|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-275 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 558.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 20 ENLTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYD 99
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQR 179
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
250
....*....|....*.
gi 494860364 260 TPTKKKTEDYITGRYG 275
Cdd:COG1117 243 NPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
28-274 |
3.28e-173 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 477.56 E-value: 3.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSVDVAAL 107
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTE 267
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 494860364 268 DYITGRY 274
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
29-257 |
1.98e-147 |
|
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: 411.57 E-value: 1.98e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSVDVAALR 108
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHdsAFGLSGGQQQRLVIARSIAI 188
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
29-275 |
2.60e-137 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 387.21 E-value: 2.60e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSVDVAALR 108
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAI 188
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTED 268
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 494860364 269 YITGRYG 275
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-275 |
3.27e-135 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 382.21 E-value: 3.27e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 19 LENLTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIY 98
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKrkLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQ 178
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFM---------YMGELI 249
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLV 238
|
250 260
....*....|....*....|....*.
gi 494860364 250 EYSDTNTLFTTPTKKKTEDYITGRYG 275
Cdd:PRK14243 239 EFDRTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-275 |
3.80e-102 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 298.29 E-value: 3.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSVDVAAL 107
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQG-IKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKK 265
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
250
....*....|
gi 494860364 266 TEDYITGRYG 275
Cdd:PRK14267 244 TEKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-275 |
1.00e-98 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 289.63 E-value: 1.00e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSVDVAAL 107
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELIND--LKNQFTVVIVTHNMQQAARVSDQTAFMY-----MGELIEYSDTNTLFTT 260
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNS 246
|
250
....*....|....*
gi 494860364 261 PTKKKTEDYITGRYG 275
Cdd:PRK14258 247 PHDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-273 |
1.16e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 274.10 E-value: 1.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYdkSVDVA 105
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGI-KEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTK 263
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
250
....*....|
gi 494860364 264 KKTEDYITGR 273
Cdd:PRK14247 239 ELTEKYVTGR 248
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-273 |
7.36e-83 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 249.19 E-value: 7.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDI-CRIEGEILLHGQNIYdkSVDV 104
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTK 263
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
250
....*....|
gi 494860364 264 KKTEDYITGR 273
Cdd:PRK14246 246 ELTEKYVIGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-275 |
2.68e-81 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 246.16 E-value: 2.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDKSvDVAAL 107
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTE 267
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
....*...
gi 494860364 268 DYITGRYG 275
Cdd:PRK14271 260 RYVAGLSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
29-270 |
9.20e-80 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 240.67 E-value: 9.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICriEGEILLHGQNIYDKSVDVAALR 108
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINL---LEEPD--SGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVVYGLRLqgIKeKRKLDEVVEqslRGAALWDEV--KDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIK--VK-KMSKAEAEE---RAMELLERVglADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKK 264
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*.
gi 494860364 265 KTEDYI 270
Cdd:COG1126 231 RTRAFL 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
23-261 |
1.18e-64 |
|
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: 210.53 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLDLYY-----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNI 97
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFDGKDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 YDKSV-DVAALRRNVGMVFQRP----NPFpKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRlhdSAFGL 172
Cdd:COG1123 330 TKLSRrSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR---YPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250
....*....|.
gi 494860364 251 YSDTNTLFTTP 261
Cdd:COG1123 486 DGPTEEVFANP 496
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
29-247 |
1.86e-64 |
|
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: 199.72 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKSVDVAALR 108
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVvyglrlqgikekrkldevveqslrgaalwdevkdrlhdsAFGLSGGQQQRLVIARSIA 187
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENI---------------------------------------ALGLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGE 247
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-248 |
5.50e-64 |
|
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: 199.68 E-value: 5.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDIcrIEGEILLHGQNIYDKSVDVAALR 108
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINL---LEEP--DSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVVYGLR-LQGIKEkrklDEVVEqslRGAALWDEV--KDRLHDSAFGLSGGQQQRLVIAR 184
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIkVKGMSK----AEAEE---RALELLEKVglADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 185 SIAIEPEVLLLDEPTSALDPisTLVIE--ELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDP--ELVGEvlDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
29-250 |
4.86e-63 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 196.97 E-value: 4.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICRieGEILLHGQNIydksVDVAALR 108
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG---LERPDS--GEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
29-250 |
1.26e-61 |
|
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: 194.26 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYD-KSVDVAAL 107
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL-----LRPDSGEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPF-PKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIARSI 186
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAE---LSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLK--NQFTVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
29-259 |
2.00e-60 |
|
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: 191.01 E-value: 2.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKsvDVAAL 107
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL-----LKPTSGEVLVDGKDITKK--NLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQrpNP----FPKSIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALWDeVKDRlhdSAFGLSGGQQQRLVIA 183
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEH-LADR---PPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF-TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
24-261 |
7.26e-60 |
|
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: 189.81 E-value: 7.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 24 DDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdicrI------EGEILLHGQNI 97
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI-----------IgllrpdSGEILVDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 YDKSVD-VAALRRNVGMVFQRPNPF-PKSIYENVVYGLRLQGIKEKRKLDEVVEQSLrgaalwDEVkdRLHDSAF----G 171
Cdd:COG1127 70 TGLSEKeLYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKL------ELV--GLPGAADkmpsE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|..
gi 494860364 250 EYSDTNTLFTTP 261
Cdd:COG1127 222 AEGTPEELLASD 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
28-261 |
3.08e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.85 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicriEGEILLHGQNIydksVDVAAL 107
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET-PD----SGRILLDGRDV----TGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKE---KRKLDEVVEQ-SLRGAAlwdevkDRL-HDsafgLSGGQQQRLV 181
Cdd:COG3842 76 KRNVGMVFQDYALFPhLTVAENVAFGLRMRGVPKaeiRARVAELLELvGLEGLA------DRYpHQ----LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPistLVIEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNT 256
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDA---KLREEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
....*
gi 494860364 257 LFTTP 261
Cdd:COG3842 223 IYERP 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
29-248 |
1.06e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.79 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydKSVDVAALR 108
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKR-KLDEVVEQSLRGAALWD-EVKDrlhdsafgLSGGQQQRLVIARSI 186
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKFDReRALELLERLGLPPDILDkPVER--------LSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-262 |
2.65e-58 |
|
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: 186.16 E-value: 2.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYG----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDKsvD 103
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRR--R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRRNVGMVFQRP----NPFpKSIYENVVYGLRLQGIKEKrklDEVVEQSLRGAALWDEVKDRL-HDsafgLSGGQQQ 178
Cdd:COG1124 74 RKAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNT 256
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
....*.
gi 494860364 257 LFTTPT 262
Cdd:COG1124 226 LLAGPK 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
29-251 |
1.08e-57 |
|
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: 183.86 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDV 104
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS-----GSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRN-VGMVFQRP----NPFpKSIYENVVYGLRLQGIKEKRK-LDEVVEQSLRGAALWDEVKDRLhdsAFGLSGGQQQ 178
Cdd:cd03257 77 RKIRRKeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRY---PHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
29-249 |
2.68e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRI----EGEILLHGQNIYDKSVDV 104
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML---------LGLlrptSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 aalRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIA 183
Cdd:COG1131 72 ---RRRIGYVPQEPALYPDlTVRENLRFFARLYGLP-RKEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF-TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGkTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
23-243 |
3.55e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 181.06 E-value: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLDLYY----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmnDLVDIcrIEGEILLHGQniy 98
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKP--TSGEVLVDGK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 dksvDVAALRRNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKeKRKLDEVVEQSLrgaalwdevkDRLHDSAFG------ 171
Cdd:COG1116 74 ----PVTGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGVP-KAERRERARELL----------ELVGLAGFEdayphq 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFM 243
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
30-243 |
4.35e-56 |
|
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: 179.20 E-value: 4.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVdvAAL 107
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLSL--KEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQrpNP----FPKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDevkdRLHDSAFGLSGGQQQRLVIA 183
Cdd:cd03225 74 RRKVGLVFQ--NPddqfFGPTVEEEVAFGLENLGLPEE-EIEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFM 243
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
29-248 |
7.91e-56 |
|
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: 178.84 E-value: 7.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD----KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYDKS-VD 103
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-DRPT----SGEVRVDGTDISKLSeKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRR-NVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLV 181
Cdd:cd03255 76 LAAFRRrHIGFVFQSFNLLPDlTALENVELPLLLAGVP-KKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMqQAARVSDQTAFMYMGEL 248
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
29-270 |
8.39e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 179.52 E-value: 8.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDVAALR 108
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITS-----GDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYG-LRLQGIKeKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSI 186
Cdd:PRK09493 77 QEAGMVFQQFYLFPHlTALENVMFGpLRVRGAS-KEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKK 265
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQR 231
|
....*
gi 494860364 266 TEDYI 270
Cdd:PRK09493 232 LQEFL 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
29-238 |
2.36e-55 |
|
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: 177.66 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQ----ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQniydksvDV 104
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGE-------PV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKEKRKLDEVveqslrgAALWDEV--KDRLHDSAFGLSGGQQQRLV 181
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERA-------EELLELVglSGFENAYPHQLSGGMRQRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSD 238
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLAD 200
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
28-259 |
9.76e-55 |
|
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: 177.16 E-value: 9.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIydKSVDVAAL 107
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-----SSGEVLLDGRDL--ASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPN-PFPKSIYENVVYGlRL--QGI--KEKRKLDEVVEQSLRGAALWDeVKDRLHDSafgLSGGQQQRLVI 182
Cdd:COG1120 74 ARRIAYVPQEPPaPFGLTVRELVALG-RYphLGLfgRPSAEDREAVEEALERTGLEH-LADRPVDE---LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
37-270 |
1.24e-54 |
|
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: 176.72 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIydKSVDVAALRRNVGMVFQ 116
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL-----IEPTSGEIFIDGEDI--REQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFP-KSIYENVVYGLRLQGIKEKRKlDEVVEQSLRGAALWD-EVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVLL 194
Cdd:cd03295 83 QIGLFPhMTVEENIALVPKLLKWPKEKI-RERADELLALVGLDPaEFADRYPHE---LSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 195 LDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDYI 270
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
29-261 |
1.52e-54 |
|
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: 176.23 E-value: 1.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYDKS-VD 103
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPT----SGSVLVDGTDLTLLSgKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRRNVGMVFQRPNPF-PKSIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVI 182
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTT 260
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
.
gi 494860364 261 P 261
Cdd:cd03258 232 P 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-261 |
7.27e-54 |
|
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: 177.17 E-value: 7.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDICRIEGEILLHGQNIYDKS-VD 103
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLLKLSeKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALR-RNVGMVFQRP----NPFpKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALwDEVKDRLHDSAFGLSGGQQQ 178
Cdd:COG0444 80 LRKIRgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDpistlV-----IEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALD-----VtiqaqILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250
....*....|
gi 494860364 252 SDTNTLFTTP 261
Cdd:COG0444 233 GPVEELFENP 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
26-263 |
3.26e-53 |
|
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: 180.48 E-value: 3.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndLVDICRIEGEILLHGQNIYDKSVD 103
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VaaLRRNVGMVFQRP--NPFPKSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLV 181
Cdd:COG1123 80 L--RGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLS-RAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
....
gi 494860364 260 TPTK 263
Cdd:COG1123 233 APQA 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
26-250 |
2.58e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.22 E-value: 2.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYDKS 101
Cdd:COG1136 2 SPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL-DRPT----SGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 VD-VAALRR-NVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDEVVEqslrgaALwDEV--KDRLHDSAFGLSGGQ 176
Cdd:COG1136 77 EReLARLRRrHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARE------LL-ERVglGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELIE 250
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-249 |
3.39e-51 |
|
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: 168.78 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG-----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcINRMNDLvdICRIEGEILLHGQNIY-DKSV 102
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTL---IQHLNGL--LKPTSGTVTIDGRDITaKKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEVKDRlhdSAFGLSGGQQQRL 180
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEE-EAEERVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
29-261 |
7.01e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 169.87 E-value: 7.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvdicrIE----GEILLHGQNIYD- 99
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------LErptsGSVLVDGVDLTAl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVDVAALRRNVGMVFQRPNPFP-KSIYENVVYGLRLQGI-KEKRKLdevveqslRGAALWDEV--KDRLHDSAFGLSGG 175
Cdd:COG1135 73 SERELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGVpKAEIRK--------RVAELLELVglSDKADAYPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSD 253
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
....*...
gi 494860364 254 TNTLFTTP 261
Cdd:COG1135 225 VLDVFANP 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
29-236 |
4.02e-50 |
|
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: 162.55 E-value: 4.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDksVDVAA 106
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDLRD--LDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVvyglrlqgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSI 186
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARV 236
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA 161
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
29-261 |
6.29e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 167.63 E-value: 6.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI------NRmndlvdicrieGEILLHGQNIYdksV 102
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpDS-----------GRIVLNGRDLF---T 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKlDEVVEQSLrgaalwdevkDRLHDSAFG------LSGG 175
Cdd:COG1118 69 NLPPRERRVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEI-RARVEELL----------ELVQLEGLAdrypsqLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIE----ELINDLknQFTVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRrwlrRLHDEL--GGTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250
....*....|
gi 494860364 252 SDTNTLFTTP 261
Cdd:COG1118 216 GTPDEVYDRP 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
30-254 |
2.26e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 164.88 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdicrIE---GEILLHGQNIydKSVDVA 105
Cdd:COG1125 3 EFENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL--------IEptsGRILIDGEDI--RDLDPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKEKRKLDEVVEqslrgaaLWDEVKdrLHDSAFG------LSGGQQQ 178
Cdd:COG1125 73 ELRRRIGYVIQQIGLFPhMTVAENIATVPRLLGWDKERIRARVDE-------LLELVG--LDPEEYRdrypheLSGGQQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYsDT 254
Cdd:COG1125 144 RVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQY-DT 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-271 |
4.08e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 162.49 E-value: 4.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndLVDICR-----IEGEILLHGQNIYDKsv 102
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLEMPRsgtlnIAGNHFDFSKTPSDK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNVGMVFQRPNPFPK-SIYENVVYG-LRLQGIKEkrklDEVVEQSlrgaalwDEVKDRLHDSAFG------LSG 174
Cdd:PRK11124 76 AIRELRRNVGMVFQQYNLWPHlTVQQNLIEApCRVLGLSK----DQALARA-------EKLLERLRLKPYAdrfplhLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSD 253
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
250
....*....|....*...
gi 494860364 254 tNTLFTTPTKKKTEDYIT 271
Cdd:PRK11124 225 -ASCFTQPQTEAFKNYLS 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-270 |
2.01e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndLVDICRiEGEILLHG------QNIYDKs 101
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN----LLETPD-SGQLNIAGhqfdfsQKPSEK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 vDVAALRRNVGMVFQRPNPFPK-SIYENVVYG-LRLQGI-KE--KRKLDEVVEQsLRgaalWDEVKDR--LHdsafgLSG 174
Cdd:COG4161 76 -AIRLLRQKVGMVFQQYNLWPHlTVMENLIEApCKVLGLsKEqaREKAMKLLAR-LR----LTDKADRfpLH-----LSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSD 253
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
250
....*....|....*..
gi 494860364 254 TNtLFTTPTKKKTEDYI 270
Cdd:COG4161 225 AS-HFTQPQTEAFAHYL 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
29-248 |
2.12e-48 |
|
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: 158.33 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI--NRMNDlvdicriEGEILLHGQNIYDKSVDVaa 106
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgLLKPD-------SGEIKVLGKDIKKEPEEV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 lRRNVGMVFQRPNPFPK-SIYENVVYglrlqgikekrkldevveqslrgaalwdevkdrlhdsafglSGGQQQRLVIARS 185
Cdd:cd03230 72 -KRRIGYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF-TVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
27-238 |
2.64e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.61 E-value: 2.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDL-YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNI-YDKSVDV 104
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVtALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGL--RLQGIKEKRKL--DEVVEQSLrgAALwDEV--KDRLHDSAFGLSGGQQ 177
Cdd:COG3638 76 RRLRRRIGMIFQQFNLVPRlSVLTNVLAGRlgRTSTWRSLLGLfpPEDRERAL--EAL-ERVglADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 178 QRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSD 238
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRYAD 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
26-250 |
2.86e-48 |
|
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: 170.01 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydKSVD 103
Cdd:COG2274 471 KGDIELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDL--RQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRRNVGMVFQRPNPFPKSIYENVVYGlrlqgiKEKRKLDEVVEqSLRGAALWDEVKD-------RLHDSAFGLSGGQ 176
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFSGTIRENITLG------DPDATDEEIIE-AARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIE 250
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVE 689
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
29-257 |
1.94e-47 |
|
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: 158.10 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicriEGEILLHGqniYDKSVDVAALR 108
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK-PD----SGSILIDG---EDVRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRpNPFPK--SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHdsafGLSGGQQQRLVIARSI 186
Cdd:COG4555 74 RQIGVLPDE-RGLYDrlTVRENIRYFAELYGLF-DEELKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-261 |
3.34e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 160.62 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmNDLVDICriEGEILLHGQNIydksVDVAAL 107
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI---AGLEDPT--SGEILIGGRDV----TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKE---KRKLDEVVEqslrgaALwdEVKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:COG3839 74 DRNIAMVFQSYALYPhMTVYENIAFPLKLRKVPKaeiDRRVREAAE------LL--GLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
44-200 |
3.44e-47 |
|
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: 154.34 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIYDKsvDVAALRRNVGMVFQRPNPFP- 122
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-----TEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 123 KSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTS 200
Cdd:pfam00005 74 LTVRENLRLGLLLKGLS-KREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
29-249 |
7.68e-47 |
|
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: 156.44 E-value: 7.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDVAAlR 108
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF-----LRPTSGSVLFDGEDITGLPPHEIA-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQG---------IKEKRKLDEVVEQSLRGAALWDevkdRLHDSAFGLSGGQQQ 178
Cdd:cd03219 75 LGIGRTFQIPRLFPElTVLENVMVAAQARTgsglllaraRREEREARERAEELLERVGLAD----LADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-266 |
9.75e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 9.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 24 DDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQniydksvD 103
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-----SGTVRLFGK-------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRRNVGMVFQRPN---PFPKSIYENVVYGLR-----LQGIKEKRKldEVVEQSLR--GAAlwdEVKDRLhdsaFG-L 172
Cdd:COG1121 70 PRRARRRIGYVPQRAEvdwDFPITVRDVVLMGRYgrrglFRRPSRADR--EAVDEALErvGLE---DLADRP----IGeL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMyMGELIEY 251
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLL-NRGLVAH 219
|
250
....*....|....*
gi 494860364 252 SDTNTLFTTPTKKKT 266
Cdd:COG1121 220 GPPEEVLTPENLSRA 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
28-250 |
1.53e-46 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 156.50 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICriEGEILLHGQNIYDKS------ 101
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINL---LETPD--SGEIRVGGEEIRLKPdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 --VD---VAALRRNVGMVFQRPNPFP-KSIYENVVYG-LRLQGIKEkrklDEVVEqslRGAALWDEV--KDRLHDSAFGL 172
Cdd:COG4598 83 vpADrrqLQRIRTRLGMVFQSFNLWShMTVLENVIEApVHVLGRPK----AEAIE---RAEALLAKVglADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPisTLVIEEL--INDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGeLI 249
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP--ELVGEVLkvMRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQG-RI 232
|
.
gi 494860364 250 E 250
Cdd:COG4598 233 E 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
28-257 |
3.34e-46 |
|
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: 162.62 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIydKSVDVAA 106
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-----YSGSILINGVDL--SDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENvvygLRLQGIKEKrklDEVVEQSLRGAALWDEVKD-------RLHDSAFGLSGGQQQR 179
Cdd:COG4988 409 WRRQIAWVPQNPYLFAGTIREN----LRLGRPDAS---DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTL 257
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
29-248 |
4.96e-46 |
|
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: 154.32 E-value: 4.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydksVDVAALR 108
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKDI----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIARSIA 187
Cdd:cd03300 72 RPVNTVFQNYALFPHlTVFENIAFGLRLKKLPKA-EIKERVAEALDLVQL-EGYANRKPSQ---LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 188 IEPEVLLLDEPTSALDpisTLVIEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:cd03300 147 NEPKVLLLDEPLGALD---LKLRKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-270 |
1.14e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 153.75 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDICRIE-GEILLHG-QNIYDKSVDVA 105
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLL-EQPEAGTIRvGDITIDTaRSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNPFP-KSIYENVVYGlrlQGIKEKRKLDEVVEqslRGAALWDEVKDRLHDSAFG--LSGGQQQRLVI 182
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPhRTVLENIIEG---PVIVKGEPKEEATA---RARELLAKVGLAGKETSYPrrLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPisTLVIEEL--INDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP--ELVGEVLntIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
250
....*....|.
