|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-252 |
0e+00 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 543.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTD 80
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIA 160
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKR 240
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
250
....*....|..
gi 489083979 241 KETEDYISGKFG 252
Cdd:PRK14239 241 KETEDYISGKFG 252
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-252 |
1.68e-179 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 493.01 E-value: 1.68e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDT 81
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIAR 161
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRK 241
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
250
....*....|.
gi 489083979 242 ETEDYISGKFG 252
Cdd:COG1117 248 RTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-251 |
6.37e-160 |
|
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: 443.27 E-value: 6.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDL 84
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVLA 164
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETE 244
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 489083979 245 DYISGKF 251
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-232 |
1.25e-126 |
|
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: 358.03 E-value: 1.25e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHdsAVGLSGGQQQRVCIARVLAT 165
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 166 SPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTK 232
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-252 |
3.24e-113 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 325.58 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDT 81
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIrdKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIAR 161
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFF---------LEGDLLECGPTK 232
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250 260
....*....|....*....|
gi 489083979 233 AMFMNPKRKETEDYISGKFG 252
Cdd:PRK14243 245 KIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
1.04e-94 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 278.26 E-value: 1.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKG-IRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKET 243
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 489083979 244 EDYISGKFG 252
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-252 |
1.80e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 273.07 E-value: 1.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVD 83
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLSDRTGFFLE-----GDLLECGPTKAMFM 236
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|....*.
gi 489083979 237 NPKRKETEDYISGKFG 252
Cdd:PRK14258 246 SPHDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-250 |
3.49e-85 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 254.07 E-value: 3.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYspRTDTVDLR 85
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGI-RDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK14247 82 RRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKET 243
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*..
gi 489083979 244 EDYISGK 250
Cdd:PRK14247 242 EKYVTGR 248
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-250 |
5.78e-73 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 223.39 E-value: 5.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSIVYNGHNIYspRTDT 81
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYFGKDIF--QIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIA 160
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKR 240
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
250
....*....|
gi 489083979 241 KETEDYISGK 250
Cdd:PRK14246 246 ELTEKYVIGR 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-248 |
2.65e-72 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 220.64 E-value: 2.65e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIVYNGHNIYSPRTDTVD 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL------EEPDsGTITVDGEDLTDSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLR-LKGIRDKSILDHAVEsSLK--GasiwneVKDRLHDSAVGLSGGQQQRVCI 159
Cdd:COG1126 75 LRRKVGMVFQQFNLFPhLTVLENVTLAPIkVKKMSKAEAEERAME-LLErvG------LADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
250
....*....|
gi 489083979 239 KRKETEDYIS 248
Cdd:COG1126 228 QHERTRAFLS 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-252 |
3.77e-72 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 221.89 E-value: 3.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRtDTVD 83
Cdd:PRK14271 20 PAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKET 243
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
....*....
gi 489083979 244 EDYISGKFG 252
Cdd:PRK14271 259 ARYVAGLSG 267
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
3.14e-61 |
|
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: 200.51 E-value: 3.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKT-----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIY 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKggvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL--LRPT---SGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 76 S-PRTDTVDLRKEIGMVFQQP----NPFpMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRL-HDsavgL 149
Cdd:COG1123 331 KlSRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHE----L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLE 227
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYlfISHDLAVVRYIADRVAVMYDGRIVE 485
|
250
....*....|..
