.55 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 16 KKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQP---TTGNVYINGRDitgLNKNQMADfrgqEIGFI 92
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPDQFQK----CVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 93 FQDFNLLENLTNRENI--ALPLSLQNVKTSAINPKVDKIA--KRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILY 168
Cdd:cd03234 87 RQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 169 GDEPTGALDSKSATELLETMKGLNEKDKVsILMVTHDPYSASYA--SRILFIKDGKI 223
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRI-VILTIHQPRSDLFRlfDRILLLSSGEI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-223 |
3.75e-38 |
|
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: 139.43 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKTY-GKKG-----EKQYQALKGISFDVARGEFVGIMGASGSGKTTL-LNILStLdQPTTGNVYINGRDITG 75
Cdd:COG4172 274 PLLEARDLKVWFpIKRGlfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR-L-IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMADFRgQEIGFIFQD-FNLLeN--LTNRENIALPLSLQNVKTSA--INPKVDKIAKRLGIDH-ILNKYPAEISGG 149
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQDpFGSL-SprMTVGQIIAEGLRVHGPGLSAaeRRARVAEALEEVGLDPaARHRYPHEFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDpYS--ASYASRILFIKDGKI 223
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD-LAvvRALAHRVMVMKDGKV 504
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-205 |
5.27e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 135.74 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknQMADf 84
Cdd:PRK11650 4 LKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:PRK11650 76 RD--IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489748581 165 AILYGDEPTGALDSK-SATELLETMKgLNEKDKVSILMVTHD 205
Cdd:PRK11650 154 AVFLFDEPLSNLDAKlRVQMRLEIQR-LHRRLKTTSLYVTHD 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-223 |
6.22e-38 |
|
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: 139.13 E-value: 6.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdf 84
Cdd:COG4987 334 LELEDVSFRYPGAGR---PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQD---FN--LLENLTnrenIAlplslqnvktsaiNPKVD-----KIAKRLGIDHILNKYP----------- 143
Cdd:COG4987 409 --RRIAVVPQRphlFDttLRENLR----LA-------------RPDATdeelwAALERVGLGDWLAALPdgldtwlgegg 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 144 AEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGR-TVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-223 |
7.58e-38 |
|
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: 135.62 E-value: 7.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLENLTNREN 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IALPLSLQNVKTSAINPkvDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLET 187
Cdd:TIGR02142 96 LRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 489748581 188 MKGLNEKDKVSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEvLRLADRVVVLEDGRV 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-223 |
7.63e-38 |
|
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: 135.61 E-value: 7.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitgLNKNQMADFRGQE---IGFIFQDFNLLENLTN 104
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFLPPHrrrIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENiaLPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:COG4148 95 RGN--LLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489748581 185 LETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
1.07e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.81 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK13632 7 MIKVENVSFSYP---NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FrgqeIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK13632 84 K----IGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-223 |
3.71e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.96 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmadfr 85
Cdd:cd03235 1 EVEDLTVSYG-----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 gqEIGFIFQDFNLLEN--LTNRENIALPL----SLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:cd03235 69 --RIGYVPQRRSIDRDfpISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLeYFDRVLLLNRTVV 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-204 |
5.73e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 5.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:COG1129 4 LLEMRGISKSFG--GVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 fRGqeIGFIFQDFNLLENLTNRENIAL---PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG1129 79 -AG--IAIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLneKDK-VSILMVTH 204
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRL--KAQgVAIIYISH 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-235 |
1.48e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 130.98 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKN----- 79
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 ----------------QMADFRGQeIGFIFQ--DFNLLENLTNRENIALPLSLQNVKTSAINpKVDKIAKRLGID-HILN 140
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRR-VGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 141 KYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIK 219
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVlEWTKRTIFFK 239
|
250
....*....|....*.
gi 489748581 220 DGKigkeIKKDGKSRE 235
Cdd:PRK13651 240 DGK----IIKDGDTYD 251
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-223 |
1.85e-36 |
|
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: 126.95 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGkkGEKQYQaLKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfR 85
Cdd:cd03246 2 EVENVSFRYP--GAEPPV-LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQDFNLLENlTNRENIalplslqnvktsainpkvdkiakrlgidhilnkypaeISGGQKQRVAAARALVHEPA 165
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNeKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-224 |
3.02e-36 |
|
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: 127.37 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnknqmADFR 85
Cdd:cd03226 1 RIENISFSYKKGTE----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQD--FNLLENLTNREniaLPLSLQNvkTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:cd03226 70 RKSIGYVMQDvdYQLFTDSVREE---LLLGLKE--LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKGLNEKDKVsILMVTHDP-YSASYASRILFIKDGKIG 224
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYeFLAKVCDRVLLLANGAIV 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-204 |
3.92e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 133.61 E-value: 3.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQ 80
Cdd:COG3845 2 MPPALELRGITKRFGGV-----VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGqeIGFIFQDFNLLENLTNRENIAL---PLSLQNVKTSAINPKVDKIAKRLG--IDhiLNKYPAEISGGQKQRVA 155
Cdd:COG3845 76 DAIALG--IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGldVD--PDAKVEDLSVGEQQRVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTH 204
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITH 199
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-205 |
5.41e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 128.42 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY-GKKG---EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGL 76
Cdd:COG4167 1 MSALLEVRNLSKTFkYRTGlfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 77 NknqmADFRGQEIGFIFQDFNllENLTNRENIA----LPLSLqNVKTSAI--NPKVDKIAKRLGI--DHiLNKYPAEISG 148
Cdd:COG4167 81 D----YKYRCKHIRMIFQDPN--TSLNPRLNIGqileEPLRL-NTDLTAEerEERIFATLRLVGLlpEH-ANFYPHMLSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 149 GQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-228 |
2.98e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.34 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTY---GKKGEKQYQA-LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQM 81
Cdd:PRK10419 5 NVSGLSHHYahgGLSGKHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 ADFRGqEIGFIFQD----FNllENLTNRENIALPLS-LQNVKTSAINPKVDKIAKRLGID-HILNKYPAEISGGQKQRVA 155
Cdd:PRK10419 85 KAFRR-DIQMVFQDsisaVN--PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKIGKEIK 228
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQP 235
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-223 |
3.31e-35 |
|
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: 132.30 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRGQeIGFIFQDFNLLeNLT 103
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID---PADLRRN-IGYVPQDPRLF-YGT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALPlslqnvktsaiNPKVD-----KIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAIL 167
Cdd:TIGR03375 555 LRDNIALG-----------APYADdeeilRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLNEkDKvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLA-GK-TLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-223 |
3.84e-35 |
|
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: 124.61 E-value: 3.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFvGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnKNQMADF 84
Cdd:cd03264 1 LQLENLTKRYGKK-----RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03264 71 R-RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMvTHDPYS-ASYASRILFIKDGKI 223
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILS-THIVEDvESLCNQVAVLNKGKL 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-202 |
3.98e-35 |
|
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: 124.85 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfR 85
Cdd:cd03224 2 EVENLNAGYGK-----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALplslqnvktSAINPKVDKIAKRlgIDHILNKYPA----------EISGGQKQRVA 155
Cdd:cd03224 76 G--IGYVPEGRRIFPELTVEENLLL---------GAYARRRAKRKAR--LERVYELFPRlkerrkqlagTLSGGEQQMLA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMV 202
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLV 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
6.29e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.51 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgkkgeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTL---DQPTTGNVYINGRDITglN 77
Cdd:PRK09984 1 MQTIIRVEKLAKTF-----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQ--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMA-DFRGQ--EIGFIFQDFNLLENLTNRENIAL------PLSLQNVK--TSAINPKVDKIAKRLGIDHILNKYPAEI 146
Cdd:PRK09984 74 EGRLArDIRKSraNTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 147 SGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
7-235 |
1.07e-34 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 124.33 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrg 86
Cdd:TIGR03864 4 VAGLSFRYGAR-----RALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 qEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAI 166
Cdd:TIGR03864 75 -RLGVVFQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 167 LYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKigkeIKKDGKSRE 235
Cdd:TIGR03864 154 LLLDEPTVGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGR----VLADGAAAE 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-246 |
1.28e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.20 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKGE-KQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglNKN 79
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEsTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADFRgQEIGFIFQD-FNLLENLTNRENIAL-PLSLqNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAA 157
Cdd:PRK13633 79 NLWDIR-NKAGMVFQNpDNQIVATIVEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKigkeIKKDGKSREEF 237
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGK----VVMEGTPKEIF 232
|
250
....*....|
gi 489748581 238 YQ-EIIAELG 246
Cdd:PRK13633 233 KEvEMMKKIG 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-223 |
1.98e-34 |
|
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: 123.60 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTY-------GKKGE---------KQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYI 68
Cdd:cd03267 1 IEVSNLSKSYrvyskepGLIGSlkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 69 NGRdITGLNKNQMAdfrgQEIGFIF-QDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEIS 147
Cdd:cd03267 81 AGL-VPWKRRKKFL----RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 148 GGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDiEALARRVLVIDKGRL 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-223 |
2.22e-34 |
|
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: 121.89 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKK-GEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILS--TLDQPTTGNVYINGRDITglnknq 80
Cdd:cd03213 3 TLSFRNLTVTVKSSpSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQeIGFIFQDFNLLENLTNRENIALPLSLQNvktsainpkvdkiakrlgidhilnkypaeISGGQKQRVAAARAL 160
Cdd:cd03213 77 KRSFRKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYSASYAS--RILFIKDGKI 223
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-223 |
2.79e-34 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 122.86 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 27 GISFDVARGEFVGIMGASGSGKT-TLLNILSTLDQPTT---GNVYINGRDITGLNknqmadFRGQEIGFIFQD----FNL 98
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPGLTqtsGEILLDGRPLLPLS------IRGRHIATIMQNprtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 LENLTN--RENIALPLSLQNVKTSAINPKVDKIakrlGIDH---ILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:TIGR02770 78 LFTMGNhaIETLRSLGKLSKQARALILEALEAV----GLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489748581 174 GALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASY-ASRILFIKDGKI 223
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARiADEVAVMDDGRI 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-204 |
3.79e-34 |
|
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: 122.65 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfRG 86
Cdd:cd03218 3 AENLSKRYGKR-----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-LG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 qeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAI 166
Cdd:cd03218 77 --IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 489748581 167 LYGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTH 204
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDH 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-216 |
3.84e-34 |
|
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: 128.56 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqmADFRGQEIGFIFQDFNLLENlT 103
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIAL------PLSLQNVKTSA-INPKVDkiAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGAL 176
Cdd:TIGR02857 412 IAENIRLarpdasDAEIREALERAgLDEFVA--ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489748581 177 DSKSATELLETMKGLNEkdKVSILMVTHDPYSASYASRIL 216
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIV 527
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-223 |
6.67e-34 |
|
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: 127.94 E-value: 6.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadfRGQEIGFIFQDFNLLENlTN 104
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE----LGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIA-LPlslqnvktsaiNPKVDKI---AKRLGI-DHIL---NKYPAEI-------SGGQKQRVAAARALVHEPAILYG 169
Cdd:COG4618 423 AENIArFG-----------DADPEKVvaaAKLAGVhEMILrlpDGYDTRIgeggarlSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489748581 170 DEPTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-223 |
8.45e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.83 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:PRK11432 7 VVLKNITKRFGSN-----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:PRK11432 78 --RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYAS-RILFIKDGKI 223
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSdTVIVMNKGKI 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
1.05e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.12 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadf 84
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDfNLL---ENLTNRENIAL------PLSLqnvkTSAINPKV-----DKIAK-RLGIDHILNKYPAEISGG 149
Cdd:COG1101 78 RAKYIGRVFQD-PMMgtaPSMTIEENLALayrrgkRRGL----RRGLTKKRrelfrELLATlGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIGKEIK 228
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGRIILDVS 232
|
....*.
gi 489748581 229 KDGKSR 234
Cdd:COG1101 233 GEEKKK 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-224 |
1.47e-33 |
|
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: 121.34 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 2 SEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGN-VYINGRDITGLNknq 80
Cdd:COG1119 1 DPLLELRNVTVRRGGK-----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRgQEIGFIFQDfnLLENLTNREN------------IALPlslQNVKTSAINpKVDKIAKRLGIDHILNKYPAEISG 148
Cdd:COG1119 73 VWELR-KRIGLVSPA--LQLRFPRDETvldvvlsgffdsIGLY---REPTDEQRE-RARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 149 GQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHdpysasYA-------SRILFIKDG 221
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVeeippgiTHVLLLKDG 219
|
...
gi 489748581 222 KIG 224
Cdd:COG1119 220 RVV 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-206 |
1.76e-33 |
|
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: 120.62 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYG--KKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGR----DIT 74
Cdd:COG4778 1 MTTLLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 75 GLNKNQMADFRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHIL-NKYPAEISGGQKQR 153
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKS---ATELLETMKglneKDKVSILMVTHDP 206
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAK----ARGTAIIGIFHDE 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-242 |
2.85e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.79 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgkkgEKQYqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF----DGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfrgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:PRK11607 91 ------RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 161 VHEPAILYGDEPTGALDSKSATEL-LETMKGLnEKDKVSILMVTHDPYSA-SYASRILFIKDGK---IG--KEIKKDGKS 233
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMqLEVVDIL-ERVGVTCVMVTHDQEEAmTMAGRIAIMNRGKfvqIGepEEIYEHPTT 243
|
....*....