gi 494860364 260 TPTKKKTEDYI 270
Cdd:PRK11264 234 DPQQPRTRQFL 244
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
29-231 |
2.15e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.13 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYD-KSVDVAA 106
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPT----SGQVLVNGQDLSRlKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQ--R--PNpfpKSIYENVVYGLRLQGiKEKRKLDEVVEQSLrgaalwDEV--KDRLHDSAFGLSGGQQQRL 180
Cdd:COG2884 77 LRRRIGVVFQdfRllPD---RTVYENVALPLRVTG-KSRKEIRRRVREVL------DLVglSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLkNQF--TVVIVTHNMQ 231
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRgtTVLIATHDLE 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
29-243 |
2.16e-45 |
|
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: 152.20 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNdLVDIcrIEGEILLHGQNIYDKSVDVAAlR 108
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MG-LLPP--RSGSIRFDGRDITGLPPHERA-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGI-KEKRKLDEVVEqslrgaaLWDEVKDRLHDSAFGLSGGQQQRLVIARSI 186
Cdd:cd03224 75 AGIGYVPEGRRIFPElTVEENLLLGAYARRRaKRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFM 243
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVL 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-228 |
3.72e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 159.95 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 21 NLTDDQKALEIKDLDLYY-GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicriEGEILLHGQNIyd 99
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-PT----SGRILIDGVDI-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGlrlqgikekrKL---DEVVEQSLRGAALWDEVKD-------RLHDSA 169
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG----------RPdatDEEVEEAAKAAQAHEFIEAlpdgydtVVGERG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 170 FGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
30-247 |
6.73e-45 |
|
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: 148.93 E-value: 6.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydKSVDVAALRR 109
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 NVGMVFQrpnpfpksiyenvvyglrlqgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSIAIE 189
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 190 PEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGE 247
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
30-249 |
9.72e-45 |
|
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: 149.12 E-value: 9.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIydKSVDVAALRR 109
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL-----LKPSSGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 NVGMVFQrpnpfpksiyenvvyGLRLQGIKEKrkldevveqslrgaalwdevKDRLHDSafgLSGGQQQRLVIARSIAIE 189
Cdd:cd03214 74 KIAYVPQ---------------ALELLGLAHL--------------------ADRPFNE---LSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 190 PEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-262 |
1.08e-44 |
|
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: 150.95 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDvaal 107
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS-----GTILFGGEDATDVPVQ---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDEV---VEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIA 183
Cdd:cd03296 73 ERNVGFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIrakVHELLKLVQL-DWLADRYPAQ---LSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDpisTLVIEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLF 258
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALD---AKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....
gi 494860364 259 TTPT 262
Cdd:cd03296 226 DHPA 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
43-270 |
1.89e-44 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 151.26 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICRieGEILLHGQNIYDKS-VDVAALRRN-VGMVFQRPNP 120
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAAMSrKELRELRRKkISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 FP-KSIYENVVYGLRLQGIKEKRKLdEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPT 199
Cdd:cd03294 114 LPhRTVLENVAFGLEVQGVPRAERE-ERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 200 SALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPtkkkTEDYI 270
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP----ANDYV 257
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
29-238 |
3.21e-44 |
|
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: 149.64 E-value: 3.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNI-YDKSVDVAA 106
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDInKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPK-SIYENVVYG-----------LRLQGIKEKRkldevveqslRGAALWDEV--KDRLHDSAFGL 172
Cdd:cd03256 76 LRRQIGMIFQQFNLIERlSVLENVLSGrlgrrstwrslFGLFPKEEKQ----------RALAALERVglLDKAYQRADQL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSD 238
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYAD 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
39-270 |
2.41e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 150.34 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNdlvdicR-IEGEILLHGQNIydKSVDVAAL---RRNVGMV 114
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE------RpTSGRVLVDGQDL--TALSEKELrkaRRQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 FQRPNPFP-KSIYENVVYGLRLQGiKEKRKLDEVVEQSLRGAALWDevkdrLHDS--AfGLSGGQQQRLVIARSIAIEPE 191
Cdd:PRK11153 88 FQHFNLLSsRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSD-----KADRypA-QLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 192 VLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDY 269
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
.
gi 494860364 270 I 270
Cdd:PRK11153 241 I 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-261 |
3.46e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 149.50 E-value: 3.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLDLYY-----------GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEIL 91
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-----SGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 92 LHGQNIYDKSV-DVAALRRNVGMVFQRP----NPfPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRL- 165
Cdd:COG4608 77 FDGQDITGLSGrELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 166 HDsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALD-PISTLVIeELINDLKNQF--TVVIVTHNMQQAARVSDQTAF 242
Cdd:COG4608 156 HE----FSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVL-NLLEDLQDELglTYLFISHDLSVVRHISDRVAV 230
|
250
....*....|....*....
gi 494860364 243 MYMGELIEYSDTNTLFTTP 261
Cdd:COG4608 231 MYLGKIVEIAPRDELYARP 249
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
39-272 |
6.60e-43 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 150.00 E-value: 6.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVD--VAALRRNVGMVFQ 116
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL-----IEPTAGQIFIDGENIMKQSPVelREVRRKKIGMVFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFP-KSIYENVVYGLRLQGI-KEKRKldEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVLL 194
Cdd:TIGR01186 79 QFALFPhMTILQNTSLGPELLGWpEQERK--EKALELLKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 195 LDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDYITG 272
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLqaTLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-228 |
8.20e-43 |
|
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: 146.15 E-value: 8.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYY---GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIydKSVDVAA 106
Cdd:cd03249 2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDI--RDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVVYGlrlqgiKEKRKlDEVVEQSLRGAALWDEVKD-------RLHDSAFGLSGGQQQR 179
Cdd:cd03249 75 LRSQIGLVSQEPVLFDGTIAENIRYG------KPDAT-DEEVEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQKQR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
29-275 |
2.77e-42 |
|
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: 144.75 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG-DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYD-KSVDVAA 106
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDITKlRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFP-KSIYENVVYGlRLQGIKEKRKLDEVV--EQSLRGAALWDEV--KDRLHDSAFGLSGGQQQRLV 181
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVLHG-RLGYKPTWRSLLGRFseEDKERALSALERVglADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIeysdtntlFT 259
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKYADRIVGLKAGEIV--------FD 227
|
250
....*....|....*.
gi 494860364 260 TPTKKKTEDYITGRYG 275
Cdd:TIGR02315 228 GAPSELDDEVLRHIYG 243
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
43-249 |
1.60e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 146.79 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICRieGEILLHGQNIYdkSVDVAAL----RRNVGMVFQRP 118
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNR---LIEPTA--GEVLIDGEDIT--KLSKKELrelrRKKMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 NPFP-KSIYENVVYGLRLQGI-KEKR--KLDEVVEQ-SLRGaalWdevKDRLHDSafgLSGGQQQRLVIARSIAIEPEVL 193
Cdd:COG4175 115 ALLPhRTVLENVAFGLEIQGVpKAERreRAREALELvGLAG---W---EDSYPDE---LSGGMQQRVGLARALATDPDIL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 194 LLDEPTSALDPistlvieeLI-NDLKNQF---------TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG4175 186 LMDEAFSALDP--------LIrREMQDELlelqaklkkTIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-249 |
1.86e-41 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 141.87 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQ--ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmnDLVDICRieGEILLHGqniYDKSVDVAA 106
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT---GELRPTS--GTAYING---YSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALwDEVKDRLhdsAFGLSGGQQQRLVIARS 185
Cdd:cd03263 73 ARQSLGYCPQFDALFDElTVREHLRFYARLKGL-PKSEIKEEVELLLRVLGL-TDKANKR---ARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-270 |
3.09e-41 |
|
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: 142.09 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNkVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDvaalR 108
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGF-----IKPDSGKILLNGKDITNLPPE----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKEK---RKLDEVVEqSLRGAALwdevkdrLHDSAFGLSGGQQQRLVIAR 184
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKKRKVDKKeieRKVLEIAE-MLGIDHL-------LNRKPETLSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 185 SIAIEPEVLLLDEPTSALDPistLVIEELINDLK-----NQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDV---RTKEKLREELKkirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
250
....*....|.
gi 494860364 260 TPTKKKTEDYI 270
Cdd:cd03299 220 KPKNEFVAEFL 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-249 |
7.39e-41 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 140.58 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICRIE-GEILLHGqniYDKSVDVAAL 107
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKM------LTTLLKPTsGRATVAG---HDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWdEVKDRLhdsAFGLSGGQQQRLVIARSI 186
Cdd:cd03265 72 RRRIGIVFQDLSVDDElTGWENLYIHARLYGVP-GAERRERIDELLDFVGLL-EAADRL---VKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-261 |
7.76e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 144.09 E-value: 7.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKSVDvaalR 108
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK-----PTEGQIFIDGEDVTHRSIQ----Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGI-KEKRKldEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIARSI 186
Cdd:PRK11432 78 RDICMVFQSYALFPHmSLGENVGYGLKMLGVpKEERK--QRVKEALELVDL-AGFEDRYVDQ---ISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
28-250 |
1.05e-40 |
|
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: 147.61 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDksVDVA 105
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDLRD--LDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNPFPKSIYENvvygLRL--QGIKekrklDEVVEQSLRGAALWDEVKD-------RLHDSAFGLSGGQ 176
Cdd:COG4987 406 DLRRRIAVVPQRPHLFDTTLREN----LRLarPDAT-----DEELWAALERVGLGDWLAAlpdgldtWLGEGGRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTlviEELINDLKNQF---TVVIVTHNMQQAARVsDQTAFMYMGELIE 250
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEALagrTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
29-249 |
1.33e-40 |
|
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: 140.12 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNdLVDICRieGEILLHGQNIYDKSVDVAAlR 108
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SG-LLPPRS--GSIRFDGEDITGLPPHRIA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRK--LDEVVEqslrgaaLWDEVKDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:COG0410 78 LGIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRadLERVYE-------LFPRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 186 IAIEPEVLLLDEPTSALDPIstLV--IEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPL--IVeeIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
40-249 |
6.92e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 6.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDVAALRRNVGMVFQRP- 118
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL-----LKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 -NPFPKSIYENVVYGLRLQGIKEKRKLDEVVEqSLRGAAL-WDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLD 196
Cdd:PRK13637 94 yQLFEETIEKDIAFGPINLGLSEEEIENRVKR-AMNIVGLdYEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 197 EPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
29-270 |
8.64e-40 |
|
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: 141.33 E-value: 8.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDKSVDvaalR 108
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDITRLPPQ----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALwDEVKDRlHDSAfgLSGGQQQRLVIARSIA 187
Cdd:TIGR03265 76 RDYGIVFQSYALFPNlTVADNIAYGLKNRGMG-RAEVAERVAELLDLVGL-PGSERK-YPGQ--LSGGQQQRVALARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALDpisTLVIEEL---INDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:TIGR03265 151 TSPGLLLLDEPLSALD---ARVREHLrteIRQLQRRLgvTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPA 227
|
....*...
gi 494860364 263 KKKTEDYI 270
Cdd:TIGR03265 228 TPFVADFV 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
28-249 |
1.34e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 138.25 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYDKSVDVAAl 107
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF-YRPT----SGRILFDGRDITGLPPHRIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQG--------------IKEKRKLDEVVEQSLRGAALwdevKDRLHDSAFGL 172
Cdd:COG0411 78 RLGIARTFQNPRLFPElTVLENVLVAAHARLgrgllaallrlpraRREEREARERAEELLERVGL----ADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
30-241 |
1.43e-39 |
|
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: 136.89 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGQNIYDKsvdvaalRR 109
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI-----LGLLKPTSGSIRVFGKPLEKE-------RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 NVGMVFQRPN---PFPKSIYENVVYGLR-----LQGIKEKRKldEVVEQSLR--GAAlwdEVKDRLHDSafgLSGGQQQR 179
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGLYghkglFRRLSKADK--AKVDEALErvGLS---ELADRQIGE---LSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTA 241
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-259 |
3.51e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 140.47 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 20 ENLTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIyd 99
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 ksVDVAALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQ 178
Cdd:PRK09452 79 --THVPAENRHVNTVFQSYALFPHmTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQLEEFAQRKPHQ----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDpisTLVIEELINDLKN-Q----FTVVIVTHNMQQAARVSDQTAFMYMGElIE--- 250
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD---YKLRKQMQNELKAlQrklgITFVFVTHDQEEALTMSDRIVVMRDGR-IEqdg 227
|
250
....*....|....
gi 494860364 251 -----YSDTNTLFT 259
Cdd:PRK09452 228 tpreiYEEPKNLFV 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
53-252 |
3.67e-39 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 135.89 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 53 KGQVTAFIGPSGCGKSTLLRCInrmndlVDICRIE-GEILLHGQNIYD--KSVDVAALRRNVGMVFQRPNPFPK-SIYEN 128
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCI------AGLEKPDgGTIVLNGTVLFDsrKKINLPPQQRKIGLVFQQYALFPHlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 129 VVYGLRLQGIKEKRKLdevVEQSLRGAALwDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTL 208
Cdd:cd03297 96 LAFGLKRKRNREDRIS---VDELLDLLGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494860364 209 VIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYS 252
Cdd:cd03297 169 QLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
37-249 |
6.19e-39 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 137.91 E-value: 6.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGqniYDKSVDVAALRRNVGMVF 115
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRM------LTTLLRpTSGTARVAG---YDVVREPRKVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 116 QRPNPFPK-SIYENVVYGLRLQGIKEKRKlDEVVEQSLRGAALWDEVKDRLHdsafGLSGGQQQRLVIARSIAIEPEVLL 194
Cdd:TIGR01188 73 QYASVDEDlTGRENLEMMGRLYGLPKDEA-EERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 195 LDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEgVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
29-248 |
8.28e-39 |
|
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: 135.07 E-value: 8.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILlhgqnIYDKSV-DVAAL 107
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS-----GRIY-----IGGRDVtDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFP-KSIYENVVYGLRLQgikeKRKLDEVVEQSLRGAALW--DEVKDRLHDSafgLSGGQQQRLVIAR 184
Cdd:cd03301 71 DRDIAMVFQNYALYPhMTVYDNIAFGLKLR----KVPKDEIDERVREVAELLqiEHLLDRKPKQ---LSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 185 SIAIEPEVLLLDEPTSALDpisTLVIEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLD---AKLRVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-270 |
1.33e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.88 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDkQALNkVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIYDKSVDvaalR 108
Cdd:COG3840 2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP-----DSGRILWNGQDLTALPPA----E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVvyGLrlqGIKEKRKLDEVVEQSLRGAA----LwDEVKDRLHDSafgLSGGQQQRLVIA 183
Cdd:COG3840 71 RPVSMLFQENNLFPHlTVAQNI--GL---GLRPGLKLTAEQRAQVEQALervgL-AGLLDRLPGQ---LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPIstLVIE--ELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|.
gi 494860364 260 TPTKKKTEDYI 270
Cdd:COG3840 220 GEPPPALAAYL 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-272 |
8.88e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.56 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIY-----DK 100
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK-----PSEGSIVVNGQTINlvrdkDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVA------ALRRNVGMVFQRPNPFPK-SIYENV------VYGLRLQGIKEK--RKLDEV-VEQSLRGaalwdevKDR 164
Cdd:PRK10619 78 QLKVAdknqlrLLRTRLTMVFQHFNLWSHmTVLENVmeapiqVLGLSKQEARERavKYLAKVgIDERAQG-------KYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 165 LHdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFM 243
Cdd:PRK10619 151 VH-----LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFL 225
|
250 260
....*....|....*....|....*....
gi 494860364 244 YMGELIEYSDTNTLFTTPTKKKTEDYITG 272
Cdd:PRK10619 226 HQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
37-237 |
1.13e-37 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 131.99 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYD-KSVDVAALRRNVGMVF 115
Cdd:TIGR02673 11 YPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPS-----RGQVRIAGEDVNRlRGRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 116 QRPNPFP-KSIYENVVYGLRLQGIKEkRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLL 194
Cdd:TIGR02673 86 QDFRLLPdRTVYENVALPLEVRGKKE-REIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494860364 195 LDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVS 237
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATHDLSLVDRVA 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
37-250 |
1.37e-37 |
|
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: 132.35 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydKSVDVAALRRNVGMVFQ 116
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI--REVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPKSIYENVVYGlRLQGIkekrklDEVVEQSLRGAALWDEVKdRL---HDSAFG-----LSGGQQQRLVIARSIAI 188
Cdd:cd03253 83 DTVLFNDTIGYNIRYG-RPDAT------DEEVIEAAKAAQIHDKIM-RFpdgYDTIVGerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGELIE 250
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
29-250 |
2.40e-37 |
|
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: 131.19 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRI-EGEILLHGQNIydksVDVAAL 107
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII------LGLIKPdSGEITFDGKSY----QKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRkldevVEQSLrgaalwDEV--KDRLHDSAFGLSGGQQQRLVIAR 184
Cdd:cd03268 71 LRRIGALIEAPGFYPNlTARENLRLLARLLGIRKKR-----IDEVL------DVVglKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-249 |
4.64e-37 |
|
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: 130.07 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKsvdvaALR 108
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAK-----ERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNP--FPKSIYENVVYGLrlqgiKEKRKLDEVVEQSLRGAALWDEvKDRlHdsAFGLSGGQQQRLVIARSI 186
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGL-----KELDAGNEQAETVLKDLDLYAL-KER-H--PLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIV-THNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIViTHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-228 |
5.00e-37 |
|
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: 137.42 E-value: 5.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 22 LTDDQKALEIKDLDLYYGDK-QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICriEGEILLHGQNIYDk 100
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG---FVDPT--EGSIAVNGVPLAD- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 sVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGikekrklDEVVEQSLRGAALWDEVKDR-------LHDSAFGLS 173
Cdd:TIGR02857 389 -ADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDAS-------DAEIREALERAGLDEFVAALpqgldtpIGEGGAGLS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-249 |
8.88e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 130.90 E-value: 8.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDvaALR 108
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS-----GTVFLGDKPISMLSSR--QLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPnPFPK--SIYENVVYG----LRLQGiKEKRKLDEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVI 182
Cdd:PRK11231 76 RRLALLPQHH-LTPEgiTVRELVAYGrspwLSLWG-RLSAEDNARVNQAMEQTRI-NHLADRRLTD---LSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDpISTLV-IEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQVeLMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-254 |
9.06e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 133.29 E-value: 9.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydksVDVAAL 107
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH-----QTSGHIRFHGTDV----SRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRL---------QGIKEK-RKLDEVVEQSlrgaalwdEVKDRLHDSafgLSGGQ 176
Cdd:PRK10851 73 DRKVGFVFQHYALFRHmTVFDNIAFGLTVlprrerpnaAAIKAKvTQLLEMVQLA--------HLADRYPAQ---LSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDpisTLVIEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGElIEY 251
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALD---AQVRKELRRWLRQlheelKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQ 217
|
...
gi 494860364 252 SDT 254
Cdd:PRK10851 218 AGT 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-250 |
1.17e-36 |
|
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: 130.04 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQ--ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicriEGEILLHGQNIYDksVDVAA 106
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD-VD----SGRILIDGHDVRD--YTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVVYGLRlqgikekRKLDEVVEQSLRgAALWDEVKDRL---HDSAFG-----LSGGQQQ 178
Cdd:cd03251 74 LRRQIGLVSQDVFLFNDTVAENIAYGRP-------GATREEVEEAAR-AANAHEFIMELpegYDTVIGergvkLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMqQAARVSDQTAFMYMGELIE 250
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRL-STIENADRIVVLEDGKIVE 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-261 |
1.31e-36 |
|
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: 135.97 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-----------GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNdlvdicRIEGEILLHGQNI 97
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 YDKSV-DVAALRRNVGMVFQrpNPF----PK-SIYENVVYGLRLQGIKEKRK-LDEVVEQSLRGAALWDEVKDRL-HDsa 169
Cdd:COG4172 350 DGLSRrALRPLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGLSAAeRRARVAEALEEVGLDPAARHRYpHE-- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 170 fgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTLV-IEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMG 246
Cdd:COG4172 426 --FSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLqrEHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
250
....*....|....*
gi 494860364 247 ELIEYSDTNTLFTTP 261
Cdd:COG4172 503 KVVEQGPTEQVFDAP 517
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
29-257 |
1.40e-36 |
|
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: 129.57 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNdLVDICRieGEILLHGQNIYDKSVDVAAlR 108
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MG-LLPVKS--GSIRLDGEDITKLPPHERA-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDEVVEqslrgaaLWDEVKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:TIGR03410 75 AGIAYVPQGREIFPRlTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
60-262 |
2.35e-36 |
|
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: 131.85 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 60 IGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIydksVDVAALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGI 138
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGF-EQPD----SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHmTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 139 kEKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLK 218
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494860364 219 NQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
29-249 |
2.74e-36 |
|
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: 129.86 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndLVDIcriEGEILLHGQNIYDKSvDVAA 106
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEE-NLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRP-NPFPKSIYEN-VVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEvkdRLHDSAFgLSGGQQQRLVIAR 184
Cdd:TIGR04520 75 IRKKVGMVFQNPdNQFVGATVEDdVAFGLENLGVPRE-EMRKRVDEALKLVGMEDF---RDREPHL-LSGGQKQRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELI 249
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIV 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
37-229 |
6.16e-36 |
|
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: 127.52 E-value: 6.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRIE----GEILLHGQNIYD-KSVDVAALRRNV 111
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI---------YKEElptsGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 112 GMVFQRPNPFPK-SIYENVVYGLRLQGIKEKrkldevvEQSLRGAALWDEV--KDRLHDSAFGLSGGQQQRLVIARSIAI 188
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGVPPR-------EIRKRVPAALELVglSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHN 229
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-249 |
6.54e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.58 E-value: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDVAAL 107
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI-----LKPSSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAAlwdeVKDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:PRK13636 81 RESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPED-EVRKRVDNALKRTG----IEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-249 |
1.04e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.98 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG-----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinRMNDLVDicRIEGEILLHGQNIYD--KS 101
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQ---HLNGLLQ--PTSGTVTIGERVITAgkKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 VDVAALRRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKE---KRKLDEVVEqsLRGaaLWDEVKDRlhdSAFGLSGGQ 176
Cdd:PRK13634 78 KKLKPLRKKVGIVFQFPEHqlFEETVEKDICFGPMNFGVSEedaKQKAREMIE--LVG--LPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
28-257 |
1.31e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 128.31 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNdLVDicriEGEILLHGQNIYDKSVdvAA 106
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQ----RGRVKVMGREVNAENE--KW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDeVKDRlhdSAFGLSGGQQQRLVIAR 184
Cdd:PRK13647 77 VRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLD-KDEVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
37-233 |
1.31e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.00 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvDICRIE-GEILLHGQNI-YDKSvDVAALRRNVGMV 114
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN------GLLRPQsGAVLIDGEPLdYSRK-GLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 FQRPNP--FPKSIYENVVYGLRLQGIKEKRkLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEV 192
Cdd:TIGR01166 74 FQDPDDqlFAADVDQDVAFGPLNLGLSEAE-VERRVREALTAVGASGLRERPTHC----LSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 193 LLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQA 233
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-233 |
1.91e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 127.67 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYG----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVD 103
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-----LAPSSGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 vaalrRnvGMVFQRPNPFP-KSIYENVVYGLRLQGI-KEKRKldEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLV 181
Cdd:COG4525 78 -----R--GVVFQKDALLPwLNVLDNVAFGLRLRGVpKAERR--ARAEELLALVGLADFARRRIWQ----LSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQA 233
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEA 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
29-234 |
2.73e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.67 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmNDLVDICRIEGEILLHGQNIYDksvdVAALR 108
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLTA----LPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKldEVVEQSLRGAALwDEVKDRlhDSAfGLSGGQQQRLVIARSIA 187
Cdd:COG4136 76 RRIGILFQDDLLFPHlSVGENLAFALPPTIGRAQRR--ARVEQALEEAGL-AGFADR--DPA-TLSGGQRARVALLRALL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494860364 188 IEPEVLLLDEPTSALDP-----ISTLVIEELINDlknQFTVVIVTHNMQQAA 234
Cdd:COG4136 150 AEPRALLLDEPFSKLDAalraqFREFVFEQIRQR---GIPALLVTHDEEDAP 198
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-249 |
2.83e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.30 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvDICRI-EGEILLHGQNIydksvdVAA 106
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL------GILAPdSGEVLWDGEPL------DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVG-MvfqrpnP-----FPK-SIYENVVYGLRLQGIKE---KRKLDEVVEQsLrgaalwdEVKDRLHDSAFGLSGGQ 176
Cdd:COG4152 69 DRRRIGyL------PeerglYPKmKVGEQLVYLARLKGLSKaeaKRRADEWLER-L-------GLGDRANKKVEELSKGN 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIV-THNMQQAARVSDQTAFMYMGELI 249
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
37-250 |
6.40e-35 |
|
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: 125.42 E-value: 6.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydKSVDVAALRRNVGMVFQ 116
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGIDI--RDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPKSIYENVVYGlrlqgikEKRKLDEVVEQSLRGAALWDEVKDR-------LHDSAFGLSGGQQQRLVIARSIAIE 189
Cdd:cd03254 85 DTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 190 PEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMqQAARVSDQTAFMYMGELIE 250
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIE 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-261 |
1.30e-34 |
|
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: 130.57 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD----KQALNKVNMNIPKGQVTAFIGPSGCGKS----TLLRcinrmndLV--DICRIEGEILLHGQNIY 98
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-------LLpdPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSVdvAALRR----NVGMVFQRP----NPFpKSIYENVVYGLRL-QGIKEKRKLDEVVEqslrgaaLWDEV-----KDR 164
Cdd:COG4172 80 GLSE--RELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLhRGLSGAAARARALE-------LLERVgipdpERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 165 LHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpistlV-----IEELINDLKNQF--TVVIVTHNMQQAARVS 237
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD-----VtvqaqILDLLKDLQRELgmALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|....