gi 489083979 228 CGPTKAMFMNPK 239
Cdd:COG1123 486 DGPTEEVFANPQ 497
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
1.49e-59 |
|
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: 187.35 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDLR 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLR-LKGIRDKSILDHAvESSLKGASIwnevKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIkVKGMSKAEAEERA-LELLEKVGL----ADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-223 |
3.01e-57 |
|
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: 180.46 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDLR 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-----EEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYglrlkgirdksildhavesslkgasiwnevkdrlhdsavGLSGGQQQRVCIARVLA 164
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIAL---------------------------------------GLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKD--YTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
5.48e-57 |
|
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: 181.72 E-value: 5.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PRT 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPD---SGEILVDGQDITGlSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIRDKSILDHAVESSLKgasiwnevkdrlhdsAVGL--------- 149
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLE---------------LVGLpgaadkmps 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 150 --SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDL 225
Cdd:COG1127 141 elSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
250
....*....|
gi 489083979 226 LECGPTKAMF 235
Cdd:COG1127 221 IAEGTPEELL 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-229 |
9.22e-55 |
|
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: 175.77 E-value: 9.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PRT 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKlSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQP----NPFpMSIYENVVYGLRLKGIRDK-SILDHAVESSLKGASIWNEVKDRL-HDsavgLSGGQ 153
Cdd:cd03257 76 LRKIRRKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKkEARKEAVLLLLVGVGLPEEVLNRYpHE----LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLlfITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-240 |
9.48e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 175.60 E-value: 9.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYspRTDTVDL 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDIT--KKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQqpNP----FPMSIYENVVYGLRLKGIrDKSILDHAVESSLK--GASiwnEVKDR-LHDsavgLSGGQQQRV 157
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALElvGLE---HLADRpPHE----LSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFM 236
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKrLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
....
gi 489083979 237 NPKR 240
Cdd:COG1122 224 DYEL 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-235 |
1.92e-54 |
|
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: 175.00 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEVtitGSIVYNGHNIYS-PRTDTVDL 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPDS---GEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIRDKSILDHAVESSLkgasiwnevkdrlhdSAVGL-----------SGG 152
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKL---------------EAVGLrgaedlypaelSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGP 230
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
....*
gi 489083979 231 TKAMF 235
Cdd:cd03261 221 PEELR 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-240 |
4.52e-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: 178.94 E-value: 4.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEVTITGSIVYNGHNIyspRTD 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDL---LEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLR-KEIGMVFQQP--NPFPMSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIWNEVKDRLHDsavgLSGGQQQRV 157
Cdd:COG1123 77 SEALRgRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLEL-LEAVGLERRLDRYPHQ----LSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLECGPTKAMF 235
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVllITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
....*
gi 489083979 236 MNPKR 240
Cdd:COG1123 232 AAPQA 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-229 |
6.48e-53 |
|
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: 170.39 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLR 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIwnevKDRLHDSAVGLSGGQQQRVCIARVLA 164
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRGVPKAEI-RARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELkeLQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-235 |
1.14e-52 |
|
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: 170.99 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRtdtv 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKPS---SGEVLLDGRDLasLSRR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPN-PFPMSIYENVVYGLR--LKGIRDKSILDH-AVESSLKGASIWnEVKDRLHDSavgLSGGQQQRVC 158
Cdd:COG1120 72 ELARRIAYVPQEPPaPFGLTVRELVALGRYphLGLFGRPSAEDReAVEEALERTGLE-HLADRPVDE---LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 159 IARVLATSPRIILLDEPTSALDPisaGKIEETLLLLKK-----DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKA 233
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDL---AHQLEVLELLRRlarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 489083979 234 MF 235
Cdd:COG1120 225 VL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-217 |
1.50e-52 |
|
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: 169.59 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIY--SPRT 79
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVRVDGTDISklSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAvESSLKGASIwnevKDRLHDSAVGLSGGQQQRVC 158
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPLLLAGVPKKERRERA-EELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRlSDRT 217
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEY-ADRI 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
1.53e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.23 E-value: 1.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdtvD 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLsaMPPP----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIR-DKSILDHAVESSLKGASIwnevkdrLHDSAVGLSGGQQQRVCIARV 162
Cdd:COG4619 72 WRRQVAYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDI-------LDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLSDRT 217
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLreYLAEEGRAVLWVSHDPEQIERVADRV 201
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-223 |
2.49e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.45 E-value: 2.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-P 77
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL--DRPT---SGEVLIDGQDISSlS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTDTVDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVE--SSLkgasiwnEVKDRLHDSAVGLSGGQ 153
Cdd:COG1136 77 ERELARLRrRHIGFVFQFFNLLPeLTALENVALPLLLAGVSRKERRERAREllERV-------GLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRlSDRTGFFLEG 223
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDG 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-239 |
7.16e-52 |
|
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: 168.83 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmndLNPEVTitGSIVYNGHNIYSPRTdt 81
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG---LERPWS--GEVTFDGRPVTRRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQP----NPFpMSIYENVVYGLRLKGIRDKsilDHAVESSLKGASIWNEVKDRL-HDsavgLSGGQQQR 156
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTylFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
....*
gi 489083979 235 FMNPK 239
Cdd:COG1124 227 LAGPK 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-239 |
1.80e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 171.05 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTD 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-----SGRILLDGRDV----TG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVESSLkgasiwnevkDRLHDSAVG------LSGGQ 153
Cdd:COG3842 72 LPPEKRNVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELL----------ELVGLEGLAdryphqLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPisagKI-EETLLLLKK-----DYTLAIVTRSMQQASRLSDRTGFFLEGDLLE 227
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDA----KLrEEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQ 216
|
250
....*....|..