gi 489748581 234 ReeFYQEII 242
Cdd:PRK11607 244 R--YSAEFI 250
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-223 |
4.22e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.65 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMA 82
Cdd:PRK13548 1 AMLEARNLSVRLGGR-----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 DFRG---QE--IGFIFqdfnllenlTNRENIAL---PLSLQNVKTSAInpkVDKIAKRLGIDHILNKYPAEISGGQKQRV 154
Cdd:PRK13548 76 RRRAvlpQHssLSFPF---------TVEEVVAMgraPHGLSRAEDDAL---VAAALAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 155 AAARALV------HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-244 |
4.39e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY-----------------GKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTT 63
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 64 GNVYINGRdITGLnknqmadfrgQEIGFIFQdfnllENLTNRENIALPLSLQNVKTSAINPKVDKIAK--RLG--IDHIL 139
Cdd:COG1134 81 GRVEVNGR-VSAL----------LELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEfaELGdfIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 140 NKYpaeiSGGQKQRVAAARALVHEPAILYGDEPTGALDS---KSATELLETMKglneKDKVSILMVTHDPYS-ASYASRI 215
Cdd:COG1134 145 KTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARIRELR----ESGRTVIFVSHSMGAvRRLCDRA 216
|
250 260 270
....*....|....*....|....*....|.
gi 489748581 216 LFIKDGKigkeIKKDGKSRE--EFYQEIIAE 244
Cdd:COG1134 217 IWLEKGR----LVMDGDPEEviAAYEALLAG 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-223 |
6.15e-33 |
|
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: 119.25 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 19 EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrgQEIGFIFQDFNL 98
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR----SMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 LENlTNRENIALPlslqnvKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAIL 167
Cdd:cd03254 89 FSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLNeKDKVSIlMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLM-KGRTSI-IIAHRLSTIKNADKILVLDDGKI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-223 |
1.01e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 122.06 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRditglnknQMADF 84
Cdd:PRK11000 4 VTLRNVTKAYG-----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--------RMNDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 ----RGqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:PRK11000 71 ppaeRG--VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-223 |
1.09e-32 |
|
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: 116.76 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADf 84
Cdd:cd03216 1 LELRGITKRFG-----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGqeIGFIFQdfnllenltnrenialplslqnvktsainpkvdkiakrlgidhilnkypaeISGGQKQRVAAARALVHEP 164
Cdd:cd03216 75 AG--IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-223 |
1.27e-32 |
|
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: 118.87 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknQMADFRgQEIGFIFQDfNLLENL 102
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLR-RAIGVVPQD-TVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIALPlslqnvKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:cd03253 90 TIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489748581 172 PTGALDSKSATELLETMKGLNeKDKVSIlMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVS-KGRTTI-VIAHRLSTIVNADKIIVLKDGRI 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-205 |
2.00e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.45 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYG-KKG----EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITG 75
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvKRGlfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMADFRgQEIGFIFQdfNLLENLTNRENI----ALPLslqnvktsAINPKVDKIAKRLGIDHILNK---------- 141
Cdd:PRK11308 82 ADPEAQKLLR-QKIQIVFQ--NPYGSLNPRKKVgqilEEPL--------LINTSLSAAERREKALAMMAKvglrpehydr 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 142 YPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-223 |
2.38e-32 |
|
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: 117.38 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRditglnknQMADF 84
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03269 68 ARNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEeLCDRVLLLNKGRA 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-247 |
6.69e-32 |
|
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: 116.82 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMadfRGQeIGFIFQDfNLLENLT 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQ-VGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALP---LSLQNVKTSA-INPKVDKIAK-RLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDS 178
Cdd:cd03252 92 IRDNIALAdpgMSMERVIEAAkLAGAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 179 KSATELLETMKGLNekDKVSILMVTHDPYSASYASRILFIKDGKigkeIKKDGKsreefYQEIIAELGR 247
Cdd:cd03252 172 ESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGR----IVEQGS-----HDELLAENGL 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
8.26e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.14 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFR 85
Cdd:COG4559 3 EAENLSVRLGGR-----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 G---Q--EIGFIFqdfnllenlTNRENIAL---PLSLQNVKTSAInpkVDKIAKRLGIDHILNKYPAEISGGQKQRVAAA 157
Cdd:COG4559 78 AvlpQhsSLAFPF---------TVEEVVALgraPHGSSAAQDRQI---VREALALVGLAHLAGRSYQTLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 158 RAL--VHEPA-----ILYGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG4559 146 RVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDlNLAAQYADRILLLHQGRL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
1.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgkKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknq 80
Cdd:PRK13650 1 MSNIIEVKNLTFKY--KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRgQEIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK13650 76 VWDIR-HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-204 |
1.93e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 116.29 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTL-----DQPTTGNVYINGRDITG 75
Cdd:COG1117 8 LEPKIEVRNLNVYYGDK-----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMAdFRgQEIGFIFQDFNLLeNLTNRENIALPLSLQNVKTSAinpKVDKIA----KRLGI-DHI---LNKYPAEIS 147
Cdd:COG1117 83 PDVDVVE-LR-RRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKS---ELDEIVeeslRKAALwDEVkdrLKKSALGLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 148 GGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTH 204
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTH 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-223 |
2.39e-31 |
|
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: 115.41 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknQMADF 84
Cdd:cd03251 1 VEFKNVTFRYPGDGPP---VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDfNLLENLTNRENIA---LPLSLQNVKTSAINPKVDKIAKRL--GIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:cd03251 75 RRQ-IGLVSQD-VFLFNDTVAENIAygrPGATREEVEEAARAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILmVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERL-MKNRTTFV-IAHRLSTIENADRIVVLEDGKI 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-223 |
2.71e-31 |
|
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: 115.33 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNqmaDFRGQeIGFIFQDFNLLENl 102
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLR---WLRSQ-IGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIALPlslqnvKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:cd03249 92 TIAENIRYG------KPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489748581 172 PTGALDSKSATELLETmkgLNE--KDKVSIlMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03249 166 ATSALDAESEKLVQEA---LDRamKGRTTI-VIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-223 |
3.01e-31 |
|
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: 113.56 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNqmadf 84
Cdd:cd03247 1 LSINNVSFSYP---EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQDFNLLeNLTNRENIALPLSlqnvktsainpkvdkiakrlgidhilnkypaeisGGQKQRVAAARALVHEP 164
Cdd:cd03247 73 LSSLISVLNQRPYLF-DTTLRNNLGRRFS----------------------------------GGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 165 AILYGDEPTGALDSKSATELLETM-KGLNEKdkvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-223 |
6.92e-31 |
|
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: 119.37 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 13 TYGKKGEKQYqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMadfrGQEIGFI 92
Cdd:TIGR01842 323 TIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF----GKHIGYL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 93 FQDFNLLENlTNRENIAL---PLSLQNVKTSAINPKVDKIAKRL--GIDHILNKYPAEISGGQKQRVAAARALVHEPAIL 167
Cdd:TIGR01842 398 PQDVELFPG-TVAENIARfgeNADPEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-172 |
1.36e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.59 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfR 85
Cdd:COG1137 5 EAENLVKSYGKR-----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:COG1137 79 G--IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
....*..
gi 489748581 166 ILYGDEP 172
Cdd:COG1137 157 FILLDEP 163
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-227 |
2.80e-30 |
|
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: 111.93 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnKNQMADF 84
Cdd:cd03268 1 LKTNDLTKTYGKK-----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ---KNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAInpkvDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03268 73 R---IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYS-ASYASRILFIKDGKIGKEI 227
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGI-TVLISSHLLSEiQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-223 |
3.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQ--DFNLLENLTNRENIALP----LSLQNVKTSAInpkvdKIAKRLGID-HILNKYPAEISGGQKQRVAAA 157
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPknfkMNLDEVKNYAH-----RLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-237 |
3.42e-30 |
|
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: 112.38 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfR 85
Cdd:COG0410 5 EVENLHAGYGG-----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALPLslqnvktsAINPKVDKIAKRLgiDHILNKYP--AE--------ISGGQKQRVA 155
Cdd:COG0410 79 G--IGYVPEGRRIFPSLTVEENLLLGA--------YARRDRAEVRADL--ERVYELFPrlKErrrqragtLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMVTHDPYSA-SYASRILFIKDGKI-----GKEIKK 229
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFAlEIADRAYVLERGRIvlegtAAELLA 225
|
....*...
gi 489748581 230 DGKSREEF 237
Cdd:COG0410 226 DPEVREAY 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-205 |
3.50e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 114.80 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQY--------QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITG 75
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKQWfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMADFRgQEIGFIFQDfnLLENLTNR----ENIALPL-------SLQNVKTsainpKVDKIAKRLGI-DHILNKYP 143
Cdd:PRK15079 88 MKDDEWRAVR-SDIQMIFQD--PLASLNPRmtigEIIAEPLrtyhpklSRQEVKD-----RVKAMMLKVGLlPNLINRYP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 144 AEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
4.74e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.56 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQ-----PTTGNVYINGRDITG 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKK-----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 76 LNKNQMaDFRgQEIGFIFQDFNLLEnLTNRENIALPLSLQNVKTSAI-NPKVDKIAKRLGI-----DHiLNKYPAEISGG 149
Cdd:PRK14239 77 PRTDTV-DLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdevkDR-LHDSALGLSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTHdpySASYASRI 215
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-237 |
5.44e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 5.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQMAD 83
Cdd:PRK13639 1 ILETRDLKYSY----PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQDF-NLLENLTNRENIAL-PLSLqNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALV 161
Cdd:PRK13639 76 VR-KTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHDPYSAS-YASRILFIKDGKIGKEikkdGKSREEF 237
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPvYADKVYVMSDGKIIKE----GTPKEVF 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-205 |
7.18e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 21 QYQALKGISFDVARGEFVGIMGASGSGK-TTLLNILSTLdqPTTGNVYINGRDITGLNKNQMADFRGQeIGFIFQDFN-- 97
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 98 LLENLTNRENIALPLSLQNVKTSAI--NPKVDKIAKRLGIDHIL-NKYPAEISGGQKQRVAAARALVHEPAILYGDEPTG 174
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAqrEQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|.
gi 489748581 175 ALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-237 |
8.30e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 8 QDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKN-QMADFRg 86
Cdd:PRK13634 6 QKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkKLKPLR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQ--DFNLLENlTNRENIAL-PLSLqNVKTSAINPKVDKIAKRLGIDH-ILNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEE-TVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTH---DpySASYASRILFIKDGKigkeIKKDGKSREEF 237
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGT----VFLQGTPREIF 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-223 |
9.65e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.75 E-value: 9.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLENLT 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATE 183
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489748581 184 LLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEV 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-205 |
1.69e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.94 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnknqmadfR 85
Cdd:PRK11248 3 QISHLYADYGGK-----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:PRK11248 69 GAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-205 |
2.98e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmadFRgQEIGFIFQDFNLLENlTN 104
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YR-QQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNVKtsainPKVDKIAK---RLGI-DHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKS 180
Cdd:PRK10247 98 YDNLIFPWQIRNQQ-----PDPAIFLDdleRFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*
gi 489748581 181 ATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-204 |
2.99e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 112.66 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 40 IMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitgLNKNQMADFRGQE---IGFIFQDFNLLENLTNRENialplsLQN 116
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKGICLPPEkrrIGYVFQDARLFPHYKVRGN------LRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 117 VKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDK 196
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
....*...
gi 489748581 197 VSILMVTH 204
Cdd:PRK11144 180 IPILYVSH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-225 |
5.67e-29 |
|
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: 114.13 E-value: 5.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYIN-GRDITGLNKNQM 81
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 aDFRG---QEIGFIFQDFNL------LENLTNRENIALPLSLQNVKtSAINPKV----DKIAKrlgidHILNKYPAEISG 148
Cdd:TIGR03269 358 -DGRGrakRYIGILHQEYDLyphrtvLDNLTEAIGLELPDELARMK-AVITLKMvgfdEEKAE-----EILDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 149 GQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKIGK 225
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIVK 508
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
5.86e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 5.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 2 SEVVQVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQM 81
Cdd:PRK13636 3 DYILKVEELNYNYSDGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 aDFRgQEIGFIFQD-FNLLENLTNRENIAL-PLSLQnVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK13636 79 -KLR-ESVGMVFQDpDNQLFSASVYQDVSFgAVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
9.30e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 9.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY-KDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MadfRGQeIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK13647 77 V---RSK-VGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDvDLAAEWADQVIVLKEGRV 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
3.68e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.26 E-value: 3.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknq 80
Cdd:PRK13642 1 MNKILEVENLVFKYEK--ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRgQEIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK13642 76 VWNLR-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-247 |
4.95e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.59 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:PRK13657 335 VEFDDVSFSYDNSR----QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLeNLTNRENIALPlslqnvKTSAINPKVDKIAKR-----------LGIDHILNKYPAEISGGQKQR 153
Cdd:PRK13657 408 R-RNIAVVFQDAGLF-NRSIEDNIRVG------RPDATDEEMRAAAERaqahdfierkpDGYDTVVGERGRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDskSATE------LLETMKGLnekdkvSILMVTHDPYSASYASRILFIKDGKIgkeI 227
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALD--VETEakvkaaLDELMKGR------TTFIIAHRLSTVRNADRILVFDNGRV---V 548
|
250 260
....*....|....*....|
gi 489748581 228 KKDGksreefYQEIIAELGR 247
Cdd:PRK13657 549 ESGS------FDELVARGGR 562
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
1.29e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.48 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTY-------GKKG--------EKQY-QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVY 67
Cdd:COG4586 1 IIEVENLSKTYrvyekepGLKGalkglfrrEYREvEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 68 INGRDItglNKNQMAdFRGQeIGFIF-QDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKyPA-E 145
Cdd:COG4586 81 VLGYVP---FKRRKE-FARR-IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 146 ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDiEALCDRVIVIDHGRI 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-223 |
1.75e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 110.14 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 16 KKGEKQYqaLKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTT---GNVYINGRDItglNKNQMadfrgQEI-GF 91
Cdd:TIGR00955 34 ERPRKHL--LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI---DAKEM-----RAIsAY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 92 IFQDFNLLENLTNRE--NIALPLSLQ-NVKTSAINPKVDKIAKRLGI---DHILNKYPAE---ISGGQKQRVAAARALVH 162
Cdd:TIGR00955 104 VQQDDLFIPTLTVREhlMFQAHLRMPrRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYA--SRILFIKDGKI 223
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFElfDKIILMAEGRV 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-225 |
2.53e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.81 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNq 80
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVP--VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madFRGQEIGFIFQDfNLLENLTNRENIALPLslqnvkTSAINPKVDKIAKRLGIDHILNKYPAEI-----------SGG 149
Cdd:TIGR00958 552 ---YLHRQVALVGQE-PVLFSGSVRENIAYGL------TDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgekgsqlSGG 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKglnEKDKvSILMVTHDPYSASYASRILFIKDGKIGK 225
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASR-TVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-223 |
2.84e-27 |
|
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: 104.54 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 15 GKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRD--ITGLNknqmadfrgqeIGFi 92
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLGLG-----------GGF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 93 fqdfnlLENLTNRENIALPLSLQNVKTSAINPKVDKIAK--RLG--IDHILNKYpaeiSGGQKQRVAAARALVHEPAILY 168
Cdd:cd03220 96 ------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELGdfIDLPVKTY----SSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 169 GDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYS-ASYASRILFIKDGKI 223
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSiKRLCDRALVLEKGKI 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-223 |
3.82e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.01 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYG-----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MAD------FRGqEIGFIFQD--FNLLENLTNRENIALPLSLQ------NVKTSAIN--PKVDKIAKRlgIDHIlnkyPA 144
Cdd:PRK11701 78 LSEaerrrlLRT-EWGFVHQHprDGLRMQVSAGGNIGERLMAVgarhygDIRATAGDwlERVEIDAAR--IDDL----PT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 145 EISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGRV 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-237 |
6.62e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 104.22 E-value: 6.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTL-----DQPTTGNVYINGRDITglnK 78
Cdd:PRK14247 3 KIEIRDLKVSFG-----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF---K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 79 NQMADFRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSA------INPKVDKIAKRLGIDHILNKYPAEISGGQKQ 152
Cdd:PRK14247 75 MDVIELR-RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkelqerVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLETMkgLNEKDKVSILMVTHDPYSASYASR-ILFIKDGKIGKEikkdG 231
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLF--LELKKDMTIVLVTHFPQQAARISDyVAFLYKGQIVEW----G 227
|
....*.