gi 494860364 238 DQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
38-249 |
1.97e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.45 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 38 YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYdksvDVAALRRNVGMVFQR 117
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGDLFIGEKRMN----DVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 PNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQS---LRGAALWD-EVKDrlhdsafgLSGGQQQRLVIARSIAIEPEV 192
Cdd:PRK11000 84 YALYPHlSVAENMSFGLKLAGAK-KEEINQRVNQVaevLQLAHLLDrKPKA--------LSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 193 LLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHnmqqaarvsDQTAFMYMGELI 249
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTH---------DQVEAMTLADKI 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
29-249 |
8.97e-34 |
|
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: 121.92 E-value: 8.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGqVTAFIGPSGCGKSTLLRCInrmndlvdiCRI----EGEILLHGQniyDKSVDV 104
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRIL---------ATLtppsSGTIRIDGQ---DVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALWDEVKDRLHdsafGLSGGQQQRLVIA 183
Cdd:cd03264 68 QKLRRRIGYLPQEFGVYPNfTVREFLDYIAWLKGI-PSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
47-243 |
9.76e-34 |
|
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: 125.60 E-value: 9.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 47 VNMNIPKGQVTAFIGPSGCGKSTLLRCI---NRMNdlvdicriEGEILLHGQNIYD--KSVDVAALRRNVGMVFQRPNPF 121
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglERPD--------SGRIRLGGEVLQDsaRGIFLPPHRRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 P-KSIYENVVYGLRLQGIKEKR-KLDEVVEqsLRG-AALwdevkdrLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEP 198
Cdd:COG4148 90 PhLSVRGNLLYGRKRAPRAERRiSFDEVVE--LLGiGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494860364 199 TSALDPISTLVIEELINDLKNQFT--VVIVTHNMQQAARVSDQTAFM 243
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDipILYVSHSLDEVARLADHVVLL 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
29-238 |
1.71e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.48 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEiLLHGqniydkSVDVAALR 108
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA-----GE-LLAG------TAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFP-KSIYENVvyGLRLQGikekrKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNV--GLGLKG-----QWRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSD 238
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAVAMAD 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-257 |
9.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvDICR-IEGEILLHGQNI-YDKSvDVA 105
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFN------GILKpTSGEVLIKGEPIkYDKK-SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEkrklDEV---VEQSLRGAALWDEVKDRLHDsafgLSGGQQQRL 180
Cdd:PRK13639 75 EVRKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGLSK----EEVekrVKEALKAVGMEGFENKPPHH----LSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIE-------YS 252
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkevFS 226
|
....*
gi 494860364 253 DTNTL 257
Cdd:PRK13639 227 DIETI 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-250 |
1.09e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSV-DVa 105
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL-----LLPEAGTITVGGMVLSEETVwDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 alRRNVGMVFQRP-NPFPKSIYEN-VVYGLRLQGIkEKRKLDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:PRK13635 80 --RRQVGMVFQNPdNQFVGATVQDdVAFGLENIGV-PREEMVERVDQALRQVGM----EDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARvSDQTAFMYMGELIE 250
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
31-243 |
1.34e-32 |
|
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: 118.49 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 31 IKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrMNDLVDicriEGEILLHGQNIYD-KSVDVAALRR 109
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIG-LLEKFD----SGQVYLNGQETPPlNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 N-VGMVFQRPNPFP-KSIYENVVYGLRLQGI--KEKRKLDEVVEQSLRgaalwdeVKDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:TIGR03608 76 EkLGYLFQNFALIEnETVEENLDLGLKYKKLskKEKREKKKEALEKVG-------LNLKLKQKIYELSGGEQQRVALARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARvSDQTAFM 243
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
29-249 |
2.01e-32 |
|
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: 118.62 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGqniYDKSVDV 104
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL-----LEPDAGFATVDG---FDVVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKE---KRKLDEVVEQSlrgaalwdEVKDRLHDSAFGLSGGQQQRL 180
Cdd:cd03266 74 AEARRRLGFVSDSTGLYDRlTARENLEYFAGLYGLKGdelTARLEELADRL--------GMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIV-THNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-249 |
2.14e-32 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 118.36 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDkQALNkVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGqniydksVDVAAL- 107
Cdd:cd03298 1 VRLDKIRFSYGE-QPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQ----SGRVLING-------VDVTAAp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 --RRNVGMVFQRPNPFPK-SIYENVvyGLrlqGIKEKRKLDEVVEQSLRGAAL---WDEVKDRLHDSafgLSGGQQQRLV 181
Cdd:cd03298 67 paDRPVSMLFQENNLFAHlTVEQNV--GL---GLSPGLKLTAEDRQAIEVALArvgLAGLEKRLPGE---LSGGERQRVA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03298 139 LARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-228 |
2.22e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 125.45 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDK--QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICRIE-GEILLHGQNIydKSVDV 104
Cdd:TIGR03797 451 AIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRL------LLGFETPEsGSVFYDGQDL--AGLDV 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPKSIYENVVYGLRLQgikekrkLDEVVEqSLRGAALWDEVKDR---LH----DSAFGLSGGQQ 177
Cdd:TIGR03797 523 QAVRRQLGVVLQNGRLMSGSIFENIAGGAPLT-------LDEAWE-AARMAGLAEDIRAMpmgMHtvisEGGGTLSGGQR 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494860364 178 QRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKnqFTVVIVTH 228
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAH 643
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
29-270 |
2.69e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.25 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydksVDVAALR 108
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ-----PTAGQIMLDGVDL----SHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRlQGIKEKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIA 187
Cdd:PRK11607 91 RPINMMFQSYALFPHmTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALD-PISTLVIEELINDLKN-QFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKK 265
Cdd:PRK11607 166 KRPKLLLLDEPMGALDkKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
....*
gi 494860364 266 TEDYI 270
Cdd:PRK11607 246 SAEFI 250
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-261 |
4.51e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.55 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYG-----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDK-- 100
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL-----LKPSSGTITIAGYHITPEtg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVAALRRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEVKDRlhdSAFGLSGGQQQ 178
Cdd:PRK13641 77 NKNLKKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDLISK---SPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
....
gi 494860364 258 FTTP 261
Cdd:PRK13641 233 FSDK 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-262 |
5.56e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.96 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 15 QKLDLENLTDDQKALEIKDLDLYYGDKQ-----ALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcINRMNDLV-------- 81
Cdd:PRK13631 8 KKLKVPNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTL---VTHFNGLIkskygtiq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 82 --DIcRIEGEILLHGQNIYD---KSVDVAALRRNVGMVFQRP--NPFPKSIYENVVYGLRLQGIKeKRKLDEVVEQSLRG 154
Cdd:PRK13631 85 vgDI-YIGDKKNNHELITNPyskKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 155 AALWDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLK-NQFTVVIVTHNMQQA 233
Cdd:PRK13631 163 MGLDDSYLER---SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|....*....
gi 494860364 234 ARVSDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-249 |
1.30e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLHGQNIYDKSVDVAAL 107
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-----ELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRnvGMVFQRPN-PFPKSIYENVVYGlRLQGIKEKRKLDEVVEQSLRGAALWDeVKDRLHDSafgLSGGQQQRLVIARSI 186
Cdd:PRK13548 77 RR--AVLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAH-LAGRDYPQ---LSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 187 A------IEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-249 |
1.44e-31 |
|
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: 114.45 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDvAALR 108
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL-----YKPDSGEILVDGKEVSFASPR-DARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQrpnpfpksiyenvvyglrlqgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSIAI 188
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-249 |
1.68e-31 |
|
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: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLHGQNIYDKSVDVAALR 108
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG-----ELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVgMVFQRPNPFPKSIYENVVYGlRLQGIKEKRKLDEVVEQSLRGAALWDeVKDRLHDSafgLSGGQQQRLVIARSIA- 187
Cdd:COG4559 77 RAV-LPQHSSLAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQT---LSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 188 ------IEPEVLLLDEPTSALDP---ISTLvieELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLahqHAVL---RLARQLARRgGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
29-238 |
1.88e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.56 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLHGQNIYDKS-VDVAAL 107
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG-----QIAPDHGEILFDGENIPAMSrSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRlqgikEKRKLDEVVEQS----------LRGAAlwdevkdRLHDSAfgLSGGQ 176
Cdd:PRK11831 83 RKRMSMLFQSGALFTDmNVFDNVAYPLR-----EHTQLPAPLLHStvmmkleavgLRGAA-------KLMPSE--LSGGM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSD 238
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIAD 212
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-260 |
2.90e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.12 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLYY---GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRM-NDLVDICRIEGEiLLHGQNIYDksv 102
Cdd:PRK13642 3 KILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGE-LLTAENVWN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 dvaaLRRNVGMVFQRP-NPF-PKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALwdEVKDRlhdSAFGLSGGQQQRL 180
Cdd:PRK13642 79 ----LRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTR---EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTLF 258
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
..
gi 494860364 259 TT 260
Cdd:PRK13642 229 AT 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-261 |
3.19e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.21 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLD-LYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKsvDVAAL 107
Cdd:PRK13652 4 IETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI-----LKPTSGSVLIRGEPITKE--NIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALwDEVKDRLhdsAFGLSGGQQQRLVIARS 185
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGLDEE-TVAHRVSSALHMLGL-EELRDRV---PHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
29-228 |
4.01e-31 |
|
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: 114.88 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRI----EGEILLHGQNIYDksvDV 104
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---------AGLlppsAGEVLWNGEPIRD---AR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRkldEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:COG4133 71 EDYRRRLAYLGHADGLKPElTVRENLRFWAALYGLRADR---EAIDEALEAVGL----AGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLVIEELIND-LKNQFTVVIVTH 228
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
43-249 |
4.23e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 116.77 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNdlvdiCRIEGEILLHGQNIYDKSV--DVAALRRNVGMVFQRPNP 120
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLITSTSKnkDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 --FPKSIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALWDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLDEP 198
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFGV-SQEEAEALAREKLALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494860364 199 TSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-251 |
4.29e-31 |
|
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: 114.69 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGqniydKSVDVAAlR 108
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI-----ILPDSGEVLFDG-----KPLDIAA-R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIA 187
Cdd:cd03269 70 NRIGYLPEERGLYPKmKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
26-250 |
5.49e-31 |
|
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: 115.22 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQA----LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQNIYDKS 101
Cdd:COG4181 6 APIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPT----SGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 VD-VAALR-RNVGMVFQR----PNpfpKSIYENVVYGLRLQGIKEKRKldevveqslRGAALWDEV--KDRLHDSAFGLS 173
Cdd:COG4181 81 EDaRARLRaRHVGFVFQSfqllPT---LTALENVMLPLELAGRRDARA---------RARALLERVglGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELIE 250
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
39-259 |
1.33e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 114.90 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGQNIYD-KSVDVAALRRNVGMVFQ 116
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARL------LLGLEKpAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RP----NPfPKSIYENVVYGLR-LQGIKEKRKLDEVVEQsLRGAALWDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPE 191
Cdd:TIGR02769 96 DSpsavNP-RMTVRQIIGEPLRhLTSLDESEQKARIAEL-LDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 192 VLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:TIGR02769 171 LIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
42-248 |
3.70e-30 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 112.50 E-value: 3.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrMNDLVDicriEGEILLHGQNI----YDKSVdvaALRRN-VGMVFQ 116
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVtnlsYSQKI---ILRRElIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPK-SIYENVVYGLRLQGIKEKRKLdEVVEQSLrgaALWDeVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:NF038007 91 SFNLIPHlSIFDNVALPLKYRGVAKKERI-ERVNQVL---NLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494860364 196 DEPTSALDPIST-LVIEELINDLKNQFTVVIVTHNmQQAARVSDQTAFMYMGEL 248
Cdd:NF038007 166 DEPTGNLDSKNArAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-257 |
4.09e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.58 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 17 LDLENLTDDQK--------ALEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicri 86
Cdd:PRK11176 322 LDLEQEKDEGKrvierakgDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD-ID---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 87 EGEILLHGQNIYDKSVdvAALRRNVGMVFQRPNPFPKSIYENVVYGlrlqgiKEKRKLDEVVEQSLRGAALWDEVKDRLH 166
Cdd:PRK11176 397 EGEILLDGHDLRDYTL--ASLRNQVALVSQNVHLFNDTIANNIAYA------RTEQYSREQIEEAARMAYAMDFINKMDN 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 167 --DSAFG-----LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQ 239
Cdd:PRK11176 469 glDTVIGengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADE 547
|
250
....*....|....*...
gi 494860364 240 TAFMYMGELIEYSDTNTL 257
Cdd:PRK11176 548 ILVVEDGEIVERGTHAEL 565
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-258 |
8.67e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.92 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-GDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDKsvDVAA 106
Cdd:PRK13648 8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-----SGEIFYNNQAITDD--NFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRP-NPFPKSIYE-NVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEVKDRLHdsafGLSGGQQQRLVIAR 184
Cdd:PRK13648 81 LRKHIGIVFQNPdNQFVGSIVKyDVAFGLENHAVPYD-EMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLK--NQFTVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTLF 258
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
42-243 |
9.88e-30 |
|
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: 111.76 E-value: 9.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmNDLVDicriEGEILLHGQniyDKSVDVA--------ALRRN-VG 112
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPD----SGSILVRHD---GGWVDLAqaspreilALRRRtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 113 MVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDevveqslRGAALWD--EVKDRLHDSA---FglSGGQQQRLVIARSI 186
Cdd:COG4778 97 YVSQFLRVIPRvSALDVVAEPLLERGVDREEARA-------RARELLArlNLPERLWDLPpatF--SGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVI-VTHNMQQAARVSDQTAFM 243
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVADRVVDV 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-257 |
1.50e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.85 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 2 ITVAPKVNQAnIGQKLDL-----ENLTDDQKALEIKDLDLYYGDKQ--ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI 74
Cdd:PRK11160 308 IASARRINEI-TEQKPEVtfpttSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 75 NRMNDLvdicrIEGEILLHGQNIydKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGL------RLQGIKEKRKLDEVV 148
Cdd:PRK11160 387 TRAWDP-----QQGEILLNGQPI--ADYSEAALRQAISVVSQRVHLFSATLRDNLLLAApnasdeALIEVLQQVGLEKLL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 149 EQSlRGAALWdevkdrLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:PRK11160 460 EDD-KGLNAW------LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260
....*....|....*....|....*....
gi 494860364 229 NMQQAARVsDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK11160 533 RLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
46-248 |
2.22e-29 |
|
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: 113.67 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 46 KVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYD--KSVDVAALRRNVGMVFQRPNPFPK 123
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGRTLFDsrKGIFLPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 124 -SIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDRLhdsafglSGGQQQRLVIARSIAIEPEVLLLDEPTSAL 202
Cdd:TIGR02142 90 lSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRL-------SGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494860364 203 DPISTlviEELINDLKN-----QFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:TIGR02142 163 DDPRK---YEILPYLERlhaefGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
35-254 |
3.86e-29 |
|
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: 109.95 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 35 DLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIydksVDVAALRRNVGMV 114
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-----IEPASGSIKVNDQSH----TGLAPYQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 FQRPNPFPK-SIYENVVYGLRlQGIKEKRKLDEVVEQSLRGAALwDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVL 193
Cdd:TIGR01277 76 FQENNLFAHlTVRQNIGLGLH-PGLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQ---LSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 194 LLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDT 254
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-236 |
4.66e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 108.46 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQA--LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGQNIydKSVDVAA 106
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-----LGLLRPTSGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVvyglrlqgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSI 186
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNM---QQAARV 236
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-261 |
6.48e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.98 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----------QALNKVNMNIPKGQVTAFIGPSGCGKSTLlrciNRMNDLVDiCRIEGEILLHGQNI- 97
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTMIE-TPTGGELYYQGQDLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 -YDKSvDVAALRRNVGMVFQRP----NPFPK--SIYEN-VVYGLRLqGIKEKRkldEVVEQSLRGAALWDEVKDRL-Hds 168
Cdd:PRK11308 81 kADPE-AQKLLRQKIQIVFQNPygslNPRKKvgQILEEpLLINTSL-SAAERR---EKALAMMAKVGLRPEHYDRYpH-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 169 AFglSGGQQQRLVIARSIAIEPEVLLLDEPTSALD-PISTLVIeELINDLKNQFTV--VIVTHNMQQAARVSDQTAFMYM 245
Cdd:PRK11308 154 MF--SGGQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQVL-NLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYL 230
|
250
....*....|....*.
gi 494860364 246 GELIEYSDTNTLFTTP 261
Cdd:PRK11308 231 GRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
28-262 |
1.05e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndLVDICRIEGEILLHGQNIYDKSV-DV 104
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKTVwDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 aalRRNVGMVFQRP-NPF-PKSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVI 182
Cdd:PRK13640 83 ---REKVGIVFQNPdNQFvGATVGDDVAFGLENRAVP-RPEMIKIVRDVLADVGMLDYIDSEPAN----LSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAArVSDQTAFMYMGELIEYSDTNTLFTT 260
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSK 233
|
..