gi 489083979 228 CGPTKAMFMNPK 239
Cdd:COG3842 217 VGTPEEIYERPA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
4.16e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 167.19 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmnDLNPEVTitGSIVYNGHNIYS 76
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKPTS--GEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 PRTDtvdlrkeIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKsildhavesslkgasiwnEVKDRLHD--SAVGL---- 149
Cdd:COG1116 78 PGPD-------RGVVFQEPALLPwLTVLDNVALGLELRGVPKA------------------ERRERAREllELVGLagfe 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 150 -------SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLL--LLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:COG1116 133 dayphqlSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLrlWQETGKTVLFVTHDVDEAVFLADR 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-216 |
7.96e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.39 E-value: 7.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSV-YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTV 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 -DLRKEIGMVFQQPNPFP-MSIYENVVYGL--RLKGIRdksildhavesSLKGaSIWNEVKDRLHD--SAVG-------- 148
Cdd:COG3638 76 rRLRRRIGMIFQQFNLVPrLSVLTNVLAGRlgRTSTWR-----------SLLG-LFPPEDRERALEalERVGladkayqr 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 149 ---LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDR 216
Cdd:COG3638 144 adqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADR 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-238 |
2.59e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.88 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIRDKSILDHAVESSLK-GASiwnevkDRLHDSAVGLSGGQQQRVCIAR 161
Cdd:PRK09493 76 RQEAGMVFQQFYLFPhLTALENVMFGpLRVRGASKEEAEKQARELLAKvGLA------ERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 162 VLATSPRIILLDEPTSALDPisagKIEETLLLLKKD-----YTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFM 236
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDP----ELRHEVLKVMQDlaeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
..
gi 489083979 237 NP 238
Cdd:PRK09493 226 NP 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-216 |
2.82e-50 |
|
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: 163.80 E-value: 2.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDt 81
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL--ERPT---SGEVLVDGEPVTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 vdlrkeIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVES----SLKGASiwnevKDRLHDsavgLSGGQQQR 156
Cdd:cd03293 75 ------RGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELlelvGLSGFE-----NAYPHQ----LSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDR 216
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVllVTHDIDEAVFLADR 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-223 |
4.34e-49 |
|
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: 160.71 E-value: 4.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYN--QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSprTDTVDL 84
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGP---TSGEVLVDGKDLTK--LSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIrDKSILDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARV 162
Cdd:cd03225 74 RRKVGLVFQNPDDqfFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEGLRDRSPFT----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-234 |
9.73e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 9.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDTVDLR 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML--LGLLRPT---SGEVRVLGEDV---ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVESSLKGASIWnevkDRLHDSAVGLSGGQQQRVCIARVLA 164
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-239 |
1.11e-48 |
|
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: 162.92 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYS-PRT 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGvvkaVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLLKlSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLR-KEIGMVFQQP----NPFpMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIwNEVKDRLHDSAVGLSGGQQ 154
Cdd:COG0444 79 ELRKIRgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSMQQASRLSDRTGFFLEGDLLECGPTK 232
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILfiTHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*..
gi 489083979 233 AMFMNPK 239
Cdd:COG0444 237 ELFENPR 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-177 |
1.20e-48 |
|
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: 157.42 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFP- 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSP---TEGTILLDGQDLTDDERK--SLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 100 MSIYENVVYGLRLKGIRDKSILDHAvESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTS 177
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
2.88e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.79 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPrtd 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI--LGLLPP---TSGTVRLFGKPPRRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 tvdlRKEIGMVFQQPN---PFPMSIYENVVYGL-------RLKGIRDKSILDHAVE----SSLKGASIWNevkdrlhdsa 146
Cdd:COG1121 74 ----RRRIGYVPQRAEvdwDFPITVRDVVLMGRygrrglfRRPSRADREAVDEALErvglEDLADRPIGE---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 147 vgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKK-DYTLAIVTRSMQQASRLSDRTgFFLEGDL 225
Cdd:COG1121 140 --LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRV-LLLNRGL 216
|
250 260
....*....|....*....|....*..