gi 489748581 232 KSREEF 237
Cdd:PRK14247 228 PTREVF 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-223 |
1.49e-26 |
|
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: 103.37 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:TIGR02323 3 LLQVSGLSKSYGGG-----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQ-----EIGFIFQdfNLLENLTNR----ENIA-LPLSLQNVKTSAINPKVDKIAKRLGIDHI-LNKYPAEISGGQKQ 152
Cdd:TIGR02323 78 AERRrlmrtEWGFVHQ--NPRDGLRMRvsagANIGeRLMAIGARHYGNIRATAQDWLEEVEIDPTrIDDLPRAFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRV 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-223 |
1.96e-26 |
|
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: 102.22 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfR 85
Cdd:TIGR03410 2 EVSNLNVYYG-----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAInpkvdkiakrlgIDHILNKYPA----------EISGGQKQRVA 155
Cdd:TIGR03410 76 G--IAYVPQGREIFPRLTVEENLLTGLAALPRRSRKI------------PDEIYELFPVlkemlgrrggDLSGGQQQQLA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMV-THDPYSASYASRILFIKDGKI 223
Cdd:TIGR03410 142 IARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-243 |
2.80e-26 |
|
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: 101.71 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnKNQMADfr 85
Cdd:TIGR03740 2 ETKNLSKRFGKQ-----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDLHK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 gqeIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPkvdkIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:TIGR03740 72 ---IGSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHDPYSASY-ASRILFIKDGKIGKEIKKDGKSR-EEFYQEIIA 243
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQG-ITVILSSHILSEVQQlADHIGIISEGVLGYQGKINKSENlEKLFVEVVK 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-206 |
2.87e-26 |
|
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: 106.29 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrgQEIGFIFQDFNLLENlT 103
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALplslqnVKTSAINPKVDKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:TIGR02868 425 VRENLRL------ARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*
gi 489748581 173 TGALDSKSATELLETM-KGLNEKdkvSILMVTHDP 206
Cdd:TIGR02868 499 TEHLDAETADELLEDLlAALSGR---TVVLITHHL 530
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-235 |
3.69e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ--- 80
Cdd:COG4152 1 MLELKGLTKRFGDK-----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGqeigfifqdfnLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:COG4152 76 LPEERG-----------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIKDGKI---GK--EIKKDGKSR 234
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVeELCDRIVIINKGRKvlsGSvdEIRRQFGRN 223
|
.
gi 489748581 235 E 235
Cdd:COG4152 224 T 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-225 |
6.16e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 21 QYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ-MADFRgQEIGFIFQ--DFN 97
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKKLR-KKVSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 98 LLENlTNRENIAL-PLSL----QNVKTSAInpkvdKIAKRLGI-DHILNKYPAEISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:PRK13641 98 LFEN-TVLKDVEFgPKNFgfseDEAKEKAL-----KWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 172 PTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYS-ASYASRILFIKDGKIGK 225
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDvAEYADDVLVLEHGKLIK 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-223 |
6.35e-26 |
|
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: 101.01 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQmad 83
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTL--VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENlTNRENIALPL---SLQNVKTSAINPKVDKIAKRL--GIDHILNKYPAEISGGQKQRVAAAR 158
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYGLqscSFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 159 ALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVsiLMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-223 |
7.59e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQmaDFRgQEIGFIFQD-------F 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ--GIR-KLVGIVFQNpetqfvgR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 97 NLLENLT-NRENIALPlslqnvkTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGA 175
Cdd:PRK13644 94 TVEEDLAfGPENLCLP-------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 176 LDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-222 |
1.10e-25 |
|
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: 99.85 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLN-ILSTLdQPTTGNVYINGRditglnknqmad 83
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 frgqeIGFIFQdFNLLENLTNRENIALPLSLQN------VKTSAINPKVDKIAKRL-------GIDhilnkypaeISGGQ 150
Cdd:cd03250 68 -----IAYVSQ-EPWIQNGTIRENILFGKPFDEeryekvIKACALEPDLEILPDGDlteigekGIN---------LSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 151 KQRVAAARALVHEPAILYGDEPTGALDSKSATELLET-MKGLNEKDKVSILmVTHDPYSASYASRILFIKDGK 222
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRIL-VTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-236 |
1.26e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 21 QYQ-----ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNqmaDFRgQEIGFIFQD 95
Cdd:PRK13648 16 QYQsdasfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE---KLR-KHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 -FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTG 174
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 175 ALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGK-----EIKKDGKSREE 236
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKegtptEIFDHAEELTR 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-223 |
2.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADF 84
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGFIFQ--DFNLLENlTNRENIALplSLQNVKTSAInpKVDKIAKR----LGIDHIL-NKYPAEISGGQKQRVAAA 157
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAF--GPQNFGVSQE--EAEALAREklalVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMVTH--DPYsASYASRILFIKDGKI 223
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHlmDDV-ANYADFVYVLEKGKL 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-203 |
2.47e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY----GKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgl 76
Cdd:PRK15112 1 VETLLEVRNLSKTFryrtGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 77 nknqMAD--FRGQEIGFIFQDFNllENLTNRENIA----LPLSLQ-NVKTSAINPKVDKIAKRLGI--DHIlNKYPAEIS 147
Cdd:PRK15112 79 ----FGDysYRSQRIRMIFQDPS--TSLNPRQRISqildFPLRLNtDLEPEQREKQIIETLRQVGLlpDHA-SYYPHMLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 148 GGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVT 203
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-240 |
2.50e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgkKGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK13652 3 LIETRDLCYSY--SGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FrgqeIGFIFQDFN-LLENLTNRENIAL-PLSLqNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALV 161
Cdd:PRK13652 79 F----VGLVFQNPDdQIFSPTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKIGKEikkdGKSREEFYQE 240
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY----GTVEEIFLQP 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-245 |
3.76e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.06 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVV---QVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLN 77
Cdd:PRK10253 1 MTESVarlRGEQLTLGYGK-----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMAdfrgQEIGFIFQDFNLLENLTNRENIA------LPLSLQNVKTSAinPKVDKIAKRLGIDHILNKYPAEISGGQK 151
Cdd:PRK10253 76 SKEVA----RRIGLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 152 QRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKIGKEikkd 230
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ---- 225
|
250
....*....|....*
gi 489748581 231 GKSREEFYQEIIAEL 245
Cdd:PRK10253 226 GAPKEIVTAELIERI 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-223 |
4.21e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrg 86
Cdd:PRK11231 5 TENLTVGYGTK-----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQDFNLLENLTNRENIAL---P-LSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASrYCDHLVVLANGHV 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-223 |
4.43e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.39 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLN-ILSTLdqPTTGNVYINGRDITGLNknqMADFRgQEIGFIFQDFNLLEN 101
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD---PESWR-KHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 102 lTNRENIAL---PLSLQNVKTSAINPKVDKIAKRL--GIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGAL 176
Cdd:PRK11174 438 -TLRDNVLLgnpDASDEQLQQALENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 177 DSKSATELletMKGLNE-KDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK11174 517 DAHSEQLV---MQALNAaSRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-223 |
4.87e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMadfrGQEIGFIFQDFNLLENLTN 104
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIAL---P-LSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKS 180
Cdd:PRK09536 95 RQVVEMgrtPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 181 ATELLETMKGLNEKDKVSILMVtHD-PYSASYASRILFIKDGKI 223
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAI-HDlDLAARYCDELVLLADGRV 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-237 |
7.47e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.76 E-value: 7.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTL-----DQPTTGNVYINGRDITGLNKNQMADFRgqEIGFIFQDFNLL 99
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRR--EVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 100 ENLTNRENIALPLSLQNVKTSA--INPKVDKIAKRLGI-DHI---LNKYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKkeLDERVEWALKKAALwDEVkdrLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 174 GALDSKSATELLETMKGLneKDKVSILMVTHDPYSASYASR-ILFIKDGKIgKEIkkdGKSREEF 237
Cdd:PRK14267 178 ANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDyVAFLYLGKL-IEV---GPTRKVF 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-223 |
1.05e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINgrditglnknqmadfRG 86
Cdd:COG0488 1 LENLSKSFGGR-----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQDFNLLENLTNRENI-------------------ALPLSLQNVKTSA-------------INPKVDKIAKRLG 134
Cdd:COG0488 61 LRIGYLPQEPPLDDDLTVLDTVldgdaelraleaeleeleaKLAEPDEDLERLAelqeefealggweAEARAEEILSGLG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 135 IDHI-LNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSaTELLETMkgLNEKDKvSILMVTHDPY---SAs 210
Cdd:COG0488 141 FPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-IEWLEEF--LKNYPG-TVLVVSHDRYfldRV- 215
|
250
....*....|...
gi 489748581 211 yASRILFIKDGKI 223
Cdd:COG0488 216 -ATRILELDRGKL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-223 |
1.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.72 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYgKKGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK13640 5 IVEFKHVSFTY-PDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRgQEIGFIFQD-FNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK13640 82 IR-EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-223 |
1.45e-24 |
|
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: 95.96 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmADFRGQEIGFIFQD---FNLLE 100
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RDAIRAGIAYVPEDrkrEGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 101 NLTNRENIALPLSLqnvktsainpkvdkiakrlgidhilnkypaeiSGGQKQRVAAARALVHEPAILYGDEPTGALDSKS 180
Cdd:cd03215 92 DLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 181 ATELLETMKGLNEKDKvSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:cd03215 140 KAEIYRLIRELADAGK-AVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-247 |
2.00e-24 |
|
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: 101.03 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQ--PTTGNV-----------YIN-- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGK-----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgYVErp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 70 ---GR--------------DITGLNKNQMADFRgQEIGFIFQ-DFNLLENLTNRENI--ALPlSLQNVKTSAINPKVDKI 129
Cdd:TIGR03269 76 skvGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVleALE-EIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 130 aKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP-YS 208
Cdd:TIGR03269 154 -EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489748581 209 ASYASRILFIKDGkigkEIKKDGKSRE--EFYQEIIAELGR 247
Cdd:TIGR03269 233 EDLSDKAIWLENG----EIKEEGTPDEvvAVFMEGVSEVEK 269
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-216 |
2.83e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGrditglnknqmadfrGQEIGFIFQDFNLLENL- 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 -TNRENIAL----PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALD 177
Cdd:NF040873 72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 489748581 178 SKSATELLETMKGLNEkDKVSILMVTHDPYSASYASRIL 216
Cdd:NF040873 152 AESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCV 189
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-239 |
7.36e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.49 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKT----TLLNILSTlDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQD---- 95
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 FN--------LLENLTNRENIAlplslqnvKTSAINP--------KVDKIAKRLGIdhilnkYPAEISGGQKQRVAAARA 159
Cdd:PRK09473 110 LNpymrvgeqLMEVLMLHKGMS--------KAEAFEEsvrmldavKMPEARKRMKM------YPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKigkeIKKDGKSREEFY 238
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR----TMEYGNARDVFY 251
|
.
gi 489748581 239 Q 239
Cdd:PRK09473 252 Q 252
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-222 |
1.03e-23 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 99.57 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPT--TGNVYINGRDITglnKNQMadfrgQEIGFIFQDFNLLENL 102
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT---KQIL-----KRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIA------LPLSL-QNVKTSAinpkVDKIAKRLGIDH-----ILNKYPAEISGGQKQRVAAARALVHEPAILYGD 170
Cdd:PLN03211 156 TVRETLVfcsllrLPKSLtKQEKILV----AESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489748581 171 EPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYA--SRILFIKDGK 222
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-205 |
3.20e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.85 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 16 KKGEKQYQALKGISFDVARGEFVGIMGASGSGKT-TLLNILSTLDQP----TTGNVYINGRDITGLNKNQMADFRGQEIG 90
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 91 FIFQD----FNLLENLtnRENIALPLSL-QNVKTSAINPKVDKIAKRLGIDHI---LNKYPAEISGGQKQRVAAARALVH 162
Cdd:PRK15134 96 MIFQEpmvsLNPLHTL--EKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAakrLTDYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489748581 163 EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-189 |
3.38e-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: 97.97 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmADFRGQeIGFIFQDfNLLENL 102
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ---ASLRAA-IGIVPQD-TVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIALPlslqnvKTSAINPKVDKIAKRLGIDHILNKYPA-----------EISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:COG5265 447 TIAYNIAYG------RPDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170
....*....|....*...