gi 494860364 261 PT 262
Cdd:PRK13640 234 VE 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-250 |
1.46e-28 |
|
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: 108.00 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI-NRMNDLVdicrIEGEILLHGQNIYDKSVDVAAl 107
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKYEV----TEGEILFKGEDITDLPPEERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPnpfpksiyenvvygLRLQGIKekrkldevveqslrgaalwdeVKDRLHDSAFGLSGGQQQRLVIARSIA 187
Cdd:cd03217 76 RLGIFLAFQYP--------------PEIPGVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARV-SDQTAFMYMGELIE 250
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEgKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
40-248 |
1.88e-28 |
|
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: 108.33 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDksVDVAALRRNVGMVFQRPN 119
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG-----GQVLLDGKPISQ--YEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPKSIYENVVYGLrlqgikEKRKLDEVVEQSLRGAA----------LWDEVKDRlhdsAFGLSGGQQQRLVIARSIAIE 189
Cdd:cd03248 99 LFARSLQDNIAYGL------QSCSFECVKEAAQKAHAhsfiselasgYDTEVGEK----GSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 190 PEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGEL 248
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-250 |
2.05e-28 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 113.66 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG--DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICriEGEILLHGQNIYDKSVdvAA 106
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPR---FYEPD--SGQILLDGHDLADYTL--AS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVVYGlRLQGIKEKRkldevVEQSLRGAALWDEVkDRLH---DSAFG-----LSGGQQQ 178
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYG-RTEQADRAE-----IERALAAAYAQDFV-DKLPlglDTPIGengvlLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGELIE 250
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-250 |
2.32e-28 |
|
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: 108.34 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGD-KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIydKSVDVAALRRNVGMVF 115
Cdd:cd03252 10 YKPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEN-----GRVLVDGHDL--ALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 116 QRPNPFPKSIYEN------------VVYGLRLQGIKE-KRKLDEVVEQSL--RGAalwdevkdrlhdsafGLSGGQQQRL 180
Cdd:cd03252 83 QENVLFNRSIRDNialadpgmsmerVIEAAKLAGAHDfISELPEGYDTIVgeQGA---------------GLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMqQAARVSDQTAFMYMGELIE 250
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVE 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
29-250 |
2.36e-28 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 108.52 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTllrCINRMNDLVDicRIEGEILLHGQNIYDKSVDVAAlR 108
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHLPMHERA-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGikekrKLDEVvEQSLRGAALWDE--VKDRLHDSAFGLSGGQQQRLVIARS 185
Cdd:TIGR04406 76 LGIGYLPQEASIFRKlTVEENIMAVLEIRK-----DLDRA-EREERLEALLEEfqISHLRDNKAMSLSGGERRRVEIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:TIGR04406 150 LATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERgIGVLITDHNVRETLDICDRAYIISDGKVLA 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
42-258 |
2.38e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.82 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNiydKSVDVAALRRNVGMVFQRPNP- 120
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS---KQKEIKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 -FPKSIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALWDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPT 199
Cdd:PRK13643 97 lFEETVLKDVAFGPQNFGI-PKEKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 200 SALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLF 258
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-229 |
2.60e-28 |
|
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: 113.22 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYdkSVDVAAL 107
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVS--SLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPKSIYENvvygLRLqGIKEKRklDEVVEQSLRGAALWDEVKDR-------LHDSAFGLSGGQQQRL 180
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVREN----LRL-ARPDAT--DEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHN 229
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-250 |
3.13e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 113.13 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydKSVDVAALRRNVGMVFQ 116
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD-----PQSGRILIDGTDI--RTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPKSIYENVVYGlrlqgiKEKRKLDEVVEQSLRGAAL-WDEVKDRLHDSAFG-----LSGGQQQRLVIARSIAIEP 190
Cdd:PRK13657 417 DAGLFNRSIEDNIRVG------RPDATDEEMRAAAERAQAHdFIERKPDGYDTVVGergrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 191 EVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMqQAARVSDQTAFMYMGELIE 250
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
40-269 |
4.91e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.71 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVD--VAALRRNVGMVFQr 117
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL-----LKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 pnpFPKS-IYENVVYGLRLQGIKE-KRKLDEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PRK13646 93 ---FPESqLFEDTVEREIIFGPKNfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 196 DEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTtpTKKKTEDY 269
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADW 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-230 |
5.21e-28 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 106.91 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQ--ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydKSVDVA 105
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK-----PTSGSVLLDGTDI--RQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRPNPFPKSIYENVVYGL------RLQGIKEKRKLDEVVEQSLRGAALwdEVKDRlhdsAFGLSGGQQQR 179
Cdd:cd03245 75 DLRRNIGYVPQDVTLFYGTLRDNITLGApladdeRILRAAELAGVTDFVNKHPNGLDL--QIGER----GRGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPIS-TLVIEELINDLKNQfTVVIVTHNM 230
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSeERLKERLRQLLGDK-TLIIITHRP 199
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-249 |
5.56e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG-----DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmNDLVDicriEGEILLHGQNIYDKSVD 103
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG-SLPPD----SGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAAlrRNVGMVFQrpNPF----PK-SIYENVV--------YGLRLqGIKEKRKlDEVVEQsLRGAALWDEvkDRLHDSAF 170
Cdd:COG1101 77 KRA--KYIGRVFQ--DPMmgtaPSmTIEENLAlayrrgkrRGLRR-GLTKKRR-ELFREL-LATLGLGLE--NRLDTKVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 171 GLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
.
gi 494860364 249 I 249
Cdd:COG1101 228 I 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-249 |
5.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 22 LTDDQKALEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGQNIY 98
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKI------LTGLLKpQSGEIKIDGITIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSVDvaALRRNVGMVFQRP-NPFPKSIYE-NVVYGL---RLQGIKEKRKLDEVVEQSlrgaalwdEVKDRLHDSAFGLS 173
Cdd:PRK13632 75 KENLK--EIRKKIGIIFQNPdNQFIGATVEdDIAFGLenkKVPPKKMKDIIDDLAKKV--------GMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELI 249
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAIL-ADKVIVFSEGKLI 221
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
26-231 |
6.47e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 112.65 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDL-YYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIydKSVD 103
Cdd:TIGR03375 461 QGEIEFRNVSFaYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQP-----TEGSVLLDGVDI--RQID 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGikekrklDEVVEQSLRGAALWDEVkdRLHDSAF---------GLSG 174
Cdd:TIGR03375 534 PADLRRNIGYVPQDPRLFYGTLRDNIALGAPYAD-------DEEILRAAELAGVTEFV--RRHPDGLdmqigergrSLSG 604
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPIS-TLVIEELINDLKNQfTVVIVTHNMQ 231
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMDNRSeERFKDRLKRWLAGK-TLVLVTHRTS 661
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
30-239 |
1.25e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.71 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYD-KSVD----V 104
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLDVATtPSRElakrL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMV----------FQRpnpFPKSiyenvvyGLRLQgiKEKRkldEVVEQSLRGAALwDEVKDRLHDSafgLSG 174
Cdd:COG4604 78 AILRQENHINsrltvrelvaFGR---FPYS-------KGRLT--AEDR---EIIDEAIAYLDL-EDLADRYLDE---LSG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQ 239
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADH 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
29-266 |
1.30e-27 |
|
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: 106.09 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRI-EGEILLHGQNIYDKSVDVAAl 107
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI------VGLVKPdSGKILLDGQDITKLPMHKRA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRKLDEVVEqslrgaaLWDEVK-DRLHDS-AFGLSGGQQQRLVIAR 184
Cdd:cd03218 74 RLGIGYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEE-------LLEEFHiTHLRKSkASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTK 263
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
...
gi 494860364 264 KKT 266
Cdd:cd03218 227 RKV 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-257 |
1.74e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.09 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 20 ENLTDDQKALEI--KDLDLY-YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLrcinrmNDLVDICRIEGEILLHGQN 96
Cdd:PRK11174 339 EKELASNDPVTIeaEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 97 IydKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYG------LRLQGIKEKRKLDEVVEQSLRGaaLWDEVKDRlhdsAF 170
Cdd:PRK11174 413 L--RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGnpdasdEQLQQALENAWVSEFLPLLPQG--LDTPIGDQ----AA 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 171 GLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIE 250
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
....*..
gi 494860364 251 YSDTNTL 257
Cdd:PRK11174 564 QGDYAEL 570
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-238 |
1.93e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCIN---RMNdlvdicriEGEILLHGQNIYDKSVdV 104
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyQPD--------SGEILLDGEPVRFRSP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYG--LRLQGIKEKRKLDEVVEQSLR--GAAL--WDEVKDrlhdsafgLSGGQQ 177
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPNlSVAENIFLGrePRRGGLIDWRAMRRRARELLArlGLDIdpDTPVGD--------LSVAQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 178 QRLVIARSIAIEPEVLLLDEPTSALDP--ISTLVieELINDLKNQ-FTVVIVTHNMQQAARVSD 238
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEreVERLF--RIIRRLKAQgVAIIYISHRLDEVFEIAD 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
29-262 |
2.86e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.50 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDICRIEGEILLHGQNIYD-KSVD 103
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNlPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALR-RNVGMVFQRP----NPFPKsIYENVVYGLRL-QGIKEKrkldEVVEQSLR--GAALWDEVKDRLHDSAFGLSGG 175
Cdd:PRK09473 91 LNKLRaEQISMIFQDPmtslNPYMR-VGEQLMEVLMLhKGMSKA----EAFEESVRmlDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGELIEYSD 253
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
....*....
gi 494860364 254 TNTLFTTPT 262
Cdd:PRK09473 246 ARDVFYQPS 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-249 |
3.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.33 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 25 DQKALEIKDLDLYYGD------KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinRMNDLVdiCRIEGEILLHGQNIY 98
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAK---HMNALL--IPSEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSvDVAALRRNVGMVFQRP-NPFPKSIYE-NVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEVKDRLHdsafGLSGGQ 176
Cdd:PRK13633 76 DEE-NLWDIRNKAGMVFQNPdNQIVATIVEeDVAFGPENLGIPPE-EIRERVDESLKKVGMYEYRRHAPH----LLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQTAFMYMGELI 249
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-258 |
3.36e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQ---ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKsvDVA 105
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL-----LEAESGQIIIDGDLLTEE--NVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMVFQRP-NPFPKSIYEN-VVYGLRLQGIKEKrKLDEVVEQSLRGAALWDeVKDRlhdSAFGLSGGQQQRLVIA 183
Cdd:PRK13650 78 DIRHKIGMVFQNPdNQFVGATVEDdVAFGLENKGIPHE-EMKERVNEALELVGMQD-FKER---EPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPISTLvieELINDLK-----NQFTVVIVTHNMQQAArVSDQTAFMYMGELIEYSDTNTLF 258
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRL---ELIKTIKgirddYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-249 |
3.62e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.84 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 22 LTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYD-K 100
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL-----MTPAHGHVWLDGEHIQHyA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVAalrRNVGMVFQRP-NPFPKSIYENVVYGLRLQG--IKEKRKLDE-VVEQSLRGAAlwdeVKDRLHDSAFGLSGGQ 176
Cdd:PRK10253 76 SKEVA---RRIGLLAQNAtTPGDITVQELVARGRYPHQplFTRWRKEDEeAVTKAMQATG----ITHLADQSVDTLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK10253 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-250 |
4.66e-27 |
|
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: 103.16 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYG--DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLHGQNIydkSVDVAA 106
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG-----DLKPQQGEITLDGVPV---SDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVvyGLRlqgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSI 186
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIE 250
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
48-272 |
6.78e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.81 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 48 NMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKS-VDVAALRRN-VGMVFQRPNPFPK-S 124
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRL-----IEPTRGQVLIDGVDIAKISdAELREVRRKkIAMVFQSFALMPHmT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 125 IYENVVYGLRLQGIKEKRKLDEVVEqSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDP 204
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALD-ALRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 205 -ISTLVIEELIN-DLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDYITG 272
Cdd:PRK10070 198 lIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
28-228 |
1.41e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.01 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMN-----DLVDICrieGEILlhGQniydksV 102
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygNDVRLF---GERR--GG------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNVGMV---FQRPNPFPKSIYENVVYGL-----RLQGI--KEKRKLDEVVEQsLRGAALwdevKDRLhdsaFG- 171
Cdd:COG1119 72 DVWELRKRIGLVspaLQLRFPRDETVLDVVLSGFfdsigLYREPtdEQRERARELLEL-LGLAHL----ADRP----FGt 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTH 228
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
44-250 |
1.63e-26 |
|
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: 103.31 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDvaalrRNVgmVFQRPNPFP- 122
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTS-----GGVILEGKQITEPGPD-----RMV--VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 123 KSIYENV---VYGLRLQGIKEKRKldEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEVLLLDEPT 199
Cdd:TIGR01184 69 LTVRENIalaVDRVLPDLSKSERR--AIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 200 SALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFM------YMGELIE 250
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
29-254 |
1.95e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.78 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK-----QALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcINRMNDLVDICRIEGEILLHGQNIYDKSVD 103
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTF---IEHLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 --------------------VAALRRNVGMVFQ--RPNPFPKSIYENVVYGLRLQGIKEKrkldEVVEQSLRGAALWDEV 161
Cdd:PRK13651 80 kekvleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 162 KDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQT 240
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|....
gi 494860364 241 AFMYMGELIEYSDT 254
Cdd:PRK13651 236 IFFKDGKIIKDGDT 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-261 |
2.34e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 103.63 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 15 QKLDLENLTDDQKALEIKDLDLyygdkqalnkvnmNIPKGQVTAFIGPSGCGKStlLRCINRMNDL-VDICRIEGEILLH 93
Cdd:PRK10418 3 QQIELRNIALQAAQPLVHGVSL-------------TLQRGRVLALVGGSGSGKS--LTCAAALGILpAGVRQTAGRVLLD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 94 GQniydkSVDVAALR-RNVGMVFQRP----NPFpKSIYENVVYGLRLQGikeKRKLDEVVEQSLRGAALwDEVKDRLHDS 168
Cdd:PRK10418 68 GK-----PVAPCALRgRKIATIMQNPrsafNPL-HTMHTHARETCLALG---KPADDATLTAALEAVGL-ENAARVLKLY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 169 AFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMG 246
Cdd:PRK10418 138 PFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLADDVAVMSHG 217
|
250
....*....|....*
gi 494860364 247 ELIEYSDTNTLFTTP 261
Cdd:PRK10418 218 RIVEQGDVETLFNAP 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
38-235 |
2.43e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 38 YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICR-IEGeillhgqniydkSVDVAALRRnVGMVFQ 116
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL------AGVLRpTSG------------TVRRAGGAR-VAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 R---PNPFPKSIYENVVYGL--RLQGIKEKRKLDE-VVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEP 190
Cdd:NF040873 63 RsevPDSLPLTVRDLVAMGRwaRRGLWRRLTRDDRaAVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 494860364 191 EVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAAR 235
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRR 184
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-249 |
2.44e-26 |
|
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: 101.86 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 14 GQKLDLENLTddqKALEIKDLDlyyGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCIN--RMNdlvdiCRIEGEIL 91
Cdd:cd03213 1 GVTLSFRNLT---VTVKSSPSK---SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTG-----LGVSGEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 92 LHGQNIYDKSvdvaaLRRNVGMVFQrpnpfpksiyENVVYGlrlqgikekrklDEVVEQSLRGAAlwdEVKdrlhdsafG 171
Cdd:cd03213 70 INGRPLDKRS-----FRKIIGYVPQ----------DDILHP------------TLTVRETLMFAA---KLR--------G 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHN-MQQAARVSDQTAFMYMGELI 249
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-250 |
2.56e-26 |
|
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: 107.90 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 14 GQKLDLENLTDDqkaLEIKDLDLYYG-DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICRIE-GEIL 91
Cdd:TIGR01193 462 KKRTELNNLNGD---IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKL------LVGFFQARsGEIL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 92 LHGQNIYDksVDVAALRRNVGMVFQRPNPFPKSIYENVvyglrLQGIKEKRKLDEVVeQSLRGAALWDEVKD-------R 164
Cdd:TIGR01193 533 LNGFSLKD--IDRHTLRQFINYLPQEPYIFSGSILENL-----LLGAKENVSQDEIW-AACEIAEIKDDIENmplgyqtE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 165 LHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPIST-LVIEELINdLKNQfTVVIVTHNMQQAARvSDQTAFM 243
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEkKIVNNLLN-LQDK-TIIFVAHRLSVAKQ-SDKIIVL 681
|
....*..
gi 494860364 244 YMGELIE 250
Cdd:TIGR01193 682 DHGKIIE 688
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
37-250 |
3.78e-26 |
|
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: 107.21 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlVDicriEGEILLHGQNIYDksVDVAALRRNVGMVFQ 116
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD-VT----SGRILIDGQDIRD--VTQASLRAAIGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPKSIYENVVYGlRLQGIkekrklDEVVEQSLRGAALWDEVkDRL---HDSAFG-----LSGGQQQRLVIARSIAI 188
Cdd:COG5265 440 DTVLFNDTIAYNIAYG-RPDAS------EEEVEAAARAAQIHDFI-ESLpdgYDTRVGerglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 189 EPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIvthnmqqAARVS-----DQTAFMYMGELIE 250
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVaRGRTTLVI-------AHRLStivdaDEILVLEAGRIVE 572
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-250 |
4.33e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.23 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGQNI--YDKSvDVAALRRNVGMVFQR 117
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARL------LVGLESpSQGNVSWRGEPLakLNRA-QRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 P----NPfPKSIYENVVYGLR-LQGIKEKRKLDEVVEQsLRGAALWDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEV 192
Cdd:PRK10419 98 SisavNP-RKTVREIIREPLRhLLSLDKAERLARASEM-LRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 193 LLLDEPTSALDPISTLVIEELINDLKNQFTV--VIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-243 |
7.89e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.62 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQ-----ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGqniydksvd 103
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----LGELEKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 vaalrrNVGMVFQRPNPFPKSIYENVVYGLRLqgikEKRKLDEVVeqslRGAALwdeVKD----------RLHDSAFGLS 173
Cdd:cd03250 67 ------SIAYVSQEPWIQNGTIRENILFGKPF----DEERYEKVI----KACAL---EPDleilpdgdltEIGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDP-ISTLVIEELIN-DLKNQFTVVIVTHNMQQAARVsDQTAFM 243
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQLLPHA-DQIVVL 200
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
42-259 |
1.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.39 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNI---YDKSVDVAALRRNVGMVFQRP 118
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL-----IISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 --NPFPKSIYENVVYGLRLQGiKEKRKLDEVVEQSLRGAALWDEVKDRlhdSAFGLSGGQQQRLVIARSIAIEPEVLLLD 196
Cdd:PRK13645 100 eyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 197 EPTSALDPISTlviEELINDL----KNQFT-VVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:PRK13645 176 EPTGGLDPKGE---EDFINLFerlnKEYKKrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-239 |
1.77e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKsvdVAAL 107
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM-----TSPDAGKITVLGVPVPAR---ARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYEN-VVYGlRLQGIKeKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARS 185
Cdd:PRK13536 113 RARIGVVPQFDNLDLEfTVRENlLVFG-RYFGMS-TREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 186 IAIEPEVLLLDEPTSALDPIST-LVIEELINDLKNQFTVVIVTHNMQQAARVSDQ 239
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARhLIWERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
29-262 |
2.49e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIydKSVDVAALR 108
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT-----LTPTAGTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPN-PFPKSIYENVVYGL-----RLQGIKEKRklDEVVEQSL-RGAAlwDEVKDRLHDSafgLSGGQQQRLV 181
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGRtphrsRFDTWTETD--RAAVERAMeRTGV--AQFADRPVTS---LSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALD---PISTL-VIEELINDLKnqfTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDinhQVRTLeLVRRLVDDGK---TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
....*
gi 494860364 258 FTTPT 262
Cdd:PRK09536 227 LTADT 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-258 |
2.55e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLrcinrMNdLVDICRIE-GEILLHGQNIYDKSVDVAAL 107
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLF-----MN-LSGLLRPQkGAVLWQGKPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNP--FPKSIYENVVYGLRLQGIKEK---RKLDEVVeqslrgaALWDEVKDRlHDSAFGLSGGQQQRLVI 182
Cdd:PRK13638 76 RQQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPEAeitRRVDEAL-------TLVDAQHFR-HQPIQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFT-VVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLF 258
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-235 |
4.62e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.18 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRIE----GEILLHGQNIYD-KSVDVAALRRNV 111
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLI---------CGIErpsaGKIWFSGHDITRlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 112 GMVFQRPNPF-PKSIYENVVYGLRLQGIKEKrKLDEVVEQSLRGAALWDEVKDrlhdSAFGLSGGQQQRLVIARSIAIEP 190
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLIIAGASGD-DIRRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494860364 191 EVLLLDEPTSALDPistlVIEELINDLKNQF-----TVVIVTHNMQQAAR 235
Cdd:PRK10908 157 AVLLADEPTGNLDD----ALSEGILRLFEEFnrvgvTVLMATHDIGLISR 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-251 |
5.48e-25 |
|
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: 99.11 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlVDICriEGEILLHGQNIydKSVDVAA 106
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL---VELS--SGSILIDGVDI--SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENvvygLRLQGIKEkrklDEVVEQSLRGAALWDEVK-------DRLHDSAFGLSGGQQQR 179
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSN----LDPFGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQRQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELIndlKNQF---TVVIVTHnmqqaaRV-----SDQTAFMYMGELIEY 251
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTI---REAFkdcTVLTIAH------RLdtiidSDRILVLDKGRVVEF 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
29-249 |
5.55e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRI-EGEILLHGQNIYDKSVDVAAl 107
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI------VGLVKPdSGRIFLDGEDITHLPMHKRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENvvyglrLQGIKEKRKLDEVvEQSLRGAALWDE-----VKDRLhdsAFGLSGGQQQRLV 181
Cdd:COG1137 77 RLGIGYLPQEASIFRKlTVEDN------ILAVLELRKLSKK-EREERLEELLEEfgithLRKSK---AYSLSGGERRRVE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVT-HNMQQAARVSDQTAFMYMGELI 249
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNVRETLGICDRAYIISEGKVL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-233 |
5.87e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.77 E-value: 5.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSvdvaAL 107
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF-----VPYQHGSITLDGKPVEGPG----AE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RrnvGMVFQRPNPFP-KSIYENVVYGLRLQGIkEKRKLDEVVEQSLRGAALWDEVKDRLhdsaFGLSGGQQQRLVIARSI 186
Cdd:PRK11248 72 R---GVVFQNEGLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYI----WQLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQA 233
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEA 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
29-229 |
8.13e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDvaALR 108
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL-----ISPTSGTLLFEGEDISTLKPE--IYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPKSIYENVV--YGLRLQGIKEKRKLDEVVEQSLRGAALWDEVKDrlhdsafgLSGGQQQRLVIARSI 186
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHN 229
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHD 197
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
40-252 |
8.31e-25 |
|
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: 98.88 E-value: 8.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDIcrIEGEILLHGQniydkSVDVAALRRNVGMVFQRPN 119
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT--TSGQILFNGQ-----PRKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPK-SIYENVVYG--LRLQGIKEKRKLDEVVEQ-SLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:cd03234 92 LLPGlTVRETLTYTaiLRLPRKSSDAIRKKRVEDvLLRDLAL----TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQFTVVIVT-HnmQQAA---RVSDQTAFMYMGELIeYS 252
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTiH--QPRSdlfRLFDRILLLSSGEIV-YS 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
40-262 |
1.21e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.88 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTllrCINRMNDLVDicRIEGEILLHGQNIydKSVDVAALRRNVGMVFQRPN 119
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLYQ--PTGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPKSIYENVVYGLRlqgikekRKLDEVVEQSLRGAALWDEVKDRLH--DSAFG-----LSGGQQQRLVIARSIAIEPEV 192
Cdd:TIGR00958 566 LFSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEFPNgyDTEVGekgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 193 LLLDEPTSALDpistLVIEELINDLKNQ--FTVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:TIGR00958 639 LILDEATSALD----AECEQLLQESRSRasRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
29-249 |
2.17e-24 |
|
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: 97.47 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVdvaalr 108
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI-----LRPTSGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGIKEKRkLDEVveqsLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIA 187
Cdd:TIGR03740 70 HKIGSLIESPPLYENlTARENLKVHTTLLGLPDSR-IDEV----LNIVDLTNTGKKKAKQ----FSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-267 |
2.45e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDICRIEGEILLHGQNIYDksVDV 104
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH--ASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRR----NVGMVFQRP----NPF---PKSIYENVVY--GLRLQGIKEK--RKLDEVveqSLRGAAlwdevkDRLHDSA 169
Cdd:PRK15134 84 QTLRGvrgnKIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRREAARGEilNCLDRV---GIRQAA------KRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 170 FGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGE 247
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260
....*....|....*....|
gi 494860364 248 LIEYSDTNTLFTTPTKKKTE 267
Cdd:PRK15134 235 CVEQNRAATLFSAPTHPYTQ 254
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
29-229 |
3.78e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.45 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDlvDICRI-EGEILLHGQNIYDKSVDVAAl 107
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGH--PKYEVtSGSILLDGEDILELSPDERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPksiyenvvyGLR----LQGIKEKRKLDEVVEQSLRGAAlwDEVKDRLH-DSAF-------GLSGG 175
Cdd:COG0396 76 RAGIFLAFQYPVEIP---------GVSvsnfLRTALNARRGEELSAREFLKLL--KEKMKELGlDEDFldryvneGFSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-VIEELINDLKNQ-FTVVIVTHN 229
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLD-IDALrIVAEGVNKLRSPdRGILIITHY 199
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-248 |
6.70e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRM--NDLVDICRIEgeilLHGQNIYDK--- 100
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIE----LLGRTVQREgrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVAALRRNVGMVFQRPNPFPK-SIYENVVYG-----------LR-LQGIKEKRKLDEVVEQSLRGAAlwdevkdrlHD 167
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRlSVLENVLIGalgstpfwrtcFSwFTREQKQRALQALTRVGMVHFA---------HQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 168 SAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLkNQ---FTVVIVTHNMQQAARVSDQTAFMY 244
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDI-NQndgITVVVTLHQVDYALRYCERIVALR 227
|
....