gi 489083979 226 LECGPTKAMFmnpkrkeTEDYISGKFG 252
Cdd:COG1121 217 VAHGPPEEVL-------TPENLSRAYG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-216 |
3.93e-47 |
|
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: 154.08 E-value: 3.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPrtDTVD 83
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PT---SGEILIDGVDLRDL--DLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVvyglrlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARVL 163
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQAsRLSDR 216
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADR 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-238 |
1.68e-46 |
|
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: 155.15 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYspRTDTVDL 84
Cdd:cd03295 1 IEFENVTkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--IEPT---SGEIFIDGEDIR--EQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASIwNEVKDRLHDSavgLSGGQQQRVCIARV 162
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELlALVGLDP-AEFADRYPHE---LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-249 |
7.85e-46 |
|
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: 153.95 E-value: 7.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PRTDTVDLR-KEIGMVFQQPNPF 98
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL--IEPT---SGKVLIDGQDIAAmSRKELRELRrKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 99 P-MSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASIWnevKDRLHDSavgLSGGQQQRVCIARVLATSPRIILLDEPT 176
Cdd:cd03294 115 PhRTVLENVAFGLEVQGVPRAEREERAAEAlELVGLEGW---EHKYPDE---LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 177 SALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETEDYISG 249
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-248 |
1.72e-45 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.24 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSPR 78
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ERPTSGSVLVDGVDLtaLSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 tDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKG-----IRDK--SILDhavessLKGASiwnevkDRLHDSAVGLS 150
Cdd:COG1135 76 -ELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGvpkaeIRKRvaELLE------LVGLS------DKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIeetLLLLK---KDYTLAIV--TRSMQQASRLSDRTGfFLE-GD 224
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI---LDLLKdinRELGLTIVliTHEMDVVRRICDRVA-VLEnGR 218
|
250 260
....*....|....*....|....
gi 489083979 225 LLECGPTKAMFMNPKRKETEDYIS 248
Cdd:COG1135 219 IVEQGPVLDVFANPQSELTRRFLP 242
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-204 |
5.24e-45 |
|
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: 160.38 E-value: 5.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRtdt 81
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL--YEPT---SGRILIDGIDLrqIDPA--- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 vDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKD-------RLHDSAVGLSGGQQ 154
Cdd:COG2274 546 -SLRRQIGVVLQDVFLFSGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQR 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA 667
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-239 |
6.48e-45 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 152.55 E-value: 6.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKT-LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIVYNGHNIYSprTDTVDL 84
Cdd:COG1125 3 EFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL------IEPTsGRILIDGEDIRD--LDPVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKG-----IRDKSI-------LDHAvesslkgasiwnEVKDRL-HDsavgLS 150
Cdd:COG1125 75 RRRIGYVIQQIGLFPhMTVAENIATVPRLLGwdkerIRARVDellelvgLDPE------------EYRDRYpHE----LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLEC 228
Cdd:COG1125 139 GGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQY 218
|
250
....*....|.
gi 489083979 229 GPTKAMFMNPK 239
Cdd:COG1125 219 DTPEEILANPA 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-216 |
1.33e-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: 150.03 E-value: 1.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIVYNGHNIYS-PRTDTV 82
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL------VEPTsGSVLIDGTDINKlKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGlRLkgirdksildhAVESSLKGASIWNEVKDRLHDSA----VG--------- 148
Cdd:cd03256 75 QLRRQIGMIFQQFNLIErLSVLENVLSG-RL-----------GRRSTWRSLFGLFPKEEKQRALAalerVGlldkayqra 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 149 --LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL--KKDYTLAIVTRSMQQASRLSDR 216
Cdd:cd03256 143 dqLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-251 |
1.90e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 149.90 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTV-DL 84
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIRDKSILDHAVESSLK-GASIWNEVKDRLhdsavgLSGGQQQRVCIAR 161
Cdd:PRK11264 84 RQHVGFVFQNFNLFPhRTVLENIIEGpVIVKGEPKEEATARARELLAKvGLAGKETSYPRR------LSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKR 240
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
250
....*....|.