gi 489748581 172 PTGALDSKSATELLETMK 189
Cdd:COG5265 521 ATSALDSRTERAIQAALR 538
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-204 |
3.46e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.67 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRGQEIGFIFQDFNLLENL 102
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS---TTAALAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENI---ALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSK 179
Cdd:PRK11288 95 TVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180
....*....|....*....|....*
gi 489748581 180 SATELLETMKGLNEKDKVsILMVTH 204
Cdd:PRK11288 175 EIEQLFRVIRELRAEGRV-ILYVSH 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
4.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYI----------NGRD 72
Cdd:PRK13631 20 IILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 73 ITGLNKNQMADFRG--QEIGFIFQ--DFNLLENLTNRENIALPLSLQNVKTSAiNPKVDKIAKRLGIDH-ILNKYPAEIS 147
Cdd:PRK13631 100 ITNPYSKKIKNFKElrRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA-KKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 148 GGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTH 204
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITH 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-222 |
1.03e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.46 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 2 SEVVQVQDITKTYgKKGEKQYQALKGISFDVARGEFVGIMGASGSGKT-TLLNILSTLDQpTTGNVYING-------RDI 73
Cdd:PRK10261 10 RDVLAVENLNIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 74 TGLNKN---QMADFRGQEIGFIFQD--FNLLENLTNRENIALPLSL-QNVKTSAINPKVDKIAKRLGI---DHILNKYPA 144
Cdd:PRK10261 88 IELSEQsaaQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPH 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 145 EISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGK 222
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-223 |
1.09e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmADF 84
Cdd:PRK11160 339 LTLNNVSFTYP---DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLeNLTNRENIALplslqnVKTSAINPKVDKIAKRLGIDHILNKYPA----------EISGGQKQRV 154
Cdd:PRK11160 413 R-QAISVVSQRVHLF-SATLRDNLLL------AAPNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 155 AAARALVHEPAILYGDEPTGALDSKSATELLETmkgLNE--KDKvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILEL---LAEhaQNK-TVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-237 |
1.19e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQ------PTTGNVYINGRDITGLNKNQMAdfrgQEIGFIFQDFNL 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 LENLTNRENIALPLSLQNVKTS-AINPKVDKIAKRLG----IDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 174 GALDSKSATELLETMKGLneKDKVSILMVTHDPYSAS-YASRILFIKDGkigkEIKKDGKSREEF 237
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVArVADYVAFLYNG----ELVEWGSSNEIF 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-237 |
1.35e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 94.04 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGeKQYQALKGISFDVARGEFVGIMGASGSGKT-TLLNILSTLDQP---TTGNVYINGRDITGLNKN 79
Cdd:PRK11022 3 LLNVDKLSVHFGDES-APFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADFRGQEIGFIFQD------------FNLLENLTNRENialpLSLQNVKTSAINpkvdkIAKRLGI---DHILNKYPA 144
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQG----GNKKTRRQRAID-----LLNQVGIpdpASRLDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 145 EISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
|
250
....*....|....
gi 489748581 224 GKEikkdGKSREEF 237
Cdd:PRK11022 233 VET----GKAHDIF 242
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-223 |
1.93e-22 |
|
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: 91.40 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNqmaDF 84
Cdd:cd03244 3 IEFKNVSLRYRPNLP---PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH---DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENlTNRENIAlPLS------LQNV-KTSAINPKVDKIAKRLGIDHILNKypAEISGGQKQRVAAA 157
Cdd:cd03244 77 R-SRISIIPQDPVLFSG-TIRSNLD-PFGeysdeeLWQAlERVGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-223 |
2.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAD 83
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQ--DFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALV 161
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-222 |
3.08e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrgqEIGFI--FQDFNLLEN 101
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 102 LTNRENIaLPLSLQNVKTS-------------AINPKVDKIA---KRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:PRK11300 95 MTVIENL-LVAQHQQLKTGlfsgllktpafrrAESEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGK 222
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmKLVMGISDRIYVVNQGT 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-223 |
5.10e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.42 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKN---QM 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSN----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlrQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 ADFRGQEiGFIFqDFNLLENLT--NRENIALPLSLQNVKTSAINPKVDKIAkrLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:TIGR01193 550 INYLPQE-PYIF-SGSILENLLlgAKENVSQDEIWAACEIAEIKDDIENMP--LGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKdkvSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-223 |
6.98e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRgQEIGFIFQDFNLLENLTNREN 107
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IALPLSLQ-NVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLE 186
Cdd:PRK11831 105 VAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 489748581 187 TMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK11831 185 LISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
1.21e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSE-VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnkn 79
Cdd:PRK13537 3 MSVaPIDFRNVEKRYGDK-----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 qMADFRGQEIGFIFQDFNLLENLTNRENIAL---PLSLQNVKTSAINPKVDKIAKrlgidhILNKYPA---EISGGQKQR 153
Cdd:PRK13537 74 -RARHARQRVGVVPQFDNLDPDFTVRENLLVfgrYFGLSAAAARALVPPLLEFAK------LENKADAkvgELSGGMKRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTH 204
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTH 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-223 |
4.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDI-TGLNK-NQMADF 84
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQ--DFNLLENlTNRENIAL-PLSLQNVKTSAINpKVDKIAKRLGI-DHILNKYPAEISGGQKQRVAAARAL 160
Cdd:PRK13645 89 R-KEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGENKQEAYK-KVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 161 VHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-223 |
5.26e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.62 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitgLNKNQMADF 84
Cdd:PRK11176 342 IEFRNVTFTYP---GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQeIGFIFQDFNLLeNLTNRENIALP----LSLQNVKTSA--------INpKVDKiakrlGIDHILNKYPAEISGGQKQ 152
Cdd:PRK11176 416 RNQ-VALVSQNVHLF-NDTIANNIAYArteqYSREQIEEAArmayamdfIN-KMDN-----GLDTVIGENGVLLSGGQRQ 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSiLMVTHDPYSASYASRILFIKDGKI 223
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTS-LVIAHRLSTIEKADEILVVEDGEI 556
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-215 |
5.35e-21 |
|
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: 87.03 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnkNQMADFRGQEIGFIFQDFNLLENLT 103
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENialpLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATE 183
Cdd:TIGR01189 90 ALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180 190
....*....|....*....|....*....|..
gi 489748581 184 LLETMKGLNEKDKvSILMVTHDPYSASYASRI 215
Cdd:TIGR01189 166 LAGLLRAHLARGG-IVLLTTHQDLGLVEAREL 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-236 |
5.70e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfRGqeIGFIFQD---FNLLE 100
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIR-AG--IAYVPEDrkgEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 101 NLTNRENIALPLSLQNVKTSAINPK-----VDKIAKRLGIdhilnKYP------AEISGGQKQRVAAARALVHEPAILYG 169
Cdd:COG1129 344 DLSIRENITLASLDRLSRGGLLDRRreralAEEYIKRLRI-----KTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 170 DEPT-----GAldsKSatELLETMKGLNEKDKvSILMVTHD-PYSASYASRILFIKDGKIGKEIKKDGKSREE 236
Cdd:COG1129 419 DEPTrgidvGA---KA--EIYRLIRELAAEGK-AVIVISSElPELLGLSDRILVMREGRIVGELDREEATEEA 485
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-205 |
7.90e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.07 E-value: 7.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKG------EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLN 77
Cdd:PRK10261 313 ILQVRNLVTRFPLRSgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 78 KNQMADFRgQEIGFIFQD--FNLLENLTNRENIALPLSLQNV-KTSAINPKVDKIAKRLGI--DHILnKYPAEISGGQKQ 152
Cdd:PRK10261 393 PGKLQALR-RDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQ 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-204 |
9.85e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 9.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFrgqEIGFIFQDFNLLENLTNRENI---ALP----LSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQR 153
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLyigRHLtkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTH 204
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISH 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
1.69e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEV-VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnKN 79
Cdd:PRK13536 37 MSTVaIDLAGVSKSYGDK-----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADFRgqeIGFIFQDFNLLENLTNRENIAL---PLSLQNVKTSAINPKVDKIAKrlgIDHILNKYPAEISGGQKQRVAA 156
Cdd:PRK13536 110 RLARAR---IGVVPQFDNLDLEFTVRENLLVfgrYFGMSTREIEAVIPSLLEFAR---LESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTH 204
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTH 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-236 |
6.96e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyqaLKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLN-----K 78
Cdd:PRK09700 265 VFEVRNVTSRDRKK-------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 79 NQMA---DFRgQEIGFiFQDFNLlenltnRENIALPLSLQNVKTSA----INPKVD-KIA----KRLGID-HILNKYPAE 145
Cdd:PRK09700 338 KGMAyitESR-RDNGF-FPNFSI------AQNMAISRSLKDGGYKGamglFHEVDEqRTAenqrELLALKcHSVNQNITE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 146 ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVsILMVTHD-PYSASYASRILFIKDGKIG 224
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSElPEIITVCDRIAVFCEGRLT 488
|
250
....*....|..
gi 489748581 225 KEIKKDGKSREE 236
Cdd:PRK09700 489 QILTNRDDMSEE 500
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-205 |
1.83e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.73 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKT----TLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFN- 97
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQEPSs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 98 -----------LLENLTNREnialpLS------LQNVKTSAInpkvdKIAKRLGI-DH--ILNKYPAEISGGQKQRVAAA 157
Cdd:COG4170 101 cldpsakigdqLIEAIPSWT-----FKgkwwqrFKWRKKRAI-----ELLHRVGIkDHkdIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 158 RALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-206 |
1.95e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQeigfifQDFnLLENLTN 104
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH------RNA-MKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNVKTSAInpkvDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALV-HEPA-ILygDEPTGALDSKSAT 182
Cdd:PRK13539 91 AENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRPIwIL--DEPTAALDAAAVA 164
|
170 180
....*....|....*....|....
gi 489748581 183 ELLETMKGLNEKDKvSILMVTHDP 206
Cdd:PRK13539 165 LFAELIRAHLAQGG-IVIAATHIP 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-206 |
4.54e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.16 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnkNQMADFRGQEIGFIFQDFNLLENLTN 104
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNvkTSAINPKVDKIAKRlGIDHILnkyPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:cd03231 91 LENLRFWHADHS--DEQVEEALARVGLN-GFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 489748581 185 LETMKGLNEKDKvSILMVTHDP 206
Cdd:cd03231 165 AEAMAGHCARGG-MVVLTTHQD 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-204 |
4.71e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglNKNQMADFRgqEIGFIFQDFNLLENLTNREN 107
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATRR--RVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLET 187
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170
....*....|....*..
gi 489748581 188 MKGLNEKDKVSILMVTH 204
Cdd:NF033858 440 LIELSREDGVTIFISTH 456
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-223 |
6.53e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 6.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINgrdiTGLnknqmad 83
Cdd:COG0488 315 VLELEGLSKSYGDK-----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 frgqEIGFIFQDFNLL-ENLTNRENIAlPLSLQNVKTSAIN---------PKVDKIAKRLgidhilnkypaeiSGGQKQR 153
Cdd:COG0488 379 ----KIGYFDQHQEELdPDKTVLDELR-DGAPGGTEQEVRGylgrflfsgDDAFKPVGVL-------------SGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 154 VAAARALVHEPAILYGDEPTGALD--SKSA-TELLETMKGlnekdkvSILMVTHDPY-SASYASRILFIKDGKI 223
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDieTLEAlEEALDDFPG-------TVLLVSHDRYfLDRVATRILEFEDGGV 507
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
1.26e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGrditglnknq 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR-----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfrGQEIGFIFQDFNLlenltnreNIALPLSLQ-------NVKTSAINPKVdkiaKRLGIDHILNKYPAEISGGQKQR 153
Cdd:PRK09544 66 -----KLRIGYVPQKLYL--------DTTLPLTVNrflrlrpGTKKEDILPAL----KRVQAGHLIDAPMQKLSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
1.78e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ 80
Cdd:PRK15439 8 APPLLCARSISKQYSG-----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 madfrGQEIG--FIFQDFNLLENLTNRENIALPLSlqnvKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAAR 158
Cdd:PRK15439 83 -----AHQLGiyLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 159 ALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG-VGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-223 |
1.97e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLdQPTTGNVYINGRDITGLNKNQMADFRG-----QEIGFIFQDFNLL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAylsqqQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 100 enltnreniALPLSlQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARAL--VH-----EPAILYGDEP 172
Cdd:COG4138 91 ---------ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 173 TGALD--SKSATE-LLETMKGLNekdkVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:COG4138 161 MNSLDvaQQAALDrLLRELCQQG----ITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-236 |
2.21e-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: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 3 EVVQVQDITKtygkKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMA 82
Cdd:COG3845 256 VVLEVENLSV----RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 DfRGqeIGFI---------FQDFNLLENLTNRENIALPLSlqnvKTSAINPK-VDKIAKRL---------GIDHilnkyP 143
Cdd:COG3845 332 R-LG--VAYIpedrlgrglVPDMSVAENLILGRYRRPPFS----RGGFLDRKaIRAFAEELieefdvrtpGPDT-----P 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 144 AE-ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMkgLNEKDK-VSILMVthdpySA------SYASRI 215
Cdd:COG3845 400 ARsLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL--LELRDAgAAVLLI-----SEdldeilALSDRI 472
|
250 260
....*....|....*....|.