gi 494860364 245 MGEL 248
Cdd:PRK09984 228 QGHV 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-268 |
6.71e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.26 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 1 MITVAPKVNQANIGQKLDlenltdDQKALEIKDLDLYYG---DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRM 77
Cdd:PTZ00265 361 IINRKPLVENNDDGKKLK------DIKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 78 NDlvdicRIEGEILLH-GQNIydKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLR---------------------- 134
Cdd:PTZ00265 435 YD-----PTEGDIIINdSHNL--KDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYslkdlealsnyynedgndsqen 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 135 ---------------------------LQGIKEKRKLD--EVVEQSLR------GAALWDEVKDRLHDSAFGLSGGQQQR 179
Cdd:PTZ00265 508 knkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKdsEVVDVSKKvlihdfVSALPDKYETLVGSNASKLSGGQKQR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLK---NQFTvVIVTHNMqQAARVSDQTAFMYMGELIEYSDTNT 256
Cdd:PTZ00265 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRIT-IIIAHRL-STIRYANTIFVLSNRERGSTVDVDI 665
|
330
....*....|..
gi 494860364 257 LFTTPTKKKTED 268
Cdd:PTZ00265 666 IGEDPTKDNKEN 677
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-251 |
7.49e-24 |
|
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: 95.56 E-value: 7.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK--QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvdicrIEGEILLHGQNIydKSVDVAA 106
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDI--STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENVvyglrlqgikekRKLDEVVEQSLRGAAlwdevkdRLHDSAFGLSGGQQQRLVIARSI 186
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNL------------DPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIEY 251
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
48-240 |
1.03e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 48 NMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNiydkSVDVAALRRNVGMVFQRPNPFPK-SIY 126
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGF-----LTPASGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFSHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 127 ENVVYG----LRLQGiKEKRKLDEVVEQ-SLrgaalwDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSA 201
Cdd:PRK10771 90 QNIGLGlnpgLKLNA-AQREKLHAIARQmGI------EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 494860364 202 LDP-----ISTLViEELINDlkNQFTVVIVTHNMQQAARVSDQT 240
Cdd:PRK10771 160 LDPalrqeMLTLV-SQVCQE--RQLTLLMVSHSLEDAARIAPRS 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
43-261 |
1.98e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDicRIEGEILLHGQNIYDKSV-DVAALRRNVGMVFQRPNPF 121
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR---LVE--SQGGEIIFNGQRIDTLSPgKLQALRRDIQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 --PK-----SIYENV-VYGLrLQGIKEKRKLDEVVEQ-SLRGAALWDevkdrlHDSAFglSGGQQQRLVIARSIAIEPEV 192
Cdd:PRK10261 414 ldPRqtvgdSIMEPLrVHGL-LPGKAAAARVAWLLERvGLLPEHAWR------YPHEF--SGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 193 LLLDEPTSALDPISTLVIEELINDLKNQFTV--VIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
37-203 |
3.91e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 96.84 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmNDLVDICriEGEILLHGQNIYDksVDVAAlrRNVGMVFQ 116
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV---AGLERIT--SGEIWIGGRVVNE--LEPAD--RDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPK-SIYENVVYGLRLQGIkEKRKLDEVVEQslrgAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PRK11650 84 NYALYPHmSVRENMAYGLKIRGM-PKAEIEERVAE----AARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
....*...
gi 494860364 196 DEPTSALD 203
Cdd:PRK11650 159 DEPLSNLD 166
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-246 |
7.84e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDVA 105
Cdd:PRK11300 3 QPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF-----YKPTGGTILLRGQHIEGLPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 AlRRNVGMVFQRPNPFPK-SIYEN------------VVYGLrLQGIKEKRKLDEVVEQslrgAALWDEV---KDRLHDSA 169
Cdd:PRK11300 78 A-RMGVVRTFQHVRLFREmTVIENllvaqhqqlktgLFSGL-LKTPAFRRAESEALDR----AATWLERvglLEHANRQA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 170 FGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMG 246
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
37-256 |
1.55e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.22 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndlvdICRI----EGEILLHGQniydksvdVAALrRNVG 112
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKL---------IAGIleptSGRVEVNGR--------VSAL-LELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 113 MVFQrpnpfPK-SIYENVVYGLRLQGIKEK---RKLDEVVEQSLRGAALWDEVKDrlhdsafgLSGGQQQRLVIARSIAI 188
Cdd:COG1134 97 AGFH-----PElTGRENIYLNGRLLGLSRKeidEKFDEIVEFAELGDFIDQPVKT--------YSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 189 EPEVLLLDEPTSALDPI----STLVIEELINDLKnqfTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNT 256
Cdd:COG1134 164 DPDILLVDEVLAVGDAAfqkkCLARIRELRESGR---TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
29-228 |
1.58e-22 |
|
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: 90.20 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDIcriEGEILlHGQNIYdksvdvaalr 108
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEPD---EGIVT-WGSTVK---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 rnvgmvfqrpnpfpksiyenVVYglrlqgikekrkldevVEQslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSIAI 188
Cdd:cd03221 65 --------------------IGY----------------FEQ---------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494860364 189 EPEVLLLDEPTSALDPIStlvIEELINDLKN-QFTVVIVTH 228
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALKEyPGTVILVSH 125
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-266 |
2.78e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 17 LDLENLtddQKALEIKD--LDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKST----LLRCINRmndlvdicriEGEI 90
Cdd:PRK15134 276 LDVEQL---QVAFPIRKgiLKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS----------QGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 91 LLHGQNIYDKSV-DVAALRRNVGMVFQRPNPF--PK-SIYENVVYGLRL-QGIKEKRKLDEVVEQSLRGAALWDEVKDRl 165
Cdd:PRK15134 343 WFDGQPLHNLNRrQLLPVRHRIQVVFQDPNSSlnPRlNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHR- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 166 HDSAFglSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFM 243
Cdd:PRK15134 422 YPAEF--SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqqKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|...
gi 494860364 244 YMGELIEYSDTNTLFTTPTKKKT 266
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYT 522
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-257 |
3.47e-22 |
|
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: 95.64 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDIcriEGEILLH--------------- 93
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT---SGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 94 --------GQNIYDKSVDV--------AALRRNVGMVFQRPNPF--PKSIYENVVYGLRLQGIKEKRKLDEVVEqslrga 155
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDFwnlsdklrRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 156 aLWDEVK--DRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQ 231
Cdd:TIGR03269 152 -LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 494860364 232 QAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
29-249 |
3.49e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.86 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLrcinrmNDLVDICR-IEGEILLHGQNIYDKSVdVAAL 107
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLL------GTLCGDPRaTSGRIVFDGKDITDWQT-AKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPK-SIYENVVYGlrlqGIKEKRKldEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSI 186
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMG----GFFAERD--QFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-262 |
5.56e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY---GDKQ----------ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndLVDICriEGEILLHGQ 95
Cdd:PRK15079 9 LEVADLKVHFdikDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKAT--DGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 96 NIYDKS-VDVAALRRNVGMVFQRP----NPfPKSIYENVVYGLRL-------QGIKEKrkldevVEQSLRGAALWDEVKD 163
Cdd:PRK15079 84 DLLGMKdDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTyhpklsrQEVKDR------VKAMMLKVGLLPNLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 164 RL-HDsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALD-PISTLVIeELINDLKNQ--FTVVIVTHNMQQAARVSDQ 239
Cdd:PRK15079 157 RYpHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDvSIQAQVV-NLLQQLQREmgLSLIFIAHDLAVVKHISDR 231
|
250 260
....*....|....*....|...
gi 494860364 240 TAFMYMGELIEYSDTNTLFTTPT 262
Cdd:PRK15079 232 VLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
39-243 |
5.77e-22 |
|
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: 94.81 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGQNIYdkSVDVAALRRNVGMVFQR 117
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL------LVGVWPpTAGSVRLDGADLS--QWDREELGRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 PNPFPKSIYENVVyglRLQGIKEkrklDEVVEqslrgAALWDEVKD-----------RLHDSAFGLSGGQQQRLVIARSI 186
Cdd:COG4618 415 VELFDGTIAENIA---RFGDADP----EKVVA-----AAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMqQAARVSDQTAFM 243
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVL 539
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-252 |
6.65e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 31 IKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvdicrieGEILL-HGQNIYDKSVDVAALRr 109
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA------------GELEPdSGEVSIPKGLRIGYLP- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 nvgmvfQRPNPFP-KSIYENVVYGLR--LQGIKEKR----KLDEVVEQSLRGAALWDE---------------------V 161
Cdd:COG0488 68 ------QEPPLDDdLTVLDTVLDGDAelRALEAELEeleaKLAEPDEDLERLAELQEEfealggweaearaeeilsglgF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 162 KDRLHDSAFG-LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNqfTVVIVTH-----NmqqaaR 235
Cdd:COG0488 142 PEEDLDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSHdryflD-----R 214
|
250
....*....|....*..
gi 494860364 236 VSDQTAFMYMGELIEYS 252
Cdd:COG0488 215 VATRILELDRGKLTLYP 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-238 |
7.87e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrMN--------DlvdicriEGEILLHGqniyd 99
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVDV----AALRRNVGMVFQRPNPFPK-SIYENVVYGL-RLQGI-----KEKRKLDEVVEQSlrGAALwdEVKDRLHDs 168
Cdd:COG3845 67 KPVRIrsprDAIALGIGMVHQHFMLVPNlTVAENIVLGLePTKGGrldrkAARARIRELSERY--GLDV--DPDAKVED- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 169 afgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPIStlvIEEL---INDLKNQ-FTVVIVTHNMQQAARVSD 238
Cdd:COG3845 142 ---LSVGEQQRVEILKALYRGARILILDEPTAVLTPQE---ADELfeiLRRLAAEgKSIIFITHKLREVMAIAD 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
44-262 |
9.06e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 9.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIydKSVDVAALRRNVGMVFQR-PNPFP 122
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPL--ESWSSKAFARKVAYLPQQlPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 123 KSIYENVVYG-------LRLQGIKEKRKLDEVVeqSLRGAAlwdEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PRK10575 100 MTVRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLK---PLAHRLVDS---LSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQ--FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
44-235 |
1.12e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 90.61 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKSVDV-AALR-RNVGMVFQRPNPF 121
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PK-SIYENVVYGLRLQGIKEKRKLDevveqslRGAALWDEV--KDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEP 198
Cdd:PRK10584 101 PTlNALENVELPALLRGESSRQSRN-------GAKALLEQLglGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 494860364 199 TSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAAR 235
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
40-261 |
1.49e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 93.62 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKSVDvaALRRNVGMVFQRPN 119
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE-----GDIRFHDIPLTKLQLD--SWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPKSIYENVVYG---LRLQGIKEKRKLDEVVEQSLRGAALWD-EVKDRlhdsAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PRK10789 400 LFSDTVANNIALGrpdATQQEIEHVARLASVHDDILRLPQGYDtEVGER----GVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMqQAARVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-251 |
1.73e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.90 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLHGQniydksvDVAA 106
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI-YPPD----SGTVTVRGR-------VSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMvfqRPNpfpKSIYENVVYGLRLQGIKEKR---KLDEVVEQSlrgaalwdEVKDRLHDSAFGLSGGQQQRLVIA 183
Cdd:cd03220 89 LGLGGGF---NPE---LTGRENIYLNGRLLGLSRKEideKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 184 RSIAIEPEVLLLDEPTSALDPI----STLVIEELINDLKnqfTVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGK---TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-250 |
2.13e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.37 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 24 DDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvdicRI---EGEILLHGQNiyDK 100
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--------RLapdAGEVHYRMRD--GQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVAAL----RRNV-----GMVFQRPNPfpksiyenvvyGLRLQ-----GIKEKrkLDEVVEQ---SLRGAAL-W-DEV 161
Cdd:PRK11701 72 LRDLYALseaeRRRLlrtewGFVHQHPRD-----------GLRMQvsaggNIGER--LMAVGARhygDIRATAGdWlERV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 162 K---DRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-----VIEELINDLknQFTVVIVTHNMQQA 233
Cdd:PRK11701 139 EidaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQarlldLLRGLVREL--GLAVVIVTHDLAVA 215
|
250
....*....|....*..
gi 494860364 234 ARVSDQTAFMYMGELIE 250
Cdd:PRK11701 216 RLLAHRLLVMKQGRVVE 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-267 |
2.16e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 93.25 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY--GDKQ--ALNKVNMNIPKGQVTAFIGPSGCGKSTL---LRCINRMNdlvdicriEGEILLHGQNIYDKS 101
Cdd:PRK10535 5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLmniLGCLDKPT--------SGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 102 VD-VAALRR-NVGMVFQRPNPFPK-SIYENV----VYGlrlqGIKEKRKLDEVVEQSLRGAalwdeVKDRLHDSAFGLSG 174
Cdd:PRK10535 77 ADaLAQLRReHFGFIFQRYHLLSHlTAAQNVevpaVYA----GLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARvSDQTAFMYMGELIeySD 253
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQ-AERVIEIRDGEIV--RN 224
|
250
....*....|....
gi 494860364 254 TNTLFTTPTKKKTE 267
Cdd:PRK10535 225 PPAQEKVNVAGGTE 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-240 |
2.54e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDicrIEGEILLhGQNI----YDKsv 102
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEP---DSGTVKL-GETVkigyFDQ-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNvgmvfqrpnpfpKSIYENVvyglrlqgikeKRKLDEVVEQSLR---------GAALWDEVKDrlhdsafgLS 173
Cdd:COG0488 386 HQEELDPD------------KTVLDEL-----------RDGAPGGTEQEVRgylgrflfsGDDAFKPVGV--------LS 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-VIEELINDlknqF--TVVIVTHNMQQAARVSDQT 240
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLD-IETLeALEEALDD----FpgTVLLVSHDRYFLDRVATRI 499
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
43-264 |
9.39e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 9.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSvDVAALRRNVGMVFQRPNP-- 120
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL-----LRPQKGKVLVSGIDTGDFS-KLQGIRKLVGIVFQNPETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 FPKSIYENVVYG---LRLQGIKEKRKLDEVVEQSLRGaalwdevKDRlHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDE 197
Cdd:PRK13644 91 VGRTVEEDLAFGpenLCLPPIEIRKRVDRALAEIGLE-------KYR-HRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 198 PTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQaARVSDQTAFMYMGELIEYSDTNTLFTTPTKK 264
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-267 |
9.81e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.46 E-value: 9.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLDLYYGDKQ----ALNKVNMNIPKGQVTAFIGPSGCGKS----TLLRCINRMNDLVDicriEGEILLHG 94
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQ----CDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 95 QN---IYDKSVDVAALRR----NVGMVFQRP----NP-FPksIYENVVYGLRL-QGI-------KEKRKLDEVveqslrg 154
Cdd:PRK10261 83 RSrqvIELSEQSAAQMRHvrgaDMAMIFQEPmtslNPvFT--VGEQIAESIRLhQGAsreeamvEAKRMLDQV------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 155 aaLWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFT--VVIVTHNMQQ 232
Cdd:PRK10261 154 --RIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGV 231
|
250 260 270
....*....|....*....|....*....|....*
gi 494860364 233 AARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTE 267
Cdd:PRK10261 232 VAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-228 |
1.43e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLDLYYGDKQALNK-VNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvdicrI----EGEILLHgqni 97
Cdd:COG4178 357 TSEDGALALEDLTLRTPDGRPLLEdLSLSLKPGERLLITGPSGSGKSTLLRAIAG---------LwpygSGRIARP---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 ydksvdvaalrRNVGMVF--QRPnpfpksiY-------ENVVYGLRLQGIKekrklDEVVEQSLRGAALwDEVKDRLHDS 168
Cdd:COG4178 424 -----------AGARVLFlpQRP-------YlplgtlrEALLYPATAEAFS-----DAELREALEAVGL-GHLAERLDEE 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 169 A---FGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:COG4178 480 AdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-239 |
1.62e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 91.24 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 19 LENLTDDQKALEIKDLDLYYgdkqaLNKVNMNIPKG--------QVTAFIGPSGCGKSTLLRCINRMNDLVD-------- 82
Cdd:PTZ00265 1156 IKNKNDIKGKIEIMDVNFRY-----ISRPNVPIYKDltfscdskKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfkn 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 83 -----------------------------------------ICRIEGEILLHGQNIYDksVDVAALRRNVGMVFQRPNPF 121
Cdd:PTZ00265 1231 ehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PKSIYENVVYGlrlqgiKEKRKLDEVvEQSLRGAALwDEVKDRL---HDSAFG-----LSGGQQQRLVIARSIAIEPEVL 193
Cdd:PTZ00265 1309 NMSIYENIKFG------KEDATREDV-KRACKFAAI-DEFIESLpnkYDTNVGpygksLSGGQKQRIAIARALLREPKIL 1380
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 494860364 194 LLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARvSDQ 239
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKR-SDK 1427
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-251 |
9.02e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVDVAAlR 108
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-----VPRDAGNIIIDDEDISLLPLHARA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENvvyglrLQGIKEKRKLDEVVEQSLRGAALWDE-----VKDRLHDSafgLSGGQQQRLVI 182
Cdd:PRK10895 78 RGIGYLPQEASIFRRlSVYDN------LMAVLQIRDDLSAEQREDRANELMEEfhiehLRDSMGQS---LSGGERRRVEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEY 251
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGHLIAH 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
38-249 |
1.04e-19 |
|
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: 85.46 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 38 YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICR-IEGEILLHGQNIYDKSVdvaALRRNVGMVF- 115
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKI------LSGLLQpTSGEVRVAGLVPWKRRK---KFLRRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 116 QRPN-----------PFPKSIY--ENVVYGLRLQGIKEKRKLDEVVEQSLRgaalwdevkdrlhdsafGLSGGQQQRLVI 182
Cdd:cd03267 102 QKTQlwwdlpvidsfYLLAAIYdlPPARFKKRLDELSELLDLEELLDTPVR-----------------QLSLGQRMRAEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 183 ARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-239 |
1.92e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICRIE-GEILLHGQNIYDKSvdvAA 106
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRM------LLGLTHPDaGSISLCGEPVPSRA---RH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPK-SIYENVV-----YGLRLQGIKEKrkldevVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRL 180
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDfTVRENLLvfgryFGLSAAAARAL------VPPLLEFAKLENKADAKVGE----LSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPIST-LVIEELINDLKNQFTVVIVTHNMQQAARVSDQ 239
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARhLMWERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-254 |
5.35e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 19 LENLTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinrM-NDLVDICriEGEILLHGQNI 97
Cdd:NF033858 257 RPADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMK----MlTGLLPAS--EGEAWLFGQPV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 YDKSVDVaalRRNVGMVFQrpnPFpkSIYE------NVVYGLRLQGIKEKR---KLDEVVEQ-SLRgaalwdEVKDRLHD 167
Cdd:NF033858 331 DAGDIAT---RRRVGYMSQ---AF--SLYGeltvrqNLELHARLFHLPAAEiaaRVAEMLERfDLA------DVADALPD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 168 SafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVsDQTAFMYM 245
Cdd:NF033858 397 S---LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHA 472
|
....*....
gi 494860364 246 GELIEySDT 254
Cdd:NF033858 473 GRVLA-SDT 480
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-239 |
6.87e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKSVDVAALRRN--VGMVFQRPNPF 121
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT-----PTSGDVIFNGQPMSKLSSAAKAELRNqkLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PK-SIYENVVYGLRLQGIKEKRKLDEVVEQsLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTS 200
Cdd:PRK11629 100 PDfTALENVAMPLLIGKKKPAEINSRALEM-LAAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494860364 201 ALDPISTLVIEELINDL-KNQFTV-VIVTHNMQQAARVSDQ 239
Cdd:PRK11629 175 NLDARNADSIFQLLGELnRLQGTAfLVVTHDLQLAKRMSRQ 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-258 |
7.39e-19 |
|
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: 86.22 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIyDKSVDvaALRRNVGMVFQRPNP 120
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGL-----LPPTSGTVLVGGKDI-ETNLD--AVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 FPK-SIYENVVYGLRLQGikekRKLDEV---VEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEVLLLD 196
Cdd:TIGR01257 1015 FHHlTVAEHILFYAQLKG----RSWEEAqleMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 197 EPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGELieYSDTNTLF 258
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL--YCSGTPLF 1146
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
39-228 |
4.14e-18 |
|
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: 83.55 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGQNIydKSVDVAALRRNVGMVFQRP 118
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----VGIWPPTSGSVRLDGADL--KQWDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 NPFPKSIYENVVY---GLRLQGIKEKRKLDEVVEQSLRGAALWDEVkdrLHDSAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:TIGR01842 402 ELFPGTVAENIARfgeNADPEKIIEAAKLAGVHELILRLPDGYDTV---IGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190
....*....|....*....|....*....|....