gi 489083979 241 KETEDYISgKF 251
Cdd:PRK11264 238 PRTRQFLE-KF 247
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-239 |
2.84e-44 |
|
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: 148.88 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRT 79
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGTDLTLlSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASiwnevkDRLHDSAVGLSGGQQQRV 157
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGVPKAEIEERVLELlELVGLE------DKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAgkiEETLLLLKK-----DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTK 232
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETT---QSILALLRDinrelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 489083979 233 AMFMNPK 239
Cdd:cd03258 227 EVFANPQ 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-240 |
4.08e-44 |
|
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: 149.91 E-value: 4.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYN-----QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PRT 79
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITAkKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSILDhAVESSLKGASIWNEVKDRlhdSAVGLSGGQQQRV 157
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEEEAEE-RVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPisAGKIE--ETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLECGPTKA 233
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDP--KGRKEilDLFKRLHKEKGLTVilVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
....*..
gi 489083979 234 MFMNPKR 240
Cdd:TIGR04521 230 VFSDVDE 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-214 |
6.66e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 6.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdtv 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-----SGRILIDGVDIrdLTLE---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVkDRLH---DSAVG-----LSGGQQ 154
Cdd:COG1132 411 SLRRQIGVVPQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFI-EALPdgyDTVVGergvnLSGGQR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI------AHRLS 536
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-223 |
6.88e-44 |
|
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: 145.47 E-value: 6.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLRK 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPT---SGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 87 EIGMVFQqpnpfpmsiyenvvyglrlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARVLATS 166
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 167 PRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLReLAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-216 |
1.53e-43 |
|
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: 147.31 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNiysPRTDTVDLR 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRML--AGLLKPD---SGSILIDGED---VRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWNEVKDRLHdsavGLSGGQQQRVCIARVLA 164
Cdd:COG4555 74 RQIGVLPDERGLYDrLTVRENIRYFAELYGLFDEEL-KKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV-TRSMQQASRLSDR 216
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFsSHIMQEVEALCDR 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-229 |
5.27e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.99 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ-KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDtvDL 84
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PY---SGSILINGVDLSDLDPA--SW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFPMSIYENvvygLRLkGIRDKSilDHAVESSLKGASIWNEVKD-------RLHDSAVGLSGGQQQRV 157
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIREN----LRL-GRPDAS--DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQAsRLSDRTgFFLE-GDLLECG 229
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRI-LVLDdGRIVEQG 553
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-187 |
2.00e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.65 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT-LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmnDLNPEvtiTGSIVYNGHNIYS-PRTDTV 82
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPT---SGQVLVNGQDLSRlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQ----PNpfpMSIYENVVYGLRLKGIRDKSIlDHAVESSLKgasiWNEVKDRLHDSAVGLSGGQQQRVC 158
Cdd:COG2884 76 YLRRRIGVVFQDfrllPD---RTVYENVALPLRVTGKSRKEI-RRRVREVLD----LVGLSDKAKALPHELSGGEQQRVA 147
|
170 180
....*....|....*....|....*....
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKI 187
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEI 176
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-232 |
2.94e-42 |
|
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: 143.41 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDTVD 83
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRPT---SGTAYINGYSI---RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRdKSILDHAVESSLKGASIwNEVKDRLhdsAVGLSGGQQQRVCIARV 162
Cdd:cd03263 73 ARQSLGYCPQFDALFDeLTVREHLRFYARLKGLP-KSEIKEEVELLLRVLGL-TDKANKR---ARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTK 232
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-239 |
9.29e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 145.67 E-value: 9.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI------NRmndlnpevtitGSIVYNGHNIY---S 76
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpDS-----------GRIVLNGRDLFtnlP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 PRTdtvdlRKeIGMVFQQPNPFP-MSIYENVVYGLRLKGiRDKSildhavesslkgasiwnEVKDRLHD--SAVG----- 148
Cdd:COG1118 72 PRE-----RR-VGFVFQHYALFPhMTVAENIAFGLRVRP-PSKA-----------------EIRARVEEllELVQlegla 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 149 ------LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFF 220
Cdd:COG1118 128 drypsqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVM 207
|
250
....*....|....*....