gi 489748581 216 LFIKDGKIGKEIKKDGKSREE 236
Cdd:COG3845 473 AVMYEGRIVGEVPAAEATREE 493
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-188 |
2.41e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 27 GISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnKNQMADFRGqeigfifqdfNLL------- 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDEYHQ----------DLLylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 100 --ENLTNRENIALPLSLQNVKTSainpkvDKIAKRL------GIDHILNKYpaeISGGQKQRVAAARALVHEPA--ILyg 169
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGDD------EALWEALaqvglaGFEDVPVRQ---LSAGQQRRVALARLWLTRAPlwIL-- 153
|
170
....*....|....*....
gi 489748581 170 DEPTGALDsKSATELLETM 188
Cdd:PRK13538 154 DEPFTAID-KQGVARLEAL 171
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-223 |
7.52e-18 |
|
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: 78.99 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEkqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:cd03369 7 IEVENLSVRYAPDLP---PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENlTNRENialpLSLQNVKTSainpkvDKIAKRLGIDHI-LNkypaeISGGQKQRVAAARALVHE 163
Cdd:cd03369 81 R-SSLTIIPQDPTLFSG-TIRSN----LDPFDEYSD------EEIYGALRVSEGgLN-----LSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIR--EEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-246 |
1.00e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 8 QDITKTYGKKGekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGlnkNQMADFRgQ 87
Cdd:PRK10522 326 RNVTFAYQDNG----FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYR-K 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 88 EIGFIFQDFNLLENLTNRENialplslqnvkTSAINPKVDKIAKRLGIDHILNKYPAEI-----SGGQKQRVAAARALVH 162
Cdd:PRK10522 398 LFSAVFTDFHLFDQLLGPEG-----------KPANPALVEKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 163 EPAILYGDEptGALDSKSA------TELLETMKglnEKDKvSILMVTHDPYSASYASRILFIKDGKIgKEIKkdGKSREE 236
Cdd:PRK10522 467 ERDILLLDE--WAADQDPHfrrefyQVLLPLLQ---EMGK-TIFAISHDDHYFIHADRLLEMRNGQL-SELT--GEERDA 537
|
250
....*....|
gi 489748581 237 FYQEIIAELG 246
Cdd:PRK10522 538 ASRDAVARTA 547
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-205 |
4.97e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQMADFRgQEIGFIFQDFNLLENL 102
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQDPEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRE-NIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSA 181
Cdd:PRK13638 93 TDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180
....*....|....*....|....
gi 489748581 182 TELLETMKGLNEKDKvSILMVTHD 205
Cdd:PRK13638 173 TQMIAIIRRIVAQGN-HVIISSHD 195
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-221 |
6.06e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.47 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINgrditglnknqmadfRGQEIGFIFQDFNL-LENLt 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLPQRPYLpLGTL- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 nRENIALPLSLQNVKTSAINP---KV--DKIAKRLGI----DHILnkypaeiSGGQKQRVAAARALVHEPAILYGDEPTG 174
Cdd:COG4178 443 -REALLYPATAEAFSDAELREaleAVglGHLAERLDEeadwDQVL-------SLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489748581 175 ALDSKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDG 221
Cdd:COG4178 515 ALDEENEAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-223 |
6.06e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 26 KGISFDVARGEFVGIMGASGSGKT----TLLNILSTLDQPTTGNVYINGRDITGlnknqmADFRGQEIGFIFQD----FN 97
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP------CALRGRKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 98 LLENLTN--REnialplSLQNVKTSAINPKVDKIAKRLGIDH---ILNKYPAEISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:PRK10418 94 PLHTMHThaRE------TCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489748581 173 TGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-176 |
6.77e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY-GKKgekqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnkn 79
Cdd:PRK10762 1 MQALLQLKGIDKAFpGVK------ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 qmadFRG----QE--IGFIFQDFNLLENLTNRENIALPLSLQN----VKTSAINPKVDKIAKRLGIDHILNKYPAEISGG 149
Cdd:PRK10762 70 ----FNGpkssQEagIGIIHQELNLIPQLTIAENIFLGREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIG 145
|
170 180
....*....|....*....|....*..
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGAL 176
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-227 |
7.07e-17 |
|
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: 76.13 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKTTLLNILS--TLDQPTTGNVYINGRDITglnknqm 81
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKR-QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 ADFRgQEIGFIFQDFNLLENLTNREniALPLSlqnvktsainpkvdkiAKRLGidhilnkypaeISGGQKQRVAAARALV 161
Cdd:cd03232 75 KNFQ-RSTGYVEQQDVHSPNLTVRE--ALRFS----------------ALLRG-----------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYAS--RILFIKDGkiGKEI 227
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQ-AILCTIHQPSASIFEKfdRLLLLKRG--GKTV 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-246 |
2.01e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLD--QPTTGNVYINGRDITGLNknqmADFRGQE-IGFIFQD------ 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELS----PDERARAgIFLAFQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 ---FNLL---ENLTNRENIALPLSLQNVKtsainpkvdKIAKRLGIDH-ILNKYPAE-ISGGQKQRVAAARALVHEP--A 165
Cdd:COG0396 92 vsvSNFLrtaLNARRGEELSAREFLKLLK---------EKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPklA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 166 ILygDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHdpysasYAsRIL-FIK--------DGKIgkeIKKDGKS--- 233
Cdd:COG0396 163 IL--DETDSGLDIDALRIVAEGVNKLRSPDR-GILIITH------YQ-RILdYIKpdfvhvlvDGRI---VKSGGKElal 229
|
250
....*....|....*
gi 489748581 234 --REEFYQEIIAELG 246
Cdd:COG0396 230 elEEEGYDWLKEEAA 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-221 |
3.32e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 77.84 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 8 QDITKTYGKKGEKQyQALKGISFDVARGEFVGIMGASGSGKTTLLNILStlDQPTTGnvYINGRDItglnknqMADFRGQ 87
Cdd:TIGR00956 763 RNLTYEVKIKKEKR-VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG--VITGGDR-------LVNGRPL 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 88 E------IGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPK---VDKIAKRLGidhiLNKYPAEISG--------GQ 150
Cdd:TIGR00956 831 DssfqrsIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLE----MESYADAVVGvpgeglnvEQ 906
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 151 KQRVAAARALVHEPA-ILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYAS--RILFIKDG 221
Cdd:TIGR00956 907 RKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-195 |
4.85e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGkkGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILS------TLDqpttGNVYINGRDIT 74
Cdd:PRK13549 2 MEYLLEMKNITKTFG--GVK---ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvyphgTYE----GEIIFEGEELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 75 GLNknqMADFRGQEIGFIFQDFNLLENLTNRENIAL---PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQK 151
Cdd:PRK13549 73 ASN---IRDTERAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 152 QRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKD 195
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHG 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-213 |
6.35e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQpTTGNVYINGRdITGLNKN------QMADFRGQeIGFIFQDFNL 98
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGR-VEFFNQNiyerrvNLNRLRRQ-VSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 LEnLTNRENIALplslqNVKTSAINPKV--DKIAKRL--------GIDHILNKYPAEISGGQKQRVAAARALVHEPAILY 168
Cdd:PRK14258 100 FP-MSVYDNVAY-----GVKIVGWRPKLeiDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489748581 169 GDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYAS 213
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-222 |
1.11e-15 |
|
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: 71.71 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVyingrditglnknqmadf 84
Cdd:cd03221 1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgqeigfifqdfnllenltnrenialplslqnvktsaINPKVDKIAkrlgidhilnkYPAEISGGQKQRVAAARALVHEP 164
Cdd:cd03221 58 -------------------------------------TWGSTVKIG-----------YFEQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 165 AILYGDEPTGALDSKSATELLETMKGLNEkdkvSILMVTHDPY-SASYASRILFIKDGK 222
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-223 |
1.19e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 73.07 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 14 YGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLdqpTTGNVYINGrDIT--GLNKNQMADFRGQEIGF 91
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEG-DIHynGIPYKEFAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 92 IFQDFNLLENLTNRENIALPLSLQNvktsainpkvdkiakrlgidhilNKYPAEISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:cd03233 88 VSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489748581 172 PTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYA--SRILFIKDGKI 223
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQ 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-222 |
1.43e-15 |
|
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: 75.63 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTT--GNVYINGRDITGLNknqM 81
Cdd:TIGR02633 1 LLEMKGIVKTFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASN---I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 ADFRGQEIGFIFQDFNLLENLTNRENIAL--PLSLQNVKT--SAINPKVDKIAKRLGIDHILNKYP-AEISGGQKQRVAA 156
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDkVSILMVTHD-PYSASYASRILFIKDGK 222
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-223 |
1.75e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILS-TLDQPT-------TGNVYINGRDITGLNKNQMADFRG-----QEIGF 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 92 IFqdfnllenlTNRENIALPLSLQNVKTSAINPKVDKIA----KRLGIDHILNKYPAEISGGQKQRVAAARALVH----- 162
Cdd:PRK13547 97 AF---------SAREIVLLGRYPHARRAGALTHRDGEIAwqalALAGATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 163 ----EPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP-YSASYASRILFIKDGKI 223
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-247 |
1.87e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.98 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 40 IMGASGSGKTTLLNILSTLDQPTTG-----NVYINGRDItgLNKNQMADFRgQEIGFIFQDFNLLEnLTNRENIalplsL 114
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFR-RRVGMLFQRPNPFP-MSIMDNV-----L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 115 QNVKTSAINPK----------VDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:PRK14271 123 AGVRAHKLVPRkefrgvaqarLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 185 LETMKGLneKDKVSILMVTHD-PYSASYASRILFIKDGKIGKEikkdGKSREEFYQEIIAELGR 247
Cdd:PRK14271 203 EEFIRSL--ADRLTVIIVTHNlAQAARISDRAALFFDGRLVEE----GPTEQLFSSPKHAETAR 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-223 |
2.13e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQYQALKgISFdvARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDI-TGLnknqmaD 83
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLN-ITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNL------D 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHE 163
Cdd:TIGR01257 1000 AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 164 PAILYGDEPTGALDSKSATELLETMkgLNEKDKVSILMVTHDPYSAS-YASRILFIKDGKI 223
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-204 |
2.20e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.29 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglnKNQMADFRgQEIGFIFQDFNLLENLTN 104
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENialplSLQNVKTSAINPKVDKIAKRLGIDHILNkYPAE-ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATE 183
Cdd:PRK13540 92 REN-----CLYDIHFSPGAVGITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 489748581 184 LLETMKGlNEKDKVSILMVTH 204
Cdd:PRK13540 166 IITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-205 |
3.09e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 17 KGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfRGqeIGFIFQDF 96
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-RG--IGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 97 NLLENLTNRENIALPLSL-QNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGA 175
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190
....*....|....*....|....*....|
gi 489748581 176 LDSKSATELLETMKGLNEKDkVSILMVTHD 205
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSG-LGVLITDHN 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-226 |
3.19e-15 |
|
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: 74.44 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 9 DITKTYG------KKGEkqyqalkgisfdVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYIngrDITGLNKNQma 82
Cdd:COG1245 346 DLTKSYGgfslevEGGE------------IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLKISYKPQ-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 dfrgqeigFIFQDFNLlenlTNRENIAlplslqnvktSAINPKVD------KIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:COG1245 409 --------YISPDYDG----TVEEFLR----------SANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAI 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489748581 157 ARALVHEpAILYG-DEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:COG1245 467 AACLSRD-ADLYLlDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVH 536
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-220 |
3.35e-15 |
|
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: 71.03 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitglnknqmadfrgqEIGFIFQDfNLLENLTN 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQR-PYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLslqnvktsainpkvdkiakrlgiDHILnkypaeiSGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:cd03223 81 REQLIYPW-----------------------DDVL-------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 489748581 185 LETMKGLnekdKVSILMVTHDPYSASYASRILFIKD 220
Cdd:cd03223 131 YQLLKEL----GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-226 |
3.44e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 9 DITKTYG------KKGEkqyqalkgisfdVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYIngrDITGLNKNQma 82
Cdd:PRK13409 345 DLTKKLGdfslevEGGE------------IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELKISYKPQ-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 dfrgqeigFIFQDFN-----LLENLTNRENialplslqnvkTSAINPKvdkIAKRLGIDHILNKYPAEISGGQKQRVAAA 157
Cdd:PRK13409 408 --------YIKPDYDgtvedLLRSITDDLG-----------SSYYKSE---IIKPLQLERLLDKNVKDLSGGELQRVAIA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 158 RALVHEpAILYG-DEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PRK13409 466 ACLSRD-ADLYLlDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGEPGKH 534
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-245 |
4.20e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknQMADFRGQ-----EIGFIFQDfnl 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvsQTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 lenlTNRENIALPlslqnvKTSAINPKVDKIAKRLGI-DHILN---KYPAEI-------SGGQKQRVAAARALVHEPAIL 167
Cdd:PRK10789 404 ----TVANNIALG------RPDATQQEIEHVARLASVhDDILRlpqGYDTEVgergvmlSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLNEKDKVSIlmVTHDPYSASYASRILFIKDGKIGKE------IKKDGKSREEF-YQE 240
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVII--SAHRLSALTEASEILVMQHGHIAQRgnhdqlAQQSGWYRDMYrYQQ 551
|
....*
gi 489748581 241 IIAEL 245
Cdd:PRK10789 552 LEAAL 556
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-213 |
6.28e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQ-----PTTGNVYINGRDITGLNK 78
Cdd:PRK14243 10 VLRTENLNVYYGS-----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 79 NQMADFRgqEIGFIFQDFNLLENlTNRENIALPLSLQNVKTSaINPKVDKIAKRLGI-DHI---LNKYPAEISGGQKQRV 154
Cdd:PRK14243 85 DPVEVRR--RIGMVFQKPNPFPK-SIYDNIAYGARINGYKGD-MDELVERSLRQAALwDEVkdkLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 155 AAARALVHEPAILYGDEPTGALDSKSATELLETMKGLneKDKVSILMVTHDPYSASYAS 213
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVS 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-205 |
9.41e-15 |
|
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: 73.28 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 34 RGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYingrdiTGLNKNQMAD-FRGQEIgfifqdFNLLENLTNrENIALPL 112
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD------EEPSWDEVLKrFRGTEL------QDYFKKLAN-GEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 113 SLQNV---------KTSAINPKVD------KIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALD 177
Cdd:COG1245 165 KPQYVdlipkvfkgTVRELLEKVDergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*...