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQ-FTVVIVTH 228
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARgITVVVITH 512
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
53-249 |
5.08e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 53 KGQVTAFIGPSGCGKSTLLrciNRMNDLVdicRIEGEILLHGQNIydKSVDVAALRRNVGMVFQR-PNPFPKSIYEnvvY 131
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLL---ARMAGLL---PGQGEILLNGRPL--SDWSAAELARHRAYLSQQqSPPFAMPVFQ---Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 132 -GLRLQGIKEKRKLDEVVEQSLRgaALwdEVKDRLHDSAFGLSGGQQQRLVIARSI-----AIEPE--VLLLDEPTSALD 203
Cdd:COG4138 90 lALHQPAGASSEAVEQLLAQLAE--AL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494860364 204 PISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:COG4138 166 VAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-228 |
7.47e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 24 DDQKAL-----EIKDLDL-YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNI 97
Cdd:PRK10790 331 NDDRPLqsgriDIDNVSFaYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-----EGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 ydKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGlrlQGIKEKRKLD--EVVEQSLRGAALWDEVKDRLHDSAFGLSGG 175
Cdd:PRK10790 406 --SSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQalETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTH 228
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-261 |
1.41e-17 |
|
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: 79.87 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvdicrieGEILL-HGQNIYD----KSVD 103
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA------------GRLAPdHGTATYImrsgAELE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAAL---------RRNVGMVFQRPNPfpksiyenvvyGLRLQ-----GIKEkRKLDEVVEQ--SLRGAAL-W-DEVK--- 162
Cdd:TIGR02323 72 LYQLseaerrrlmRTEWGFVHQNPRD-----------GLRMRvsagaNIGE-RLMAIGARHygNIRATAQdWlEEVEidp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 163 DRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQT 240
Cdd:TIGR02323 140 TRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRL 219
|
250 260
....*....|....*....|.
gi 494860364 241 AFMYMGELIEYSDTNTLFTTP 261
Cdd:TIGR02323 220 LVMQQGRVVESGLTDQVLDDP 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
44-231 |
1.43e-17 |
|
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: 79.30 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEIllHGQNIYDKSVDVAAL----RRNVGMVFQRPN 119
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKV--HWSNKNESEPSFEATrsrnRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPKSIYENVVYGLRLQGIKEKRKLDEVVEQ---SLRGAALWDEVKDRlhdsAFGLSGGQQQRLVIARSIAIEPEVLLLD 196
Cdd:cd03290 90 LLNATVEENITFGSPFNKQRYKAVTDACSLQpdiDLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 494860364 197 EPTSALD-PISTLVIEELINDL--KNQFTVVIVTHNMQ 231
Cdd:cd03290 166 DPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
35-227 |
3.15e-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: 77.67 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 35 DLYY------GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI-NRMNDLVdicrIEGEILLHGQNIydksvdVAAL 107
Cdd:cd03232 8 NLNYtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGV----ITGEILINGRPL------DKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRPNPFPKSiyenvvyglrlqgikekrkldeVVEQSLRGAALWdevkdRlhdsafGLSGGQQQRLVIARSIA 187
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL----------------------TVREALRFSALL-----R------GLSVEQRKRLTIGVELA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494860364 188 IEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVT 227
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCT 164
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-248 |
5.36e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 76.70 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLyygdKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRIE-GEILLHGQNIYDKSVDvAA 106
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL------FGLRPPAsGEITLDGKPVTRRSPR-DA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVfqrpnP--------FPK-SIYENVVygLRLQgikekrkldevveqslrgaalwdevkdrlhdsafgLSGGQQ 177
Cdd:cd03215 73 IRAGIAYV-----PedrkreglVLDlSVAENIA--LSSL-----------------------------------LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 178 QRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-228 |
7.49e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.76 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLvDIcrIEGEILLHGQNIYDKSVDVA 105
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAY-KI--LEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 AlRRNVGMVFQRPNPFPKSIYENVvygLRLqGIKEKRKLDEVVEqsLRGAALWDEVKDRLH----DSAF-------GLSG 174
Cdd:CHL00131 82 A-HLGIFLAFQYPIEIPGVSNADF---LRL-AYNSKRKFQGLPE--LDPLEFLEIINEKLKlvgmDPSFlsrnvneGFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-VIEELINDLKNQFT-VVIVTH 228
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLD-IDALkIIAEGINKLMTSENsIILITH 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
46-249 |
7.65e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 46 KVNMNIPKGQVTAFIGPSGCGKSTLlrcINRMNDLV--DicriEGEILLHGQNIYD--KSVDVAALRRNVGMVFQRPNPF 121
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSL---INAISGLTrpQ----KGRIVLNGRVLFDaeKGICLPPEKRRIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PK-SIYENVVYGLRLqgiKEKRKLDEVVEqsLRGAalwDEVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVLLLDEPTS 200
Cdd:PRK11144 89 PHyKVRGNLRYGMAK---SMVAQFDKIVA--LLGI---EPLLDRYPGS---LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 201 ALD-PISTLVI---EELINDLKnqFTVVIVTHNMQQAARVSDQTAFMYMGELI 249
Cdd:PRK11144 158 SLDlPRKRELLpylERLAREIN--IPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
39-230 |
8.27e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 80.37 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 39 GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGQNIYdksVDVAALRRNvgmvfqrp 118
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKGSVAY---VPQQAWIQN-------- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 npfpKSIYENVVYGLRLQgikEKRkldevVEQSLRGAALWDEVK-----DR--LHDSAFGLSGGQQQRLVIARSIAIEPE 191
Cdd:TIGR00957 713 ----DSLRENILFGKALN---EKY-----YQQVLEACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494860364 192 VLLLDEPTSALDP-ISTLVIEELIND---LKNQfTVVIVTHNM 230
Cdd:TIGR00957 781 IYLFDDPLSAVDAhVGKHIFEHVIGPegvLKNK-TRILVTHGI 822
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-261 |
1.20e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDK----QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNdLVDI-CRIEGEIL-LHGQNIYDKSv 102
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAI--MG-LIDYpGRVMAEKLeFNGQDLQRIS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 dvAALRRN-----VGMVFQRP----NPFPKSIYEnVVYGLRL-QGIKEKRKLDEVVEQsLRGAALWDEvKDRLHDSAFGL 172
Cdd:PRK11022 80 --EKERRNlvgaeVAMIFQDPmtslNPCYTVGFQ-IMEAIKVhQGGNKKTRRQRAIDL-LNQVGIPDP-ASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|.
gi 494860364 251 YSDTNTLFTTP 261
Cdd:PRK11022 235 TGKAHDIFRAP 245
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-270 |
1.69e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.92 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 17 LDLENLTddqkaLEIKDLDlyyGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI---NRMNDLV--DICRIEGEIL 91
Cdd:PRK15093 4 LDIRNLT-----IEFKTSD---GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvTKDNWRVtaDRMRFDDIDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 92 LHGQNIYDKSVdvaaLRRNVGMVFQRP----NP-----------FPKSIYEnvvyGLRLQGIK-EKRKLDEVveqsLRGA 155
Cdd:PRK15093 76 LRLSPRERRKL----VGHNVSMIFQEPqsclDPservgrqlmqnIPGWTYK----GRWWQRFGwRKRRAIEL----LHRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 156 ALWDEvKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQA 233
Cdd:PRK15093 144 GIKDH-KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQML 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 494860364 234 ARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDYI 270
Cdd:PRK15093 223 SQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-253 |
2.48e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 23 TDDQKALEIKDLdlyyGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI---NRmndlvdicRIEGEILLHGQNIYD 99
Cdd:COG1129 251 APGEVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgaDP--------ADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVdVAALRRNVGMV---------FQrpnpfPKSIYENVVY--------GLRLQGIKEKRKLDEVVEQ-SLRGAALWDEV 161
Cdd:COG1129 319 RSP-RDAIRAGIAYVpedrkgeglVL-----DLSIRENITLasldrlsrGGLLDRRRERALAEEYIKRlRIKTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 162 KDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpistlV-----IEELINDLKNQFTVVIVthnmqqaarV 236
Cdd:COG1129 393 GN--------LSGGNQQKVVLAKWLATDPKVLILDEPTRGID-----VgakaeIYRLIRELAAEGKAVIV---------I 450
|
250
....*....|....*..
gi 494860364 237 SDqtafmYMGELIEYSD 253
Cdd:COG1129 451 SS-----ELPELLGLSD 462
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-254 |
2.76e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY-----GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHgqnIYDKSVD 103
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV-----LEPTSGEVNVR---VGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 VAALR--------RNVGMVFQRPNPFP-KSIYENVVYGLRLQGIKEKRKLDEVVeqSLRGAALWDE----VKDRLHDSaf 170
Cdd:TIGR03269 352 MTKPGpdgrgrakRYIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEEkaeeILDKYPDE-- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 171 gLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:TIGR03269 428 -LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*.
gi 494860364 249 IEYSDT 254
Cdd:TIGR03269 507 VKIGDP 512
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
28-235 |
3.09e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLrcinrmnDLVDICRI--EGEILLHGQNIYDksvdvA 105
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEVLGGDMAD-----A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVG-----MvfqrP-----NPFPK-SIYENVVYGLRL--QGIKE-KRKLDEVveqsLRGAALwDEVKDRLhdsAFG 171
Cdd:NF033858 69 RHRRAVCpriayM----PqglgkNLYPTlSVFENLDFFGRLfgQDAAErRRRIDEL----LRATGL-APFADRP---AGK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLK---NQFTVVIVTHNMQQAAR 235
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRaerPGMSVLVATAYMEEAER 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-260 |
1.48e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDICRI-EGEILLHGQNIYDksvd 103
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKA------LMGFVRLaSGKISILGQPTRQ---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 vaALRRN-VGMVFQRPN---PFPkSIYENVV----YG----LRLQGIKEKRKLDEVVEQSlrgaalwdEVKDRLHDSAFG 171
Cdd:PRK15056 74 --ALQKNlVAYVPQSEEvdwSFP-VLVEDVVmmgrYGhmgwLRRAKKRDRQIVTAALARV--------DMVEFRHRQIGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAfMYMGELIE 250
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLA 221
|
250
....*....|
gi 494860364 251 YSDTNTLFTT 260
Cdd:PRK15056 222 SGPTETTFTA 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
42-275 |
2.65e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIydKSVDVAALRRNVGMVFQRP--- 118
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM-----IEPTSGELLIDDHPL--HFGDYSYRSQRIRMIFQDPsts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 -NPfPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAALwdeVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDE 197
Cdd:PRK15112 100 lNP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 198 PTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLFTTPTKKKTEDYITGRYG 275
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFG 255
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-261 |
2.91e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.56 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 17 LDLENLTddqkaLEIKDLDlyyGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDICRIEGEIL-LHGQ 95
Cdd:COG4170 4 LDIRNLT-----IEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTADRFrWNGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 96 NIYDKSVDV--AALRRNVGMVFQRP----NPFPK-------SIYENVVYGLRLQGIKEKRKldevveqslRGAALWDEVK 162
Cdd:COG4170 74 DLLKLSPRErrKIIGREIAMIFQEPssclDPSAKigdqlieAIPSWTFKGKWWQRFKWRKK---------RAIELLHRVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 163 DRLHDS-----AFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLkNQF---TVVIVTHNMQQAA 234
Cdd:COG4170 145 IKDHKDimnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL-NQLqgtSILLISHDLESIS 223
|
250 260
....*....|....*....|....*..
gi 494860364 235 RVSDQTAFMYMGELIEYSDTNTLFTTP 261
Cdd:COG4170 224 QWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-231 |
1.08e-14 |
|
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: 73.79 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 9 NQANIGQKLDLEN--LTD---DQKALEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlv 81
Cdd:TIGR01271 1193 GKYQLSTVLVIENphAQKcwpSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL---- 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 82 diCRIEGEILLHGqnIYDKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLR-----LQGIKEKRKLDEVVEQslrgaa 156
Cdd:TIGR01271 1269 --LSTEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLKSVIEQ------ 1338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 157 LWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQ 231
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
29-231 |
4.80e-14 |
|
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: 70.27 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdiCRIEGEILLHGQNIydKSVDVAA 106
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVSW--NSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIYENV-VYGL----RLQGIKEKRKLDEVVEQslrgaaLWDEVKDRLHDSAFGLSGGQQQRLV 181
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLdPYGKwsdeEIWKVAEEVGLKSVIEQ------FPGQLDFVLVDGGCVLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494860364 182 IARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQ 231
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-228 |
5.29e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.95 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGqniydksvdvaalRRNVGMVFQRPNpFPk 123
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGMPE-------------GEDLLFLPQRPY-LP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 124 siyenvvyglrlQGikekrkldevveqSLRGAAL--WDEVkdrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSA 201
Cdd:cd03223 77 ------------LG-------------TLREQLIypWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*..
gi 494860364 202 LDPISTLVIEELINDLKnqFTVVIVTH 228
Cdd:cd03223 122 LDEESEDRLYQLLKELG--ITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-271 |
9.54e-14 |
|
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: 70.62 E-value: 9.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDIcriEGEILLHGQNIYDKSVDVAAlR 108
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTW---DGEIYWSGSPLKASNIRDTE-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGlrlQGIKEKRKLDEVVEQSLRGAALWDEVK-DRLHDS--AFGLSGGQQQRLVIAR 184
Cdd:TIGR02633 78 AGIVIIHQELTLVPElSVAENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQlDADNVTrpVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTLfttptk 263
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM------ 228
|
....*...
gi 494860364 264 kKTEDYIT 271
Cdd:TIGR02633 229 -SEDDIIT 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-238 |
1.22e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDKSVdVAALRRNVGMVFQRPNPF 121
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDGQEMRFAST-TAALAAGVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PK-SIYENVVYGlRLQ---GIKEKRKLDEVVEQSLRGAALWDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEVLLLDE 197
Cdd:PRK11288 92 PEmTVAENLYLG-QLPhkgGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 198 PTSALDPISTLVIEELINDLKNQFTVVI-VTHNMQQAARVSD 238
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCD 208
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-253 |
1.69e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.28 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicRIEGEILLHGQNIYDKSVDVAAlR 108
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE---VTGGTVEFKGKDLLELSPEDRA-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRP-------NPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRgaaLWDEVKDRLHDSA-FGLSGGQQQRL 180
Cdd:PRK09580 78 EGIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIA---LLKMPEDLLTRSVnVGFSGGEKKRN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKN-QFTVVIVTHNMQQAARVS-DQTAFMYMGELIEYSD 253
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGD 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-249 |
4.76e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDIC--------RIEGEILLHGQNIydK 100
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-----DLTgggaprgaRVTGDVTLNGEPL--A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SVDVAALRRNVGMVFQRPNP-FPKSIYENVVYG----LRLQGIKEKRKlDEVVEQSLRGAALwDEVKDRlhdSAFGLSGG 175
Cdd:PRK13547 75 AIDAPRLARLRAVLPQAAQPaFAFSAREIVLLGryphARRAGALTHRD-GEIAWQALALAGA-TALVGR---DVTTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 176 QQQRLVIARSIA---------IEPEVLLLDEPTSALDPISTLVIEELINDLKN--QFTVVIVTHNMQQAARVSDQTAFMY 244
Cdd:PRK13547 150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLA 229
|
....*
gi 494860364 245 MGELI 249
Cdd:PRK13547 230 DGAIV 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-231 |
5.05e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 38 YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRI----EGEILLHGQNIYDKSvdvAALRRNVGM 113
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML---------TGIlvptSGEVRVLGYVPFKRR---KEFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 114 VF-QRPNPFP-----------KSIYE--NVVYglrlqgikeKRKLDEVVEQslrgaaLwdEVKDRLHDSAFGLSGGQQQR 179
Cdd:COG4586 100 VFgQRSQLWWdlpaidsfrllKAIYRipDAEY---------KKRLDELVEL------L--DLGELLDTPVRQLSLGQRMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNMQ 231
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
41-246 |
7.25e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI--NRMNDLVdicrIEGEILLHGqniydKSVDVAALRRNVGMVFQRP 118
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafRSPKGVK----GSGSVLLNG-----MPIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 NPFPK-SIYENVVYG--LRLQ---GIKEKR-KLDEVVEQ-SLRGAA-----LWDEVKdrlhdsafGLSGGQQQRLVIARS 185
Cdd:TIGR00955 109 LFIPTlTVREHLMFQahLRMPrrvTKKEKReRVDEVLQAlGLRKCAntrigVPGRVK--------GLSGGERKRLAFASE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVT-HnmQQAARVS---DQTAFMYMG 246
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiH--QPSSELFelfDKIILMAEG 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-238 |
1.16e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 36 LYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINrmndlvdicrieGEILL-HGQNIYDKSVDVAALRrnvgmv 114
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLdDGRIIYEQDLIVARLQ------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 fQRPnpfPK----SIYENVVYGLRLQGIKEKR------------------KLDEVVEQsLRGAALWdEVKDRLHD--SAF 170
Cdd:PRK11147 73 -QDP---PRnvegTVYDFVAEGIEEQAEYLKRyhdishlvetdpseknlnELAKLQEQ-LDHHNLW-QLENRINEvlAQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 171 G---------LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTlvIEELINDLKN-QFTVVIVTH------NMqqAA 234
Cdd:PRK11147 147 GldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirNM--AT 221
|
....
gi 494860364 235 RVSD 238
Cdd:PRK11147 222 RIVD 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-229 |
1.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRIE-GEILLHGQNIYDKSVDVA-- 105
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLI------AGLLPPAaGTIKLDGGDIDDPDVAEAch 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ------ALRRNVgmvfqrpnpfpkSIYENVVYGLRLQGIKEKRkldevVEQSLRGAALwdevkDRLHDSAFG-LSGGQQQ 178
Cdd:PRK13539 77 ylghrnAMKPAL------------TVAENLEFWAAFLGGEELD-----IAAALEAVGL-----APLAHLPFGyLSAGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELIND-LKNQFTVVIVTHN 229
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-233 |
1.75e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 22 LTDDQKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCIN------RMNDLVDICRIEGEillhGQ 95
Cdd:PRK10938 254 LPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgYSNDLTLFGRRRGS----GE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 96 NIYDksvdvaaLRRNVGMVFQ------RPNpfpkSIYENVVyglrLQGIKEKRKLDEVVEQSLRgaALWDEVKDRLH--- 166
Cdd:PRK10938 330 TIWD-------IKKHIGYVSSslhldyRVS----TSVRNVI----LSGFFDSIGIYQAVSDRQQ--KLAQQWLDILGidk 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 167 ---DSAF-GLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPIS-TLV---IEELINDLKNQftVVIVTHNMQQA 233
Cdd:PRK10938 393 rtaDAPFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrQLVrrfVDVLISEGETQ--LLFVSHHAEDA 465
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
29-238 |
2.75e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlVDICRIE-GEILLHGQNIyDKsvDVAAL 107
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLI------AGLLNPEkGEILFERQSI-KK--DLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 108 RRNVGMVFQRP--NPFpKSIYENVVYGLRLQgiKEKRKLDEVVEQSLRGAALwdevkdrlhDSAFG-LSGGQQQRLVIAR 184
Cdd:PRK13540 73 QKQLCFVGHRSgiNPY-LTLRENCLYDIHFS--PGAVGITELCRLFSLEHLI---------DYPCGlLSSGQKRQVALLR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARVSD 238
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
42-272 |
2.83e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrmndLVDI-CRIEGEILLHGQNIYDKSVDvAALRRNVGMVFQRPNP 120
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKC------LFGIyQKDSGSILFQGKEIDFKSSK-EALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 F-PKSIYENV---VYGLRLQGIKEKRKLDEVveqslrgAALWDEV------KDRLHDsafgLSGGQQQRLVIARSIAIEP 190
Cdd:PRK10982 85 VlQRSVMDNMwlgRYPTKGMFVDQDKMYRDT-------KAIFDELdididpRAKVAT----LSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 191 EVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEysdtntlfTTPTKKKTEDY 269
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDK 225
|
...