gi 489748581 178 SKSATELLETMKGLNEKDKvSILMVTHD 205
Cdd:COG1245 245 IYQRLNVARLIRELAEEGK-YVLVVEHD 271
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-223 |
9.63e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 9.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYGKkgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLnknQ 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK-----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 81 MADFRGQEIGFIFQDFNLLENLTNRENIAL-------PLSLQNVK-TSAINPKV-DKIAKRLGIdhilnkypaeISGGQK 151
Cdd:PRK11614 74 TAKIMREAVAIVPEGRRVFSRMTVEENLAMggffaerDQFQERIKwVYELFPRLhERRIQRAGT----------MSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 152 QRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEkDKVSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQAlKLADRGYVLENGHV 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-205 |
1.55e-14 |
|
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: 70.86 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 8 QDITKTYGKKGEKQYQalkgisFDVAR-GEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYING--RDItglnknqMADF 84
Cdd:cd03236 4 DEPVHRYGPNSFKLHR------LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwDEI-------LDEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIgfifQDFnlLENLTNrENIALPLSLQNV---------KTSAINPKVDK------IAKRLGIDHILNKYPAEISGG 149
Cdd:cd03236 71 RGSEL----QNY--FTKLLE-GDVKVIVKPQYVdlipkavkgKVGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHD 205
Cdd:cd03236 144 ELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHD 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-221 |
1.60e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.44 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLniLSTLD--QPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLeNL 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGemQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIAL--PLSLQNVK----TSAINPKVD--------KIAKRlGIDhilnkypaeISGGQKQRVAAARALVHEPAILY 168
Cdd:cd03290 94 TVEENITFgsPFNKQRYKavtdACSLQPDIDllpfgdqtEIGER-GIN---------LSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 169 GDEPTGALDSKSATELLET--MKGLNEkDKVSILMVTHDPYSASYASRILFIKDG 221
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgiLKFLQD-DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-225 |
2.20e-14 |
|
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: 70.13 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 31 DVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQeigfiFQDFnlLENLTNREnial 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGT-----VRDL--LSSITKDF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 111 pLSLQNVKTSAINPkvdkiakrLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKG 190
Cdd:cd03237 90 -YTHPYFKTEIAKP--------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....*
gi 489748581 191 LNEKDKVSILMVTHDPYSASYASRILFIKDGKIGK 225
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-200 |
6.78e-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: 70.81 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 2 SEVVQVQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnkNQM 81
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 ADFRgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALV 161
Cdd:TIGR01257 2008 SDVH-QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190
....*....|....*....|....*....|....*....
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSIL 200
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-215 |
7.58e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQP----TTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNl 98
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQEPQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 99 lENLTNRENIALPLsLQNV----------------KTSAInpkvdKIAKRLGI-DH--ILNKYPAEISGGQKQRVAAARA 159
Cdd:PRK15093 100 -SCLDPSERVGRQL-MQNIpgwtykgrwwqrfgwrKRRAI-----ELLHRVGIkDHkdAMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSAS-YASRI 215
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSqWADKI 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-226 |
8.33e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKQyqALKGISFDVARGEFVGIMGASGSGKTTLLN-ILSTLDQPTTGNVYINGRditglnknqmAD 83
Cdd:PLN03130 615 ISIKNGYFSWDSKAERP--TLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT----------VA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQeIGFIFqdfnlleNLTNRENIALPLSLQNvktsainPKVDKIAKRLGIDHILNKYPA-----------EISGGQKQ 152
Cdd:PLN03130 683 YVPQ-VSWIF-------NATVRDNILFGSPFDP-------ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQ 747
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLET-MKG-LNEKDKVsilMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIKDeLRGKTRV---LVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-207 |
1.02e-13 |
|
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: 69.96 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINgrditglnknqmad 83
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE----ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 fRGQEIGFIFQDFNLLENLTNRENIALPLSLQ----------NVKTSAINPKVDKIAKRLG-----IDHI---------- 138
Cdd:TIGR03719 66 -PGIKVGYLPQEPQLDPTKTVRENVEEGVAEIkdaldrfneiSAKYAEPDADFDKLAAEQAelqeiIDAAdawdldsqle 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 139 -----LNKYP-----AEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL---LETMKGlnekdkvSILMVTHD 205
Cdd:TIGR03719 145 iamdaLRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLerhLQEYPG-------TVVAVTHD 217
|
..
gi 489748581 206 PY 207
Cdd:TIGR03719 218 RY 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-223 |
1.24e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVA-------------RGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdfrgQEIG 90
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 91 FIFQDFNLLENLTNRENIAL---PL--SLQNVKtSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPA 165
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIgryPWhgALGRFG-AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 166 ILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEM 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-230 |
1.33e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITktygkkGEkqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLN-KNQMA 82
Cdd:PRK15439 268 VLTVEDLT------GE----GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 dfRG--------QEIGfIFQDFNLLENLTNRENIALPLSLQNVKTSAInpkVDKIAKRLGIDHILNKYPAE-ISGGQKQR 153
Cdd:PRK15439 338 --RGlvylpedrQSSG-LYLDAPLAWNVCALTHNRRGFWIKPARENAV---LERYRRALNIKFNHAEQAARtLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYS-ASYASRILFIKDGKIGKEIKKD 230
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEiEQMADRVLVMHQGEISGALTGA 488
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-178 |
1.64e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.36 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKkgekQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMAdf 84
Cdd:PRK10790 341 IDIDNVSFAYRD----DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rgQEIGFIFQDFNLLENlTNRENIAL--PLSLQNVKTSAINPKVDKIAKRL--GIDHILNKYPAEISGGQKQRVAAARAL 160
Cdd:PRK10790 415 --QGVAMVQQDPVVLAD-TFLANVTLgrDISEEQVWQALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170
....*....|....*...
gi 489748581 161 VHEPAILYGDEPTGALDS 178
Cdd:PRK10790 492 VQTPQILILDEATANIDS 509
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-155 |
2.86e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 68.67 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 6 QVQDITKTY-GKKGEKQYqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADF 84
Cdd:COG4615 329 ELRGVTYRYpGEDGDEGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---REAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENLTNRENIALPlslqnvktsainPKVDKIAKRLGIDHILnkypaEI----------SGGQKQRV 154
Cdd:COG4615 405 R-QLFSAVFSDFHLFDRLLGLDGEADP------------ARARELLERLELDHKV-----SVedgrfsttdlSQGQRKRL 466
|
.
gi 489748581 155 A 155
Cdd:COG4615 467 A 467
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-222 |
4.02e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLdQPTTGNVYINGRDITGLNKNQMADFRG-----QEIGFIFQDFNLLEnl 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAylsqqQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 tnrenialpLSL-QNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRV--AAARALVHePAI-LYG-----DEPT 173
Cdd:PRK03695 92 ---------LHQpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlAAVVLQVW-PDInPAGqllllDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489748581 174 GALD--SKSATE-LLETMKGLNekdkVSILMVTHD-PYSASYASRILFIKDGK 222
Cdd:PRK03695 162 NSLDvaQQAALDrLLSELCQQG----IAVVMSSHDlNHTLRHADRVWLLKQGK 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-207 |
9.97e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVV-QVQDITKTYGKKgekqYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYIngrditglnkn 79
Cdd:PRK11819 2 MAQYIyTMNRVSKVVPPK----KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 qMADFRgqeIGFIFQDFNLLENLTNRENIALPLS-----LQ-----NVKTSAINPKVDKIAKRLG-----IDHI------ 138
Cdd:PRK11819 67 -APGIK---VGYLPQEPQLDPEKTVRENVEEGVAevkaaLDrfneiYAAYAEPDADFDALAAEQGelqeiIDAAdawdld 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 139 ---------LNKYPAE-----ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL---LETMKGlnekdkvSILM 201
Cdd:PRK11819 143 sqleiamdaLRCPPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLeqfLHDYPG-------TVVA 215
|
....*.
gi 489748581 202 VTHDPY 207
Cdd:PRK11819 216 VTHDRY 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-230 |
1.23e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 20 KQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYING----------------------------- 70
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrskigvvsqdpllfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 71 ------------RDITGL-------------NKNQMADFRGQEIGfifqDFNLLEN-LTNRENIALPLSLQNVKTSainp 124
Cdd:PTZ00265 476 iknnikyslyslKDLEALsnyynedgndsqeNKNKRNSCRAKCAG----DLNDMSNtTDSNELIEMRKNYQTIKDS---- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 125 KVDKIAKRLGIDHILNKYP-----------AEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNE 193
Cdd:PTZ00265 548 EVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
250 260 270
....*....|....*....|....*....|....*..
gi 489748581 194 KDKVSILMVTHDPYSASYASRILFIKDGKIGKEIKKD 230
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVD 664
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-235 |
1.66e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgeKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNIL---------------------STLDQPTT 63
Cdd:PTZ00265 1166 IEIMDVNFRYISR--PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndMTNEQDYQ 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 64 GN-----VYINGRDITGLNKNQMAD----FRGQ-EI---GFIFQDFNL--LENL---TNRENIALPLSL-QNVK---TSA 121
Cdd:PTZ00265 1244 GDeeqnvGMKNVNEFSLTKEGGSGEdstvFKNSgKIlldGVDICDYNLkdLRNLfsiVSQEPMLFNMSIyENIKfgkEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 122 INPKVDKIAKRLGIDHIL----NKYPAEI-------SGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKG 190
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIeslpNKYDTNVgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489748581 191 LNEKDKVSILMVTHDPYSASYASRI-LFIKDGKIGKEIKKDGKSRE 235
Cdd:PTZ00265 1404 IKDKADKTIITIAHRIASIKRSDKIvVFNNPDRTGSFVQAHGTHEE 1449
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-205 |
2.66e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 34 RGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVyingrditglNKNQMAD-----FRGQEIgfifqdFNLLENLTNREnI 108
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY----------EEEPSWDevlkrFRGTEL------QNYFKKLYNGE-I 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 109 ALPLSLQNV---------KTSAINPKVDK------IAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:PRK13409 161 KVVHKPQYVdlipkvfkgKVRELLKKVDErgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|..
gi 489748581 174 GALDSKSATELLETMKGLNEKDKVsiLMVTHD 205
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-204 |
3.01e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY----------------GKKGEKQYqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTG 64
Cdd:PRK13545 1 MNYKVKFEHVTKKYkmynkpfdklkdlffrSKDGEYHY-ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 65 NVYINGRDI-----TGLNknqmadfrgqeigfifqdfNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKrlgIDHIL 139
Cdd:PRK13545 80 TVDIKGSAAliaisSGLN-------------------GQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFAD---IGKFI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 140 NKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTH 204
Cdd:PRK13545 138 YQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISH 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-226 |
4.03e-12 |
|
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: 63.31 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLD--QPTTGNVYINGRDITGLNKNQMADfRGqeIGFIFQDfnllenl 102
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR-LG--IFLAFQY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 tnrenialPLSLQNVKTSainpkvdkiakrlgidHILNKYPAEISGGQKQRVAAARALVHEP--AILygDEPTGALDSKS 180
Cdd:cd03217 86 --------PPEIPGVKNA----------------DFLRYVNEGFSGGEKKRNEILQLLLLEPdlAIL--DEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489748581 181 ATELLETMKGLNEKDKvSILMVTHDPYSASY--ASRILFIKDGKIGKE 226
Cdd:cd03217 140 LRLVAEVINKLREEGK-SVLIITHYQRLLDYikPDRVHVLYDGRIVKS 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-242 |
6.71e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDItglNKNQMADFRGQEIGFIFQDFN---LLEN 101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPQDGLANGIVYISEDRKrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 102 LTNRENIALPlSLQnvKTSAINPKVDKIAKRLGIDHILN----KYPA------EISGGQKQRVAAARALVHEPAILYGDE 171
Cdd:PRK10762 345 MSVKENMSLT-ALR--YFSRAGGSLKHADEQQAVSDFIRlfniKTPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489748581 172 PTGALD---SKSATELLETMKglneKDKVSILMVTHD-PYSASYASRILFIKDGKIGKEIkkdgkSREEFYQEII 242
Cdd:PRK10762 422 PTRGVDvgaKKEIYQLINQFK----AEGLSIILVSSEmPEVLGMSDRILVMHEGRISGEF-----TREQATQEKL 487
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
5-206 |
1.12e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKG-EKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNIL--STLDQPTTGNVYINGRDITglnknqm 81
Cdd:COG2401 25 ERVAIVLEAFGVELrVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 82 adfrgqeigfifQDFNLLENLTNRENIALPLSLQNvkTSAINPKVDKIAKrlgidhilnkyPAEISGGQKQRVAAARALV 161
Cdd:COG2401 98 ------------REASLIDAIGRKGDFKDAVELLN--AVGLSDAVLWLRR-----------FKELSTGQKFRFRLALLLA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489748581 162 HEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDP 206
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-223 |
1.27e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITglnKNQMADFRgQEIGFIFQDFNLLENlTN 104
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGLTDLR-RVLSIIPQSPVLFSG-TV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIAlPLSLQN-------VKTSAINPKVDKiaKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALD 177
Cdd:PLN03232 1327 RFNID-PFSEHNdadlweaLERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489748581 178 SKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:PLN03232 1404 VRTDSLIQRTIR--EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-226 |
5.88e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLN-ILSTLDQPTTGNVYINGrditglnknqmADFRGQEIGFIFqdfnlleNLT 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------SVAYVPQVSWIF-------NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIalpLSLQNVKTSAINPKVDKIAkrlgIDHILNKYPAE-----------ISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:PLN03232 695 VRENI---LFGSDFESERYWRAIDVTA----LQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489748581 173 TGALDSKSATELLET-MK-GLNEKDKVsilMVTHDPYSASYASRILFIKDGKIGKE 226
Cdd:PLN03232 768 LSALDAHVAHQVFDScMKdELKGKTRV---LVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-205 |
1.41e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.90 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTYgkkgEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDIT-GLNKN 79
Cdd:PRK15056 3 QQAGIVVNDVTVTW----RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADF-RGQEIGFIFQdfNLLEN--LTNRENIALPLSLQNVKTSAInpkVDKIAKRLGIDHILNKYPAEISGGQKQRVAA 156
Cdd:PRK15056 79 LVAYVpQSEEVDWSFP--VLVEDvvMMGRYGHMGWLRRAKKRDRQI---VTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489748581 157 ARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHD 205
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHN 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-236 |
1.61e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLN-ILSTLDQPTTGNVYINGRDItglNKNQMADFRGQEIGFIFQD---FNLLENLT 103
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPV---DIRNPAQAIRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALPLSLQNVKTSAINPKVDKIAKRLGID--HILNKYP----AEISGGQKQRVAAARALVHEPAILYGDEPTGALD 177
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 178 SKSATELLETMKGLNEKDkVSILMVTHD-PYSASYASRILFIKDGKIGKEIKKDGKSREE 236
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEG-VAIIVVSSElAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-246 |
1.70e-10 |
|
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: 60.73 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGrditglnknqmadfrgqEIGFIFQDfNLLENLTN 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQN------VKTSAINPKVDKIAKrlGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDS 178
Cdd:TIGR00957 716 RENILFGKALNEkyyqqvLEACALLPDLEILPS--GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 179 KSATELLETMKGLNE--KDKVSILmVTHdpySASYASRILFI---KDGKIgkeikkdgkSREEFYQEIIAELG 246
Cdd:TIGR00957 794 HVGKHIFEHVIGPEGvlKNKTRIL-VTH---GISYLPQVDVIivmSGGKI---------SEMGSYQELLQRDG 853
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
2.64e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYI----------NGRDI 73
Cdd:TIGR03719 322 VIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 74 TGLNKNQMadfrgQEIgfifQDFNLLENLTNREnialplslqnVKT----SAINPKVDKIAKRLGidhilnkypaEISGG 149
Cdd:TIGR03719 397 LDPNKTVW-----EEI----SGGLDIIKLGKRE----------IPSrayvGRFNFKGSDQQKKVG----------QLSGG 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 150 QKQRVAAARALVHEPAILYGDEPTGALDsksatelLETMKGLNE 193
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETLRALEE 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-189 |
3.45e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 7 VQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLdQPTTGNVYINGrdiTGLNKNQMADFRg 86
Cdd:TIGR01271 1220 VQGLTAKYTEAGRA---VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG---VSWNSVTLQTWR- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 87 QEIGFIFQDFNLLENlTNRENIalplslqNVKTSAINPKVDKIAKRLGIDHILNKYPAE-----------ISGGQKQRVA 155
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSG-TFRKNL-------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMC 1363
|
170 180 190
....*....|....*....|....*....|....
gi 489748581 156 AARALVHEPAILYGDEPTGALDSKSATELLETMK 189
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-223 |
3.74e-10 |
|
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: 59.96 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRGQeIGFIFQDFNLLE---- 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQDPVLFSgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 101 -NLT-----NRENIALPLSLQNVKTSAinpkvdkIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTG 174
Cdd:TIGR00957 1378 mNLDpfsqySDEEVWWALELAHLKTFV-------SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489748581 175 ALDSKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDGKI 223
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-221 |
4.04e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRditglnknqmadfrgqeIGFIFQdFNLLENLTN 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQ-TSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQNVK-TSAIN-----------PKVDKIakrlgidhILNKYPAEISGGQKQRVAAARALVHEPAILYGDEP 172
Cdd:TIGR01271 504 KDNIIFGLSYDEYRyTSVIKacqleedialfPEKDKT--------VLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489748581 173 TGALDSKSATELLET--MKGLNEKDKVsilMVTHDPYSASYASRILFIKDG 221
Cdd:TIGR01271 576 FTHLDVVTEKEIFESclCKLMSNKTRI---LVTSKLEHLKKADKILLLHEG 623
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-177 |
5.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNknqMADFRgQEIGFIFQD--------- 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQApvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 FNLleNLTNRENIA-LPLSLQNVKTSainpkvDKIAKR-LGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPT 173
Cdd:PLN03130 1331 FNL--DPFNEHNDAdLWESLERAHLK------DVIRRNsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
....
gi 489748581 174 GALD 177
Cdd:PLN03130 1403 AAVD 1406
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-223 |
1.16e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVyingrditglnknQMADf 84
Cdd:PRK15064 320 LEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 rGQEIGFIFQDfnllenltNRENIALPLSLQNVKTSAINPKVDKIAKR--LG-----IDHIlNKYPAEISGGQKQRVAAA 157
Cdd:PRK15064 381 -NANIGYYAQD--------HAYDFENDLTLFDWMSQWRQEGDDEQAVRgtLGrllfsQDDI-KKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 158 RALVHEPAILYGDEPTGALDsksatelLETMKGLN---EKDKVSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD-------MESIESLNmalEKYEGTLIFVSHDrEFVSSLATRIIEITPDGV 513
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-247 |
1.33e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.44 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGkkgekQYQALKGISFDVARGEFVGIMGASGSG--KTTLLNILSTLD---QPTTGNVYINGRDITglnKN 79
Cdd:NF000106 14 VEVRGLVKHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRAL---RR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 80 QMADFRGQEIGfifqdfnLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARA 159
Cdd:NF000106 86 TIG*HRPVR*G-------RRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 160 LVHEPAILYGDEPTGALDSKSATELLETMKGLnEKDKVSILMVTHDPYSASYASRIL-------FIKDGKIGKEIKKDGK 232
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELtvidrgrVIADGKVDELKTKVGG 237
|
250
....*....|....*
gi 489748581 233 SREEFYQEIIAELGR 247
Cdd:NF000106 238 RTLQIRPAHAAELDR 252
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-241 |
2.13e-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: 56.40 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 5 VQVQDITKTYGKKGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQpTTGNVYINGrdiTGLNKNQMADF 84
Cdd:cd03289 3 MTVKDLTAKYTEGGNA---VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG---VSWNSVPLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RgQEIGFIFQDFNLLENlTNRENIAlPLSLQNvktsaiNPKVDKIAKRLGIDHILNKYPAE-----------ISGGQKQR 153
Cdd:cd03289 76 R-KAFGVIPQKVFIFSG-TFRKNLD-PYGKWS------DEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 154 VAAARALVHEPAILYGDEPTGALDSKSATELLETMKglNEKDKVSILMVTHDPYSASYASRILFIKDGKIGK--EIKKDG 231
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLECQRFLVIEENKVRQydSIQKLL 224
|
250
....*....|
gi 489748581 232 KSREEFYQEI 241
Cdd:cd03289 225 NEKSHFKQAI 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-235 |
3.15e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLN-ILSTLDQPTTGNVYINGRDITGLNKNQMADfrgQEIGFIFQD---FNLLENLT 103
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQAIA---QGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYP------AEISGGQKQRVAAARALVHEPAILYGDEPTGALD 177
Cdd:PRK13549 358 VGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 178 SKSATELLETMKGLnEKDKVSILMVTHD-PYSASYASRILFIKDGKIGKEIKKDGKSRE 235
Cdd:PRK13549 438 VGAKYEIYKLINQL-VQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGDLINHNLTQE 495
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-225 |
4.57e-09 |
|
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: 54.12 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 31 DVARGEFVGIMGASGSGKTTLLNILSTLDQPttgnvyingrditglnknqmadfrgqeigfifqdfnllenltNRENIAL 110
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIP------------------------------------------NGDNDEW 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 111 PLSLQNVKTSAInpkvdkiakrlgidhilnkypaEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKG 190
Cdd:cd03222 59 DGITPVYKPQYI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|....*
gi 489748581 191 LNEKDKVSILMVTHDPYSASYASRILFIKDGKIGK 225
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-222 |
4.64e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.95 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 8 QDITKTYGkkGEKqyqALKGISFDVARGEFVGIMGASGSGKTTLLNILStldqpttgNVYINGR---DITglnknqmadF 84
Cdd:NF040905 5 RGITKTFP--GVK---ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS--------GVYPHGSyegEIL---------F 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 85 RGQEIGF-------------IFQDFNLLENLTNRENIAlpLSLQNVKTSAIN-----PKVDKIAKRLGIDHILNKYPAEI 146
Cdd:NF040905 63 DGEVCRFkdirdsealgiviIHQELALIPYLSIAENIF--LGNERAKRGVIDwnetnRRARELLAKVGLDESPDTLVTDI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 147 SGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSIlMVTHDPYSASY-ASRILFIKDGK 222
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRvADSITVLRDGR 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-173 |
5.29e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 4 VVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDitglnknqMAD 83
Cdd:NF033858 1 VARLEGVSHRYGKT-----VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD--------MAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 84 FRGQE-----IGFIFQDF--NLLENLTNRENIALPLSL--QNVKTSAInpKVDKIAKRLGIDHILNKyPA-EISGGQKQR 153
Cdd:NF033858 68 ARHRRavcprIAYMPQGLgkNLYPTLSVFENLDFFGRLfgQDAAERRR--RIDELLRATGLAPFADR-PAgKLSGGMKQK 144
|
170 180
....*....|....*....|
gi 489748581 154 VAAARALVHEPAILYGDEPT 173
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPT 164
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-227 |
5.29e-09 |
|
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: 53.87 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNilstldqpTTGNVYINGRDITGLNKnqmadFRGQEIGFIFQdfnlLENLT 103
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLPK-----FSRNKLIFIDQ----LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NrenialplslqnvktsainpkvdkiakrLGIDHI-LNKYPAEISGGQKQRVAAARAL-VHEPAILY-GDEPTGALDSKS 180
Cdd:cd03238 73 D----------------------------VGLGYLtLGQKLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489748581 181 ATELLETMKGLNEKdKVSILMVTHDPYSASYASRILFI--KDGKIGKEI 227
Cdd:cd03238 125 INQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDFgpGSGKSGGKV 172
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-223 |
5.46e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 1 MSEVVQVQDITKTY---------------GKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGN 65
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrtnkermkdaliPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 66 VYINGrditglnknqmadfrgqEIGFIFQDFNLLENLTNRENIALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAE 145
Cdd:PRK13546 81 VDRNG-----------------EVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489748581 146 ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSA-SYASRILFIKDGKI 223
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVrQFCTKIAWIEGGKL 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-189 |
8.86e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 18 GEKQYQALKGISFDVARGEFVGIMGASGSGKTTLLNILStlDQPTTGnvYINGR-DITGLNKNQMADFRGQeiGFIFQDF 96
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLA--GRKTGG--YIEGDiRISGFPKKQETFARIS--GYCEQND 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 97 NLLENLTNRENIALPLSLQNVKTSAINPK---VDKIAKRLGIDHILNK---YPA--EISGGQKQRVAAARALVHEPAILY 168
Cdd:PLN03140 963 IHSPQVTVRESLIYSAFLRLPKEVSKEEKmmfVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180
....*....|....*....|.
gi 489748581 169 GDEPTGALDSKSATELLETMK 189
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVR 1063
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-209 |
9.25e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRditglnKNQMADfRGQEIGFIFQDFNLLENLTNREN 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------TATRGD-RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IALPLSLQNVKTSAINPKVDKIAKRLGIDHILNKypaEISGGQKQRVAAARaLVHEPAILY-GDEPTGALDSKSATeLLE 186
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALAR-LWLSPAPLWlLDEPYANLDLEGIT-LVN 177
|
170 180
....*....|....*....|...
gi 489748581 187 TMKGLNEKDKVSILMVTHDPYSA 209
Cdd:PRK13543 178 RMISAHLRGGGAALVTTHGAYAA 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-221 |
9.47e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.48 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRditglnknqmadfrgqeIGFIFQdFNLLENLTN 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQ-FSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 105 RENIALPLSLQN------VKTSAINPKVDKIAKRLGIdhILNKYPAEISGGQKQRVAAARAlVHEPAILY-GDEPTGALD 177
Cdd:cd03291 115 KENIIFGVSYDEyryksvVKACQLEEDITKFPEKDNT--VLGEGGITLSGGQRARISLARA-VYKDADLYlLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489748581 178 SKSATELLETMKGLNEKDKVSILmVTHDPYSASYASRILFIKDG 221
Cdd:cd03291 192 VFTEKEIFESCVCKLMANKTRIL-VTSKMEHLKKADKILILHEG 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-203 |
1.42e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 29 SFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEigfiFQDFN--LLE------ 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQRNNtdMLSpgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 101 NLTNRENIalplsLQNVKTsaiNPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKS 180
Cdd:PRK10938 99 GRTTAEII-----QDEVKD---PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180
....*....|....*....|...
gi 489748581 181 ATELLETMKGLNEKDKVSILMVT 203
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLN 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-239 |
1.57e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 24 ALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQ---------MADFRGQEI-GFIF 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalvTEERRSTGIyAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 94 QDFN-LLENLTNRENialplslqnvKTSAINPKVDKIAKRLGIDHILNKYPAE------ISGGQKQRVAAARALVHEPAI 166
Cdd:PRK10982 343 IGFNsLISNIRNYKN----------KVGLLDNSRMKSDTQWVIDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489748581 167 LYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIKDGKIGKEIKKDGKSREEFYQ 239
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQNEILR 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-68 |
2.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 2 SEVVQVQDITKTYGKKgekqyQALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYI 68
Cdd:PRK11819 322 DKVIEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-189 |
1.05e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 10 ITKTYGKKGEKQYQALKGISFDVARGEFVGIMGASGSGKTTLL-NILSTLDQ---PTTGNVYINGrditgLNKNQMADFR 85
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDG-----ITPEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 86 GQEIGFIFQDFNLLENLTNRENIALPLSLQNVKT--------SAINPKVDKIAKRLGIDH-----ILNKYPAEISGGQKQ 152
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgvsreEYAKHIADVYMATYGLSHtrntkVGNDFVRGVSGGERK 216
|
170 180 190
....*....|....*....|....*....|....*..