gi 494860364 270 ITG 272
Cdd:PRK10982 226 IIA 228
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
54-236 |
3.03e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 54 GQVTAFIGPSGCGKSTLLRCINRMNDLvdicriEGEILLHGQNIYDKSVDVAALRRNVGMVFQRPnPFPKSIYEnvvY-- 131
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLEAWSAAELARHRAYLSQQQTP-PFAMPVFQ---Ylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 132 -----GLRLQGIKEKrkLDEVVEQsLRgaalwdeVKDRLHDSAFGLSGGQQQR-------LVIARSIAIEPEVLLLDEPT 199
Cdd:PRK03695 92 lhqpdKTRTEAVASA--LNEVAEA-LG-------LDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 200 SALDPISTLVIEELINDLKNQFTVVIVT-----HNMQQAARV 236
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSshdlnHTLRHADRV 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-250 |
3.91e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYygDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIYDKSvDVAALRR 109
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRS-PLDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 NVGMVFQ--RPNPF-PK-SIYENVVYG--LRLQGIKEKRKL-DEVVEQSLRgaalwDEVKDRL-------HDSAFGLSGG 175
Cdd:PRK09700 339 GMAYITEsrRDNGFfPNfSIAQNMAISrsLKDGGYKGAMGLfHEVDEQRTA-----ENQRELLalkchsvNQNITELSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVI-VTHNMQQAARVSDQTAFMYMGELIE 250
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-257 |
4.00e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrMNDLVDICRIE-GEILLHGQNIYDKSVDv 104
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTM------MKVLTGIYTRDaGSILYLGKEVTFNGPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 105 AALRRNVGMVFQRPNPFPK-SIYENVVYGL----RLQGIKEKRKLDEVveqslrgaalwDEVKDRL---HDS---AFGLS 173
Cdd:PRK10762 75 SSQEAGIGIIHQELNLIPQlTIAENIFLGRefvnRFGRIDWKKMYAEA-----------DKLLARLnlrFSSdklVGELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 174 GGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYS 252
Cdd:PRK10762 144 IGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKEIFEICDDVTVFRDGQFIAER 223
|
....*
gi 494860364 253 DTNTL 257
Cdd:PRK10762 224 EVADL 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-236 |
5.27e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 31 IKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvdicRIEGEILLHGQNIYDKSVDVAALRRn 110
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--------RIQGNNFTGTILANNRKPTKQILKR- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 111 VGMVFQRPNPFPK-SIYENVVYG--LRLQGIKEKRKLDEVVEQSLRGAALwDEVKDRLHDSAF--GLSGGQQQRLVIARS 185
Cdd:PLN03211 142 TGFVTQDDILYPHlTVRETLVFCslLRLPKSLTKQEKILVAESVISELGL-TKCENTIIGNSFirGISGGERKRVSIAHE 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 494860364 186 IAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTvVIVTHNMQQAARV 236
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-254 |
6.32e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNiYDKSVDVAALR 108
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-----VPPDSGTLEIGGNP-CARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGL-RLQGIKEKrkldevVEQSLrgAALWDEVKdrLHDSAFGLSGGQQQRLVIARSI 186
Cdd:PRK15439 86 LGIYLVPQEPLLFPNlSVKENILFGLpKRQASMQK------MKQLL--AALGCQLD--LDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFM------YMGELIEYSDT 254
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQLADRISVMrdgtiaLSGKTADLSTD 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-270 |
6.85e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdiCRI------EGEIL-----LHGQNI 97
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL---------SGVyphgtyEGEIIfegeeLQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 98 YDKSvdvaalRRNVGMVFQRPNPFPK-SIYENVVYG---------------LRLQGIKEKRKLDEVVEQslrgaalwdEV 161
Cdd:PRK13549 77 RDTE------RAGIAIIHQELALVKElSVLENIFLGneitpggimdydamyLRAQKLLAQLKLDINPAT---------PV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 162 KDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQT 240
Cdd:PRK13549 142 GN--------LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISDTI 213
|
250 260 270
....*....|....*....|....*....|
gi 494860364 241 AFMYMGELIEysdtntlfTTPTKKKTEDYI 270
Cdd:PRK13549 214 CVIRDGRHIG--------TRPAAGMTEDDI 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-251 |
7.32e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 33 DLDLyygdkqALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDksVDVAALRRNVG 112
Cdd:TIGR00957 1297 DLDL------VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAK--IGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 113 MVFQRPNPFPKSiyenvvygLRLQGIKEKRKLDEVVEQSLRGAALWDEVK---DRL-HDSAFG---LSGGQQQRLVIARS 185
Cdd:TIGR00957 1364 IIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWWALELAHLKTFVSalpDKLdHECAEGgenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 186 IAIEPEVLLLDEPTSALDpistLVIEELIND-LKNQF---TVVIVTHNMQQaarVSDQTAFMYM--GELIEY 251
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVD----LETDNLIQStIRTQFedcTVLTIAHRLNT---IMDYTRVIVLdkGEVAEF 1500
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-248 |
8.26e-12 |
|
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: 64.85 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD---KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdiCRIEGEILLHGQNIYDKSVdVA 105
Cdd:TIGR02633 258 LEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP----GKFEGNVFINGKPVDIRNP-AQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 ALRRNVGMV---FQRPNPFPK-SIYENVVYGLrLQGIKEKRKLDEVVEQSLRGAALwdevkDRLHDSAF-------GLSG 174
Cdd:TIGR02633 333 AIRAGIAMVpedRKRHGIVPIlGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAI-----QRLKVKTAspflpigRLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
40-258 |
2.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 40 DKQALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrmndlvdICRIEGEiLLHGQniyDKSVDVaalRRNVGMVFQRPN 119
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSL------------ISAMLGE-LSHAE---TSSVVI---RGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFPKSIYENVVYGLRLQGIKEKRKLDEVVEQS----LRGAALwDEVKDRlhdsAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYWRAIDVTALQHdldlLPGRDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 196 DEPTSALDP-ISTLVIEELINDLKNQFTVVIVT---HNMQQAARVSDQTAFMYM--GELIEYSDTNTLF 258
Cdd:PLN03232 765 DDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDRIILVSEGMIKeeGTFAELSKSGSLF 833
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
41-235 |
3.38e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI-NRMNDLVDICRIEGEillhgqniydksvdvaalrrnvgmvfqrPN 119
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLaGALKGTPVAGCVDVP----------------------------DN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 120 PFP--KSIYENVvygLRLQGIKEKRKLDEVVeqSLRGAALW----DEvkdrlhdsafgLSGGQQQRLVIARSIAIEPEVL 193
Cdd:COG2401 95 QFGreASLIDAI---GRKGDFKDAVELLNAV--GLSDAVLWlrrfKE-----------LSTGQKFRFRLALLLAERPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 194 LLDEPTSALDPIstlvieelindlknqfTVVIVTHNMQQAAR 235
Cdd:COG2401 159 VIDEFCSHLDRQ----------------TAKRVARNLQKLAR 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
31-230 |
4.56e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 31 IKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndLVDICRIEGEILLHGQniydksvdvaaLRrn 110
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-----LGLVAPDEGVIKRNGK-----------LR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 111 VGMVfqrpnpfPKSIYENVVYGLRlqgIKEKRKLDEVVEQSLRGAALWDEVKDRLHDSAF-GLSGGQQQRLVIARSIAIE 189
Cdd:PRK09544 69 IGYV-------PQKLYLDTTLPLT---VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMqKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494860364 190 PEVLLLDEPTSALDPISTLVIEELINDLKNQF--TVVIVTHNM 230
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-228 |
6.59e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCIN----------RMNDLVDICRIegeillhgqn 96
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITgqeqpdsgtiEIGETVKLAYV---------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 97 iyDKSVDvaALRRNvgmvfqrpnpfpKSIYENVVYGLRLQGIKEKrkldevveqslrgaalwdEVKDRLHDSAFG----- 171
Cdd:TIGR03719 391 --DQSRD--ALDPN------------KTVWEEISGGLDIIKLGKR------------------EIPSRAYVGRFNfkgsd 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 172 -------LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-VIEELINDLKNqfTVVIVTH 228
Cdd:TIGR03719 437 qqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-VETLrALEEALLNFAG--CAVVISH 498
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-228 |
6.78e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDL-VDicriEGEIllhgqniydKSVDVAa 106
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELePD----SGTV---------KWSENA- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 lrrNVGMvfqrpnpFPKSIYENVVYGLRL-----QGIKEKrklDEvvEQSLRGA---ALW--DEVKdrlhDSAFGLSGGQ 176
Cdd:PRK15064 383 ---NIGY-------YAQDHAYDFENDLTLfdwmsQWRQEG---DD--EQAVRGTlgrLLFsqDDIK----KSVKVLSGGE 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPIStlvIEELINDLKN-QFTVVIVTH 228
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSH 493
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-214 |
7.13e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.20 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQniydksvdvaalr 108
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-----PLAGRVLLNGG------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 rnvGMVFQRPnpfpkSIYENVVYGLRLQGIK------EKRKL------DEVVEQSLRGAALwdevkDRLHDSAFG-LSGG 175
Cdd:cd03231 63 ---PLDFQRD-----SIARGLLYLGHAPGIKttlsvlENLRFwhadhsDEQVEEALARVGL-----NGFEDRPVAqLSAG 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 494860364 176 QQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELI 214
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-243 |
8.31e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNiYDKSVDVAALR 108
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNIN-YNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENV---------VYGLRLQGIKEKRKldevveqslRGAALWDEV--KDRLHDSAFGLSGGQ 176
Cdd:PRK09700 80 LGIGIIYQELSVIDElTVLENLyigrhltkkVCGVNIIDWREMRV---------RAAMMLLRVglKVDLDEKVANLSISH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 177 QQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFT-VVIVTHNMQQAARVSDQTAFM 243
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVM 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-230 |
1.17e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 51 IPK-GQVTAFIGPSGCGKSTLLRCI--------NRMNDLVD----ICRIEG-EILLHGQNIYDKSVDVAalrRNVGMVFQ 116
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSwdevLKRFRGtELQNYFKKLYNGEIKVV---HKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPKSIYEnvvyglRLQGIKEKRKLDEVVEQsLRGAALWD-EVKDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PRK13409 172 IPKVFKGKVRE------LLKKVDERGKLDEVVER-LGLENILDrDISE--------LSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQFTVVIVTHNM 230
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-258 |
1.43e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 60.31 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGD--KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIydKSVDVAA 106
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD-----GKIVIDGIDI--SKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRPNPFPKSIyenvvyglRLQGIKEKRKLDEVVEQSLRGAALWDEVKDR-------LHDSAFGLSGGQQQR 179
Cdd:cd03288 93 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTLF 258
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-254 |
1.51e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 21 NLTDDQKaleIKDldlyyGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCinrMNDLVDICRIEGEILLHGQNIYDK 100
Cdd:TIGR00956 764 NLTYEVK---IKK-----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDS 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 101 SvdvaaLRRNVGMVFQRPNPFPKS-IYENVVYGLRLQ-----GIKEKrklDEVVEQSLRGAALWDEVKDRLHDSAFGLSG 174
Cdd:TIGR00956 833 S-----FQRSIGYVQQQDLHLPTStVRESLRFSAYLRqpksvSKSEK---MEYVEEVIKLLEMESYADAVVGVPGEGLNV 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 175 GQQQRLVIARSIAIEPEVLL-LDEPTSALDPISTLVIEELINDLKNQFTVVIVT-HN-----MQQAARV-----SDQTAf 242
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQpsailFEEFDRLlllqkGGQTV- 983
|
250
....*....|..
gi 494860364 243 mYMGELIEYSDT 254
Cdd:TIGR00956 984 -YFGDLGENSHT 994
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-254 |
2.40e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYY--GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlVDICriEGEILLHGQNIydKSVDVAA 106
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM---VEVC--GGEIRVNGREI--GAYGLRE 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 107 LRRNVGMVFQRP-----------NPFPKSIYENVVYGLRLQGIKEkrkldevveqslRGAALWDEVKDRLHDSAFGLSGG 175
Cdd:PTZ00243 1382 LRRQFSMIPQDPvlfdgtvrqnvDPFLEASSAEVWAALELVGLRE------------RVASESEGIDSRVLEGGSNYSVG 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 176 QQQRLVIARSIAIEPE-VLLLDEPTSALDPISTLVIEELINDLKNQFTVVIVTHNMQQAAR-----VSDQTAFMYMG--- 246
Cdd:PTZ00243 1450 QRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQydkiiVMDHGAVAEMGspr 1529
|
....*...
gi 494860364 247 ELIEYSDT 254
Cdd:PTZ00243 1530 ELVMNRQS 1537
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-256 |
3.01e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 17 LDLENLTDdQKALEIKDldlyygdkqalnkVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQN 96
Cdd:PRK10982 251 LEVRNLTS-LRQPSIRD-------------VSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 97 IYDKSVDVA-----AL----RRNVGMVFQRPNPFpKSIYENV-----VYGLrLQGIKEKRKLDEVVEqSLRgaalwdeVK 162
Cdd:PRK10982 312 INNHNANEAinhgfALvteeRRSTGIYAYLDIGF-NSLISNIrnyknKVGL-LDNSRMKSDTQWVID-SMR-------VK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 163 DRLHDSAFG-LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQT 240
Cdd:PRK10982 382 TPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRI 461
|
250
....*....|....*.
gi 494860364 241 AFMYMGELIEYSDTNT 256
Cdd:PRK10982 462 LVMSNGLVAGIVDTKT 477
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
51-244 |
3.12e-10 |
|
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: 58.92 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 51 IPK-GQVTAFIGPSGCGKSTLLRCINrmNDLV-DICRIEG-----EILLH--G---QN----IYDKSVDVAALRRNVGMV 114
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILA--GKLKpNLGKFDDppdwdEILDEfrGselQNyftkLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 fqrpnpfPKSIYENVvyGLRLQGIKEKRKLDEVVEQ-SLRGaalwdeVKDRLHDSafgLSGGQQQRLVIARSIAIEPEVL 193
Cdd:cd03236 100 -------PKAVKGKV--GELLKKKDERGKLDELVDQlELRH------VLDRNIDQ---LSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 194 LLDEPTSALDPISTL----VIEELINDLKnqfTVVIVTHNMQQAARVSDQTAFMY 244
Cdd:cd03236 162 FFDEPSSYLDIKQRLnaarLIRELAEDDN---YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-257 |
3.43e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 28 ALEIKDLDLY-YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMndlvdICRIEGEILLHGQNIYDKSVD--- 103
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL-----RPPASGSIRLDGEDITGLSPRerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 104 ---VAAL---RRNVGMVfqrPNpFpkSIYENVVygLRLQGIKEKRK---LD---------EVVEQ-SLRGAALWDEVKdr 164
Cdd:COG3845 332 rlgVAYIpedRLGRGLV---PD-M--SVAENLI--LGRYRRPPFSRggfLDrkairafaeELIEEfDVRTPGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 165 lhdsafGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFM 243
Cdd:COG3845 402 ------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILALSDRIAVM 475
|
250
....*....|....
gi 494860364 244 YMGELIEYSDTNTL 257
Cdd:COG3845 476 YEGRIVGEVPAAEA 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-226 |
3.67e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLY---YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCI-----NRmndlvdicRIEGEILLHGQNIY 98
Cdd:NF040905 256 VVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsyGR--------NISGTVFKDGKEVD 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSVD---------VAALRRNVGMVFqrpnpfPKSIYENVVYGlRLQGIKEKRKLDEVVEqslRGAAlwDEVKDRLHDSA 169
Cdd:NF040905 328 VSTVSdaidaglayVTEDRKGYGLNL------IDDIKRNITLA-NLGKVSRRGVIDENEE---IKVA--EEYRKKMNIKT 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 170 FG-------LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVIV 226
Cdd:NF040905 396 PSvfqkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
51-247 |
6.47e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 6.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 51 IPK-GQVTAFIGPSGCGKSTLLRCI--------NRMNDLVD----ICRIEG-EILLHGQNIYDKSVDVAALRRNVGMVfq 116
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILsgelkpnlGDYDEEPSwdevLKRFRGtELQDYFKKLANGEIKVAHKPQYVDLI-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 rpnpfPKSIYENVvyGLRLQGIKEKRKLDEVVEQsLRGAALWD-EVKDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:COG1245 173 -----PKVFKGTV--RELLEKVDERGKLDELAEK-LGLENILDrDISE--------LSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 494860364 196 DEPTSALDPISTLVIEELINDL-KNQFTVVIVTHNMQQAARVSDQTAFMYmGE 247
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDLAILDYLADYVHILY-GE 288
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-250 |
7.58e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 22 LTDDQKALEIKDLDLYY---GDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrmndlvdICRIEGEIllhgQNIY 98
Cdd:PLN03130 608 LEPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSL------------ISAMLGEL----PPRS 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 99 DKSVdvaALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQ----SLRGAALwDEVKDRlhdsAFGLSG 174
Cdd:PLN03130 672 DASV---VIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQhdldLLPGGDL-TEIGER----GVNISG 743
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 175 GQQQRLVIARSIAIEPEVLLLDEPTSALDP-ISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIE 250
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
60-262 |
9.25e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 60 IGPSGCGKSTLLrcinrmNDLVDICRIE-GEILLHGQNIydKSVDVAALRRNVGMVFQRPNPFPKSIYENvvyglrlqgi 138
Cdd:PLN03232 1268 VGRTGAGKSSML------NALFRIVELEkGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFSGTVRFN---------- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 139 kekrkLDEVVEQSlrGAALWD-----EVKDRLHDSAFGL-----------SGGQQQRLVIARSIAIEPEVLLLDEPTSAL 202
Cdd:PLN03232 1330 -----IDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 203 DPISTLVIEELINDLKNQFTVVIVTHNMQQAARVsDQTAFMYMGELIEYSDTNTLFTTPT 262
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-228 |
1.14e-09 |
|
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: 56.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 29 LEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVdicriEGEILLHGQNIYDKSvdvAALR 108
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD-----SGEVRWNGTPLAEQR---DEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 109 RNVGMVFQRPNPFPK-SIYENVVYGLRLQGiKEKRKLDEVVEQ-SLRGAAlwdevkdrlHDSAFGLSGGQQQRLVIARSI 186
Cdd:TIGR01189 73 ENILYLGHLPGLKPElSALENLHFWAAIHG-GAQRTIEDALAAvGLTGFE---------DLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 494860364 187 AIEPEVLLLDEPTSALDPISTLVIEELIND-LKNQFTVVIVTH 228
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-246 |
1.16e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.77 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDIcriEGEILLHGQNIYDKsvdvaalrrnvgmvfQRPNPFPK 123
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSGRISFSP---------------QTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 124 SIYENVVYGL-----RLQGIKEKRKLDEVVeqslrgAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEP 198
Cdd:TIGR01271 502 TIKDNIIFGLsydeyRYTSVIKACQLEEDI------ALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 494860364 199 TSALDPISTLVI-EELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMG 246
Cdd:TIGR01271 576 FTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
41-235 |
1.27e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLrcinrmndlvdicriegEILLHGQNIYDKSVDVAalrRNVGMVFQRPNP 120
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLL-----------------QSLLSQFEISEGRVWAE---RSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 FPKSIYENVVY-----GLRLQGIKEKRKLDEVVEQslRGAALWDEVKDRlhdsAFGLSGGQQQRLVIARSIAIEPEVLLL 195
Cdd:PTZ00243 733 MNATVRGNILFfdeedAARLADAVRVSQLEADLAQ--LGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 494860364 196 DEPTSALDP-ISTLVIEELINDLKNQFTVVIVTHNMQQAAR 235
Cdd:PTZ00243 807 DDPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPR 847
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
44-228 |
1.66e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinrmndlvdicrIEGEIL-LHGQNIYDKSvdvaalRRNVGMVFQRPNPFP 122
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-------------ILGELWpVYGGRLTKPA------KGKLFYVPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 123 KSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAAL---------WDEVKDRLHDsafgLSGGQQQRLVIARSIAIEPEVL 193
Cdd:TIGR00954 529 GTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 494860364 194 LLDEPTSAldpISTLVIEELINDLKN-QFTVVIVTH 228
Cdd:TIGR00954 605 ILDECTSA---VSVDVEGYMYRLCREfGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-231 |
2.78e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 30 EIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinrmndlvdicriegeiLLHGQniydksvdvaaLRR 109
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK------------------LMLGQ-----------LQA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 110 NVGMV----------FQ--RPNPFP-KSIYENVVYGlrlqgikekrKLDEVVEQSLRgaalwdEVKDRLHDSAF------ 170
Cdd:PRK11147 372 DSGRIhcgtklevayFDqhRAELDPeKTVMDNLAEG----------KQEVMVNGRPR------HVLGYLQDFLFhpkram 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 171 ----GLSGGQQQRLVIARsIAIEPEVLL-LDEPTSALDpISTL-VIEELINDLknQFTVVIVTHNMQ 231
Cdd:PRK11147 436 tpvkALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD-VETLeLLEELLDSY--QGTVLLVSHDRQ 498
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
172-248 |
6.64e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 6.64e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
43-257 |
6.98e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLHGqniydksvDVAALRRNVGMVFQRPNpfp 122
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG-----SLSPTVGKVDRNG--------EVSVIAISAGLSGQLTG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 123 ksiYENVVYGLRLQGIKEK--RKL-DEVVEQSLRGAALWDEVKDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPT 199
Cdd:PRK13546 103 ---IENIEFKMLCMGFKRKeiKAMtPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 200 SALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQnKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
44-247 |
7.39e-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: 55.25 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrMNDLVDIcriEGEILLHGQNIYDKSVDVAalrrnvgmvfqrpnpFPK 123
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSGRISFSSQFSWI---------------MPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 124 SIYENVVYGL-----RLQGIKEKRKLDEVVeqslrgAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEP 198
Cdd:cd03291 113 TIKENIIFGVsydeyRYKSVVKACQLEEDI------TKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 494860364 199 TSALDPISTL-VIEELINDLKNQFTVVIVTHNMQQaARVSDQTAFMYMGE 247
Cdd:cd03291 187 FGYLDVFTEKeIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
26-259 |
9.40e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKStllrcinrmndlvdicriEGEILLH------GQNIYD 99
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**------------------RGALPAHv*gpdaGRRPWR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 100 KSVDVA---ALRRNVGMvfQRPNPFPK----SIYENVVY---GLRLQGIKEKRKLDEVVEQ-SLRGAAlwdevkdrlHDS 168
Cdd:NF000106 73 F*TWCAnrrALRRTIG*--HRPVR*GRresfSGRENLYMigr*LDLSRKDARARADELLERfSLTEAA---------GRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 169 AFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDP-ISTLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYMGE 247
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPrTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
250
....*....|..