gi 489748581 153 RVAAARALVHEPAILYGDEPTGALDSKSATELLETMK 189
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-230 |
1.16e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITgLNKNQMADFRG--------QEIGfIFQDFNLL 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAIRAGimlcpedrKAEG-IIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 100 ENLtnreNIA-----LPLS-LQNVKTSAINpkVDKIAKRLGIdhilnKYPA------EISGGQKQRVAAARALVHEPAIL 167
Cdd:PRK11288 350 DNI----NISarrhhLRAGcLINNRWEAEN--ADRFIRSLNI-----KTPSreqlimNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 168 YGDEPTGALDSKSATELLETMKGLNEKdKVSILMVTHD-PYSASYASRILFIKDGKIGKEIKKD 230
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLGVADRIVVMREGRIAGELARE 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-223 |
1.40e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 30 FDVARGEFVGIMGASGSGKTTLLNILS---TLDQpttGNVYING------------RDITGlnknQMADFRG---QEIGF 91
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQdlivarlqqdppRNVEG----TVYDFVAegiEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 92 IFQDF----NLLENLTNRENIALPLSLQNVKTSA----INPKVDKIAKRLGIDHilNKYPAEISGGQKQRVAAARALVHE 163
Cdd:PRK11147 97 YLKRYhdisHLVETDPSEKNLNELAKLQEQLDHHnlwqLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 164 PAILYGDEPTGALDSKSAT---ELLETMKGlnekdkvSILMVTHD-PYSASYASRILFIKDGKI 223
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEwleGFLKTFQG-------SIIFISHDrSFIRNMATRIVDLDRGKL 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-225 |
1.94e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILStlDQP----TTGNVYINGRDITGLNKNQMADfRGQEIGFIF------- 93
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEERAH-LGIFLAFQYpieipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 94 --QDFNLLENLTNRENIAL----PLSLQNVktsaINPKVDKIakrlGID-HILNKYPAE-ISGGQKQRVAAARALVHEP- 164
Cdd:CHL00131 100 snADFLRLAYNSKRKFQGLpeldPLEFLEI----INEKLKLV----GMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSe 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489748581 165 -AILygDEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASY--ASRILFIKDGKIGK 225
Cdd:CHL00131 172 lAIL--DETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYikPDYVHVMQNGKIIK 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-206 |
2.52e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 34 RGEFVGIMGASGSGKTTLLNILST-LDQPTTGNVYINGRDITGLNKNQMadfrgqeigfifqdfnllenltnrenialpl 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 113 slqnvktsainpkvdkiakrlgIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLE-----T 187
Cdd:smart00382 50 ----------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrL 107
|
170
....*....|....*....
gi 489748581 188 MKGLNEKDKVSILMVTHDP 206
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDE 126
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-204 |
5.34e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKNQMADfrgQEIGFIFQDFNLLENL 102
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRENIAL---PLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALDSK 179
Cdd:PRK10982 89 SVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180
....*....|....*....|....*
gi 489748581 180 SATELLETMKGLNEKDkVSILMVTH 204
Cdd:PRK10982 169 EVNHLFTIIRKLKERG-CGIVYISH 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-73 |
7.50e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 7.50e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGRDI 73
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI 1374
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-222 |
1.11e-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: 48.98 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 28 ISFDVARGEFVGIMGASGSGKTTLLNILSTLdQPTTGNVYINGRDitglnknqmadfrgQEIGFIFQDfNLLENLTNREN 107
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAK--------------GKLFYVPQR-PYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 108 IALPLSLQNVKTSAINPKV-DKIAKRLGIDHILNK---------YPAEISGGQKQRVAAARALVHEP--AILygDEPTGA 175
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDlEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPqfAIL--DECTSA 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489748581 176 LdsksATELLETMKGLNEKDKVSILMVTHDPYSASYASRILFIkDGK 222
Cdd:TIGR00954 613 V----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-177 |
3.22e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILsTLDQPTTgnvYINgrDITGLNKNqmadfRG---------QEIGFIFQD 95
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHPQG---YSN--DLTLFGRR-----RGsgetiwdikKHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 FNLlenlTNRENIalplSLQNVKTS----------AINPKVDKIAK----RLGIDHILNKYP-AEISGGQKQRVAAARAL 160
Cdd:PRK10938 345 LHL----DYRVST----SVRNVILSgffdsigiyqAVSDRQQKLAQqwldILGIDKRTADAPfHSLSWGQQRLALIVRAL 416
|
170
....*....|....*..
gi 489748581 161 VHEPAILYGDEPTGALD 177
Cdd:PRK10938 417 VKHPTLLILDEPLQGLD 433
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-177 |
4.08e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 23 QALKGISFDVARGEFVGIMGASGSGKTTLlnILS----TLDQPTTGNVYINGRDITGLNknqMADFRGQEIGFIFQD--- 95
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSvfgrSYGRNISGTVFKDGKEVDVST---VSDAIDAGLAYVTEDrkg 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 --FNLLENLtnRENIALPlSLQNVKTSAInpkVDKIA---------KRLGIdhilnKYP------AEISGGQKQRVAAAR 158
Cdd:NF040905 349 ygLNLIDDI--KRNITLA-NLGKVSRRGV---IDENEeikvaeeyrKKMNI-----KTPsvfqkvGNLSGGNQQKVVLSK 417
|
170
....*....|....*....
gi 489748581 159 ALVHEPAILYGDEPTGALD 177
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-208 |
6.92e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 40 IMGASGSGKTTLLNILSTLDQPTTGNVYINGRDITGLNKnqmadfrgQEIGFIFQDFNLLENLTNRENIALPLSLQNVKT 119
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK--------PYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 120 SainpkVDKIAKRLGIDHILNKYPAEISGGQKQRVAAARALVHEPAILYGDEPTGALdSKSATELLETMKGLNEKDKVSI 199
Cdd:PRK13541 103 T-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL-SKENRDLLNNLIVMKANSGGIV 176
|
....*....
gi 489748581 200 LMVTHDPYS 208
Cdd:PRK13541 177 LLSSHLESS 185
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-223 |
1.08e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 26 KGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINGrditglnKNQMADFRGQEIGFIFQDFNLLenltnr 105
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-------KVRMAVFSQHHVDGLDLSSNPL------ 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 106 enialpLSLQNVKTSAINPKVDKIAKRLGIDHILNKYPA-EISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATEL 184
Cdd:PLN03073 593 ------LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489748581 185 LETMKGLnekdKVSILMVTHDPYSASYASRILF-IKDGKI 223
Cdd:PLN03073 667 IQGLVLF----QGGVLMVSHDEHLISGSVDELWvVSEGKV 702
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-204 |
1.46e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLD--QPTTGNVYINGRDITGLNKNQMAdfrGQEIGFIFQDFNLLENL 102
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 103 TNRenIALPLSLQNVKTSAINPKVDKIAKRLGIDH--ILNKYPAEI---------SGGQKQRVAAARALVHEPAILYGDE 171
Cdd:PRK09580 94 SNQ--FFLQTALNAVRSYRGQEPLDRFDFQDLMEEkiALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190
....*....|....*....|....*....|...
gi 489748581 172 PTGALDSKSATELLETMKGLNEkDKVSILMVTH 204
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRD-GKRSFIIVTH 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-223 |
3.21e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILS-TLDQ-------------------PTTGNVYINGRD--ITGLNKNQMA 82
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgKLDPslkvsgeityngyrlnefvPRKTSAYISQNDvhVGVMTVKETL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 83 DF--RGQEIGfifQDFNLLENLTNRENIA--LP----------LSLQNVKTSAINpkvDKIAKRLGIDHILNKYPAE--- 145
Cdd:PLN03140 261 DFsaRCQGVG---TRYDLLSELARREKDAgiFPeaevdlfmkaTAMEGVKSSLIT---DYTLKILGLDICKDTIVGDemi 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 146 --ISGGQKQRVAAARALVHEPAILYGDEPTGALDSKSATELLETMKGLNEKDKVSILMVTHDPYSASYA--SRILFIKDG 221
Cdd:PLN03140 335 rgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDlfDDIILLSEG 414
|
..
gi 489748581 222 KI 223
Cdd:PLN03140 415 QI 416
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-235 |
5.58e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 133 LGIDHI-LNKYPAEISGGQKQRVAAARalvHEPAILYG-----DEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDP 206
Cdd:PRK00635 463 LGLPYLtPERALATLSGGEQERTALAK---HLGAELIGityilDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDE 538
|
90 100 110
....*....|....*....|....*....|.
gi 489748581 207 YSASYASRILFI--KDGKIGKEIKKDGKSRE 235
Cdd:PRK00635 539 QMISLADRIIDIgpGAGIFGGEVLFNGSPRE 569
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
61-235 |
1.70e-04 |
|
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: 42.31 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 61 PTTGNVYINGRDItglnknqmADFRGQEIGFIFQDFNLLENLTNRENIALPLsLQNVKTSAinpkvdKIAKRLGIDHI-L 139
Cdd:TIGR00630 418 PEALAVTVGGKSI--------ADVSELSIREAHEFFNQLTLTPEEKKIAEEV-LKEIRERL------GFLIDVGLDYLsL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 140 NKYPAEISGGQKQRVAAAR----ALVhepAILYG-DEPTGALDSKSATELLETMKGLNEKDKvSILMVTHDPYSASYASR 214
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATqigsGLT---GVLYVlDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTIRAADY 558
|
170 180
....*....|....*....|...
gi 489748581 215 ILFI--KDGKIGKEIKKDGKSRE 235
Cdd:TIGR00630 559 VIDIgpGAGEHGGEVVASGTPEE 581
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-177 |
3.38e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 29 SFDVARGEFVGIMGASGSGKTTLLNILS--TLDQ-PTTGNVY-----INGRDITGLNKNQMADFR-----GQEIGFIFQD 95
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGiPKNCQILhveqeVVGDDTTALQCVLNTDIErtqllEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 96 FNL-LENLTNRENIAlplSLQNVKTSAINPKVDKIAKRLgidHILNKYPAE-----------------------ISGGQK 151
Cdd:PLN03073 277 RELeFETETGKGKGA---NKDGVDKDAVSQRLEEIYKRL---ELIDAYTAEaraasilaglsftpemqvkatktFSGGWR 350
|
170 180
....*....|....*....|....*.
gi 489748581 152 QRVAAARALVHEPAILYGDEPTGALD 177
Cdd:PLN03073 351 MRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-205 |
8.65e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGNVYINgrdiTGLnknqmadfrgqEIGFIFQDFNLLE-NLT 103
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKL-----------EVAYFDQHRAELDpEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 104 NRENIAlplslQNVKTSAINPKvdkiaKRlgidHILNkY-------------PAE-ISGGQKQRVAAARALVHEPAILYG 169
Cdd:PRK11147 400 VMDNLA-----EGKQEVMVNGR-----PR----HVLG-YlqdflfhpkramtPVKaLSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 489748581 170 DEPTGALDsksaTELLETMKGLNEKDKVSILMVTHD 205
Cdd:PRK11147 465 DEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-78 |
1.22e-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: 40.00 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLN--ILSTLDQPTTGNVYINGR--DITGLNK 78
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPGRytSIEGLEH 681
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-205 |
1.93e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.10 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 39 GIMGASGSGKTTLLNILSTLDQPTTGNVYI-NGRDITGLNKNQmadfrgqeigFIFQDFNLL-----------ENLTNRE 106
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ----------FAFEEFTVLdtvimghtelwEVKQERD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 107 NI-ALP-------LSLQNVKT--------SAiNPKVDKIAKRLGIDHILNKYP-AEISGGQKQRVAAARALVHEPAILYG 169
Cdd:PRK15064 101 RIyALPemseedgMKVADLEVkfaemdgyTA-EARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 489748581 170 DEPTGALDSKSaTELLETMkgLNEKDKVSILmVTHD 205
Cdd:PRK15064 180 DEPTNNLDINT-IRWLEDV--LNERNSTMII-ISHD 211
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
39-102 |
1.95e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 37.82 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489748581 39 GIMGASGSGKTTLLN--------ILSTLDQPTTGNVYINGRDITGLNKNQMADFRGQEIGFIFQDFNLLENL 102
Cdd:cd00882 1 VVVGRGGVGKSSLLNallggevgEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELARLL 72
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-219 |
2.10e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 40 IMGASGSGKTTLLNILS---TLDQPTTGNVYINGRDITGLNKNqmadfRGQ-EIGF---------IFQDFNLLENltnre 106
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyalTGELPPNSKGGAHDPKLIREGEV-----RAQvKLAFenangkkytITRSLAILEN----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 107 nialplslqnvktsAInpkvdkIAKRLGIDHILNKYPAEISGGQKQ------RVAAARALVHEPAILYGDEPTGALDSKS 180
Cdd:cd03240 97 --------------VI------FCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489748581 181 ATE-LLETMKGLNEKDKVSILMVTHDPYSASYASRILFIK 219
Cdd:cd03240 157 IEEsLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-77 |
2.79e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLN-IL-STLDQPTTGNVYINGR--DITGLN 77
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTLyKALARKLNGAKKVPGKhkEIEGLE 681
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
25-114 |
7.77e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 36.58 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489748581 25 LKGISFDVARGEFVGIMGASGSGKTTLLNILSTLDQPTTGnvyingrDITGLnknqmadfRGQEIGFIFQDFnLLENLTN 104
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEG-------DFIGL--------RGDALPLGANSF-ILPGLTG 66
|
90
....*....|
gi 489748581 105 RENIALPLSL 114
Cdd:PRK15177 67 EENARMMASL 76
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
37-74 |
9.51e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 34.90 E-value: 9.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489748581 37 FVGIMGASGSGKTTLLNILS------------TLDqPTTGNVYINGRDIT 74
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTgakaivsdypgtTRD-PNEGRLELKGKQII 49
|
|
| |