gi 494860364 248 LIEYSDTNTLFT 259
Cdd:NF000106 222 VIADGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
43-240 |
1.73e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrMNDLVDI---CRIEGEILLHGQ-----NIYDKSvdvaalRRNVGMV 114
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTL------MKVLSGVyphGSYEGEILFDGEvcrfkDIRDSE------ALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 FQRPNPFPK-SIYENVVYGlrlqgikekrkldevVEQSLRGAALWDEVKDR---------LHDSAFGLSG----GQQQRL 180
Cdd:NF040905 84 HQELALIPYlSIAENIFLG---------------NERAKRGVIDWNETNRRarellakvgLDESPDTLVTdigvGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 181 VIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQT 240
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-228 |
1.80e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEIllhgqniydksvdVAALRRNVGMVFQ 116
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----DFNGEA-------------RPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFP-KSIYENVVYGLRlqgiKEKRKLDEVVEQSLRGA-------ALWDE---VKDRLhDSAFG-------------- 171
Cdd:TIGR03719 76 EPQLDPtKTVRENVEEGVA----EIKDALDRFNEISAKYAepdadfdKLAAEqaeLQEII-DAADAwdldsqleiamdal 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 172 -----------LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNqfTVVIVTH 228
Cdd:TIGR03719 151 rcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
60-259 |
2.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 60 IGPSGCGKSTLLrcinrmNDLVDICRIE-GEILLHGQNIydKSVDVAALRRNVGMVFQRPNPFPKSIYENvvyglrlqgi 138
Cdd:PLN03130 1271 VGRTGAGKSSML------NALFRIVELErGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSGTVRFN---------- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 139 kekrkLDEVVEQSlrGAALWD-----EVKDRLHDSAFGL-----------SGGQQQRLVIARSIAIEPEVLLLDEPTSAL 202
Cdd:PLN03130 1333 -----LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 494860364 203 DPISTLVIEELINDLKNQFTVVIVTHNMQQAARvSDQTAFMYMGELIEYSDTNTLFT 259
Cdd:PLN03130 1406 DVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
43-238 |
2.40e-08 |
|
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: 52.33 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 43 ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinrmndlvDICRIEGEILLHG---QNIYDKSVDVAALRR--NVGMVFQR 117
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISflpKFSRNKLIFIDQLQFliDVGLGYLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 PNpfpksiyenvvyglrlqgikekRKLDEvveqslrgaalwdevkdrlhdsafgLSGGQQQRLVIARSIAIEPE--VLLL 195
Cdd:cd03238 81 LG----------------------QKLST-------------------------LSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 494860364 196 DEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHN---MQQAARVSD 238
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLgNTVILIEHNldvLSSADWIID 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
171-248 |
2.55e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 2.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 171 GLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQFTVVI-VTHNMQQAARVSDQTAFMYMGEL 248
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
172-248 |
4.73e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 4.73e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-255 |
7.76e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 7 KVNQANIGQKLDLENLTDDQkaleIKDLDLYYGDKQ---ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdi 83
Cdd:PRK13545 4 KVKFEHVTKKYKMYNKPFDK----LKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 84 crieGEILLHGQNIYDKSVDVAALRRNVGMVFQRpnpfpkSIYENVVYGLRLQGIKeKRKLDEVVEQSLRGAalwdEVKD 163
Cdd:PRK13545 71 ----AGVTMPNKGTVDIKGSAALIAISSGLNGQL------TGIENIELKGLMMGLT-KEKIKEIIPEIIEFA----DIGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 164 RLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAF 242
Cdd:PRK13545 136 FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALW 215
|
250
....*....|...
gi 494860364 243 MYMGELIEYSDTN 255
Cdd:PRK13545 216 LHYGQVKEYGDIK 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
54-220 |
9.89e-08 |
|
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: 51.11 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 54 GQVTAFIGPSGCGKSTLLRCINrmNDLVDICRIEGEILLHGqniYDKSVDVAALRRNVGMVFQRPNPFPK-SIYENVVYG 132
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNG---IPYKEFAEKYPGEIIYVSEEDVHFPTlTVRETLDFA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 133 LRLQGikekrklDEVVEqslrgaalwdevkdrlhdsafGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLvieE 212
Cdd:cd03233 108 LRCKG-------NEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL---E 156
|
....*...
gi 494860364 213 LINDLKNQ 220
Cdd:cd03233 157 ILKCIRTM 164
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-228 |
2.03e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 26 QKALEIKDLDLYYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMnDLVDicriEGEILLhGQniydkSVDVA 105
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ-EQPD----SGTIKI-GE-----TVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 106 AlrrnvgmVFQ-R----PNpfpKSIYENVVYGLRLqgIKEKRKldevveqslrgaalwdEVKDRLHDSAFG--------- 171
Cdd:PRK11819 391 Y-------VDQsRdaldPN---KTVWEEISGGLDI--IKVGNR----------------EIPSRAYVGRFNfkggdqqkk 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 172 ---LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDpISTL-VIEELINDlknqF--TVVIVTH 228
Cdd:PRK11819 443 vgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-VETLrALEEALLE----FpgCAVVISH 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
55-239 |
2.19e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 55 QVTafiGPSGCGKSTLLRCINRMNDlvdicRIEGEILLHGQNIydksvdvaalRRnvgmvfQRPNPFPKSIY-------- 126
Cdd:PRK13538 31 QIE---GPNGAGKTSLLRILAGLAR-----PDAGEVLWQGEPI----------RR------QRDEYHQDLLYlghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 127 ------ENVVYGLRLQGIKEkrklDEVVEQSLRGAALwdevKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTS 200
Cdd:PRK13538 87 teltalENLRFYQRLHGPGD----DEALWEALAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 494860364 201 ALDPISTLVIEELIND-LKNQFTVVIVTHnmQQAARVSDQ 239
Cdd:PRK13538 159 AIDKQGVARLEALLAQhAEQGGMVILTTH--QDLPVASDK 196
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
27-229 |
2.31e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 27 KALEIKDLDLYYGdkqalnKVNMNIPKGqVTAFIGPSGCGKSTLLRCI----------------NRMNDLVDICRIEGEi 90
Cdd:COG0419 3 LRLRLENFRSYRD------TETIDFDDG-LNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEASVELE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 91 LLHGQNIYdksvdvaALRRNVGMVFQRPNPFPKSIYENV--VYGL-RLQGIKEK-RKLDEVVEQSLRGAALWDEVKDRLH 166
Cdd:COG0419 75 FEHGGKRY-------RIERRQGEFAEFLEAKPSERKEALkrLLGLeIYEELKERlKELEEALESALEELAELQKLKQEIL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 167 DSAFG------LSGGQQQRLVIARSIAiepevLLLDepTSALDPISTLVIEELINDLKnqftvvIVTHN 229
Cdd:COG0419 148 AQLSGldpietLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA------IITHV 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
42-228 |
2.62e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 42 QALNKVNMNIPKGQVTAFIGPSGCGKSTLlrcinrMNDLVDicR-----IEGEILLHGqniYDKSVDVAAlrRNVGMVFQ 116
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTL------MDVLAG--RktggyIEGDIRISG---FPKKQETFA--RISGYCEQ 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RPNPFPK-SIYENVVYGLRLQGIKEKRKLDEV--VEQSLRGAALwdevkDRLHDSAFGLSG------GQQQRLVIARSIA 187
Cdd:PLN03140 961 NDIHSPQvTVRESLIYSAFLRLPKEVSKEEKMmfVDEVMELVEL-----DNLKDAIVGLPGvtglstEQRKRLTIAVELV 1035
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 494860364 188 IEPEVLLLDEPTSALDP-ISTLVIEELINDLKNQFTVVIVTH 228
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDArAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-250 |
2.82e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 24 DDQKALEIKDLDLYYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDicrieGEILLHGQNIYDKsv 102
Cdd:PRK10522 318 PDWQTLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-----GEILLDGKPVTAE-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 103 DVAALRRNVGMVFQRPNPFPksiyenvvyglRLQGIKEKRKLDEVVEQSLRGAALWDEVkdRLHD---SAFGLSGGQQQR 179
Cdd:PRK10522 391 QPEDYRKLFSAVFTDFHLFD-----------QLLGPEGKPANPALVEKWLERLKMAHKL--ELEDgriSNLKLSKGQKKR 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 180 LVIARSIAIEPEVLLLDEPTSALDPISTLVI-EELINDLKNQ-FTVVIVTHN---MQQAARVSDqtafMYMGELIE 250
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMgKTIFAISHDdhyFIHADRLLE----MRNGQLSE 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
47-248 |
4.37e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 47 VNMNIPKGQVTAFIGPSGCGKSTLLRCI---NRmndlvdicRIEGEILLHGQNIYDKSVDVA-----AL----RRNVGMV 114
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTR--------RTAGQVYLDGKPIDIRSPRDAiragiMLcpedRKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 115 FQRpnpfpkSIYENV---------VYGLRLQGIKEKRKLDEVVeQSLRgaalwdeVKDRLHDSAFG-LSGGQQQRLVIAR 184
Cdd:PRK11288 344 PVH------SVADNInisarrhhlRAGCLINNRWEAENADRFI-RSLN-------IKTPSREQLIMnLSGGNQQKAILGR 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494860364 185 SIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQAARVSDQTAFMYMGEL 248
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
173-228 |
5.91e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELIndLKNQFTVVIVTH 228
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-246 |
7.89e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 14 GQKLDLENLTDDQKaleikdldLYYGDKQ-ALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILL 92
Cdd:TIGR01257 1932 GNKTDILRLNELTK--------VYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATV 1998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 93 HGQNIYDKSVDVaalRRNVGMVfqrpnPFPKSI------YENVVYGLRLQGIKEKrKLDEVVEQSLRGAALwDEVKDRLh 166
Cdd:TIGR01257 1999 AGKSILTNISDV---HQNMGYC-----PQFDAIddlltgREHLYLYARLRGVPAE-EIEKVANWSIQSLGL-SLYADRL- 2067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 167 dsAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPIS-TLVIEELINDLKNQFTVVIVTHNMQQAARVSDQTAFMYM 245
Cdd:TIGR01257 2068 --AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
.
gi 494860364 246 G 246
Cdd:TIGR01257 2146 G 2146
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
56-228 |
1.22e-06 |
|
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: 47.99 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 56 VTAFIGPSGCGKSTLLRCI------------NRMNDLVDICRI---EGEILLHGQNIYDKSVDVaalRRNVgmvfqrpnp 120
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyaltgelppnsKGGAHDPKLIREgevRAQVKLAFENANGKKYTI---TRSL--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 fpkSIYENVVYglrlqgikekrkldevVEQslrgaalwDEVKDRLHDSAFGLSGGQQQ------RLVIARSIAIEPEVLL 194
Cdd:cd03240 92 ---AILENVIF----------------CHQ--------GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 494860364 195 LDEPTSALDPIS-TLVIEELINDLKNQ--FTVVIVTH 228
Cdd:cd03240 145 LDEPTTNLDEENiEESLAEIIEERKSQknFQLIVITH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
53-229 |
1.51e-06 |
|
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: 46.98 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 53 KGQVTAFIGPSGCGKSTLLRCINRMndlvdicriegeillhgqniydksvdvaaLRRNVGMVFqrpnpfpksiyenvvyg 132
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-----------------------------LGPPGGGVI----------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 133 lrlqgikekrkldEVVEQSLRGAALWDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEE 212
Cdd:smart00382 35 -------------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180
....*....|....*....|....
gi 494860364 213 LI-------NDLKNQFTVVIVTHN 229
Cdd:smart00382 102 LEelrllllLKSEKNLTVILTTND 125
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-228 |
2.12e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 37 YYGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDlvdicRIEGEIllhgqniydksvdVAALRRNVGMVFQ 116
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----EFEGEA-------------RPAPGIKVGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 117 RP--NPfPKSIYENVVYGLrlQGIKEK-RKLDEV--------------------VEQSLRGAALWD-----EVK-DRLH- 166
Cdd:PRK11819 78 EPqlDP-EKTVRENVEEGV--AEVKAAlDRFNEIyaayaepdadfdalaaeqgeLQEIIDAADAWDldsqlEIAmDALRc 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 167 ---DSAFG-LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDLKNqfTVVIVTH 228
Cdd:PRK11819 155 ppwDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG--TVVAVTH 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-203 |
1.12e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 38 YGDKQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRmndlvDICRIEGEILLhgqniyDKSVDVAALRRNvGMVFQR 117
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----ELAPVSGEIGL------AKGIKLGYFAQH-QLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 118 PNPFPksiyenvvyglrLQGIKekRKLDEVVEQSLRgaalwDEVK------DRLHDSAFGLSGGQQQRLVIARSIAIEPE 191
Cdd:PRK10636 390 ADESP------------LQHLA--RLAPQELEQKLR-----DYLGgfgfqgDKVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170
....*....|..
gi 494860364 192 VLLLDEPTSALD 203
Cdd:PRK10636 451 LLLLDEPTNHLD 462
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
44-230 |
1.55e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLL-----RCINRMNDLVDIC-----RIEGEillhgQNIyDKSVDV--AALRRNv 111
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdRIEGL-----EHI-DKVIVIdqSPIGRT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 112 gmvfQRPNPfpkSIYENVVYGLR---LQGIKEKRKLDEVVEQSLRGAALWD-----------------EVKDRLH----- 166
Cdd:cd03271 84 ----PRSNP---ATYTGVFDEIRelfCEVCKGKRYNRETLEVRYKGKSIADvldmtveealeffenipKIARKLQtlcdv 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494860364 167 --------DSAFGLSGGQQQRLVIARSI---AIEPEVLLLDEPTSAL--DPISTL--VIEELInDLKNqfTVVIVTHNM 230
Cdd:cd03271 157 glgyiklgQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLhfHDVKKLleVLQRLV-DKGN--TVVVIEHNL 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
170-235 |
1.87e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 170 FGLSGGQQQRLVIARSIAIE---PEVL-LLDEPTSALDPISTLVIEELIND-LKNQFTVVIVTHNMQQAAR 235
Cdd:cd03227 76 LQLSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL 146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
172-238 |
2.21e-05 |
|
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: 44.71 E-value: 2.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494860364 172 LSGGQQQRLVIARSIAIEPEVLLLDEPTSALDP----ISTLVIEELIndLKNQFTVVIVTHNMQQAARVSD 238
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFA--ENNEKTAFVVEHDIIMIDYLAD 184
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-271 |
3.86e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 41 KQALNKVNMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVDIcRIEGEILLHGqniYDKSVDVAALRRNVGMVFQRPNP 120
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHI-GVEGVITYDG---ITPEEIKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 121 FPK-SIYENVVYGLRLQ-------GIKEKRKLDEVVEQSLRGAALwDEVKDRL--HDSAFGLSGGQQQRLVIARSIAIEP 190
Cdd:TIGR00956 150 FPHlTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGL-SHTRNTKvgNDFVRGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 191 EVLLLDEPTSALDPISTLvieELINDLKNQFTVVIVTHNM------QQAARVSDQTAFMYMGELIEYSDTN---TLFTT- 260
Cdd:TIGR00956 229 KIQCWDNATRGLDSATAL---EFIRALKTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQIYFGPADkakQYFEKm 305
|
250
....*....|....*
gi 494860364 261 ----PTKKKTEDYIT 271
Cdd:TIGR00956 306 gfkcPDRQTTADFLT 320
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
44-238 |
4.74e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRcinrmndlvdicrieGEILLHGQNIYDKSVDVAAlRRNVGMVfQRP----- 118
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAF---------------DTIYAEGQRRYVESLSAYA-RQFLGQM-DKPdvdsi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 --------------NPFPKS-------IYENvvygLRL----QGIKEK-RKLDEVVEQSLRgaalwdevkdrLHDSAFGL 172
Cdd:cd03270 74 eglspaiaidqkttSRNPRStvgtvteIYDY----LRLlfarVGIRERlGFLVDVGLGYLT-----------LSRSAPTL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494860364 173 SGGQQQRLVIARSIAIEPEVLL--LDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHN---MQQAARVSD 238
Cdd:cd03270 139 SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDedtIRAADHVID 210
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
84-229 |
6.11e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 84 CRIEGEILLHGQNIYDKSVDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGIKEKRKLDEVVEQSLRGAaLWDEVKD 163
Cdd:pfam13304 150 PLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGL-ILLENGG 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 164 RLHDSAFGLSGGQQQ--RLVIA-RSIAIEPEVLLLDEPTSALDP-ISTLVIEELINDLKNQFTVVIVTHN 229
Cdd:pfam13304 229 GGELPAFELSDGTKRllALLAAlLSALPKGGLLLIDEPESGLHPkLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
58-229 |
7.28e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 58 AFIGPSGCGKSTLLRCINrmndlvdicrieGEillhgqniydksvdvaaLRRNVGMVFQRPNPFPKSIYENVVYGLRLQG 137
Cdd:PLN03073 539 AMVGPNGIGKSTILKLIS------------GE-----------------LQPSSGTVFRSAKVRMAVFSQHHVDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 138 ---IKEKRKLDEVVEQSLRGaalwdevkdrlHDSAFG------------LSGGQQQRLVIARSIAIEPEVLLLDEPTSAL 202
Cdd:PLN03073 590 nplLYMMRCFPGVPEQKLRA-----------HLGSFGvtgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180
....*....|....*....|....*...
gi 494860364 203 DPIStlvIEELINDLK-NQFTVVIVTHN 229
Cdd:PLN03073 659 DLDA---VEALIQGLVlFQGGVLMVSHD 683
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-230 |
7.61e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.85 E-value: 7.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 164 RLHDSAFGLSGGQQQRLVIARSI---AIEPEVLLLDEPTSAL--DPISTL--VIEELInDLKNqfTVVIVTHNM 230
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfDDIKKLleVLQRLV-DKGN--TVVVIEHNL 892
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
158-244 |
8.11e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.17 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 158 WDEVKDRLHDSAFGLSGGQQQRLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELINDL--KNQFTVVIVTHNMQQAAR 235
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDY 137
|
....*....
gi 494860364 236 VSDQTAFMY 244
Cdd:cd03222 138 LSDRIHVFE 146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
51-203 |
1.50e-04 |
|
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: 42.85 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 51 IPKGQVTAFIGPSGCGKSTLLRCIN--------RMNDLVDIC----RIEGEillhgqniYDKSVDvAALRRNVGmvfqrp 118
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAgvlkpdegEVDEDLKISykpqYISPD--------YDGTVE-EFLRSANT------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 119 NPFPKSIYEN-VVYGLRLQGIKEKrkldevveqslrgaalwdEVKDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDE 197
Cdd:COG1245 428 DDFGSSYYKTeIIKPLGLEKLLDK------------------NVKD--------LSGGELQRVAIAACLSRDADLYLLDE 481
|
....*.
gi 494860364 198 PTSALD 203
Cdd:COG1245 482 PSAHLD 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
51-203 |
4.35e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 51 IPKGQVTAFIGPSGCGKSTLLRCinrmndLV-DICRIEGEILLHGQNIY-------DKSVDVAALRRNVgmvfqrPNPFP 122
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKL------LAgVLKPDEGEVDPELKISYkpqyikpDYDGTVEDLLRSI------TDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 123 KSIYEN-VVYGLRLQGIKEKrkldevveqslrgaalwdEVKDrlhdsafgLSGGQQQRLVIARSIAIEPEVLLLDEPTSA 201
Cdd:PRK13409 430 SSYYKSeIIKPLQLERLLDK------------------NVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
..
gi 494860364 202 LD 203
Cdd:PRK13409 484 LD 485
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
44-258 |
8.42e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 44 LNKVNMNIPKGQVTAFIGPSGCGKSTLLRCInrmndlvdicriEGEILLHGQNIydksvdvaALRRNVGM--VFQRPNPF 121
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL------------KNEISADGGSY--------TFPGNWQLawVNQETPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 122 PKSIYENVVYGLR--------LQGIKEKR----------KLDEVVEQSL--RGAALWDEV---KDRLHDSAFGLSGGQQQ 178
Cdd:PRK10636 77 PQPALEYVIDGDReyrqleaqLHDANERNdghaiatihgKLDAIDAWTIrsRAASLLHGLgfsNEQLERPVSDFSGGWRM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDPISTLVIEELindLKN-QFTVVIVTHNMQQAARVSDQTAFMYMGELIEYSDTNTL 257
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW---LKSyQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSS 233
|
.
gi 494860364 258 F 258
Cdd:PRK10636 234 F 234
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
172-238 |
9.33e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 9.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494860364 172 LSGGQQQRLVIARSIAIEPE--VLLLDEPTSALDPISTLVIEELINDLKNQ-FTVVIVTHNMQQ---AARVSD 238
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIID 549
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
5-92 |
1.13e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 40.49 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494860364 5 APKVNQANIGQKLDLENLTDD--QKALEIKDLDLYYGDkqalnkvnmnIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVD 82
Cdd:COG5192 28 AKAFAVAAIGQMARQAMRTADieEKKLHVPMVDRTPKD----------LPPPFIVAVVGPPGTGKSTLIRSLVRRFTKQT 97
|
90
....*....|
gi 494860364 83 ICRIEGEILL 92
Cdd:COG5192 98 IDEIRGPITV 107
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
53-71 |
1.65e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.65e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
172-238 |
1.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494860364 172 LSGGQQQRLVIARSI---AIEPEVLLLDEPTSALdpiSTLVIEELIN---DLKNQ-FTVVIVTHNMqQAARVSD 238
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYvlqSLTHQgHTVVIIEHNM-HVVKVAD 879
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
51-74 |
1.91e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 39.11 E-value: 1.91e-03
10 20
....*....|....*....|....
gi 494860364 51 IPKGQVTAFIGPSGCGKSTLLRCI 74
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQL 33
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
179-228 |
2.80e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 494860364 179 RLVIARSIAIEPEVLLLDEPTSALDpISTLV-IEELINDLKNqfTVVIVTH 228
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INTIRwLEDVLNERNS--TMIIISH 210
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
53-71 |
3.17e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 3.17e-03
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
53-71 |
3.96e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.88 E-value: 3.96e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
172-230 |
7.25e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 7.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494860364 172 LSGGQQQRLVIAR---SIAIEPEVLLLDEPTSAL--DPISTL--VIEELInDLKNqfTVVIVTHNM 230
Cdd:COG0178 827 LSGGEAQRVKLASelsKRSTGKTLYILDEPTTGLhfHDIRKLleVLHRLV-DKGN--TVVVIEHNL 889
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
48-82 |
9.82e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 36.83 E-value: 9.82e-03
10 20 30
....*....|....*....|....*....|....*
gi 494860364 48 NMNIPKGQVTAFIGPSGCGKSTLLRCINRMNDLVD 82
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFLSDAAR 49
|
|
| |