gi 489083979 221 LEGDLLECGPTKAMFMNPK 239
Cdd:COG1118 208 NQGRIEQVGTPDEVYDRPA 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-203 |
2.27e-41 |
|
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: 141.67 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPR-TDTV 82
Cdd:TIGR02315 1 MLEVENLSkVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDITKLRgKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGlRL---KGIRdkSILDHAVESSLKGA-SIWNEV--KDRLHDSAVGLSGGQQQ 155
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIErLTVLENVLHG-RLgykPTWR--SLLGRFSEEDKERAlSALERVglADKAYQRADQLSGGQQQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVI 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-222 |
3.83e-41 |
|
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: 140.65 E-value: 3.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDTVdLR 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MGLLPP---RSGSIRFDGRDITGLPPHER-AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRD-KSILDHAVEsslkgasIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:cd03224 75 AGIGYVPEGRRIFPeLTVEENLLLGAYARRRAKrKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRtGFFLE 222
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADR-AYVLE 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-219 |
7.10e-41 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.30 E-value: 7.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDTVDLR 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDI---KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYglrlkgirdksildhavesslkgasiwnevkdrlhdsavglSGGQQQRVCIARVLA 164
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENLKL-----------------------------------------SGGMKQRLALAQALL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV-TRSMQQASRLSDRTGF 219
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLsSHILEEAERLCDRVAI 167
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-249 |
7.71e-41 |
|
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: 143.84 E-value: 7.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 18 KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRTDTVDLRKEIGMVFQQP 95
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL--IEPT---AGQIFIDGENImkQSPVELREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 NPFP-MSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIwNEVKDRLHDSavgLSGGQQQRVCIARVLATSPRIILLDE 174
Cdd:TIGR01186 81 ALFPhMTILQNTSLGPELLGWPEQERKEKALEL-LKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 175 PTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETEDYISG 249
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
2.36e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 139.55 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTE---PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSP 77
Cdd:COG4598 1 MTDtapPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL-----ETPDSGEIRVGGEEIRLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTDT-----VD------LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIRDKSILDHAvESSLKGASIWnevkDRLHD 144
Cdd:COG4598 76 PDRDgelvpADrrqlqrIRTRLGMVFQSFNLWShMTVLENVIEApVHVLGRPKAEAIERA-EALLAKVGLA----DKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 145 SAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGkieETLLLLKKdytLA-------IVTRSMQQASRLSDRT 217
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVG---EVLKVMRD---LAeegrtmlVVTHEMGFARDVSSHV 224
|
250 260
....*....|....*....|..
gi 489083979 218 GFFLEGDLLECGPTKAMFMNPK 239
Cdd:COG4598 225 VFLHQGRIEEQGPPAEVFGNPK 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-204 |
1.11e-39 |
|
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: 144.14 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRT 79
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF--LDPQ---SGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DtvDLRKEIGMVFQQPNPFPMSIYENvvygLRLkGIRDKSilDHAVESSLKGASIWNEVKD-------RLHDSAVGLSGG 152
Cdd:COG4987 405 D--DLRRRIAVVPQRPHLFDTTLREN----LRL-ARPDAT--DEELWAALERVGLGDWLAAlpdgldtWLGEGGRRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT 527
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-248 |
2.18e-39 |
|
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: 136.31 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKtLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysprTDTVDLR 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPD---SGKILLNGKDI----TNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKgIRDKSILDHAVESSLKGASIwnevKDRLHDSAVGLSGGQQQRVCIARVLA 164
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKKR-KVDKKEIERKVLEIAEMLGI----DHLLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKE 242
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVlhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*.
gi 489083979 243 TEDYIS 248
Cdd:cd03299 226 VAEFLG 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-229 |
2.85e-39 |
|
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: 134.49 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRtdtvDL 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPS---SGEILLDGKDLasLSPK----EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQpnpfpmsiyenvvygLRLKGIRDKsildhavesslkgasiwnevKDRLHDSavgLSGGQQQRVCIARVLA 164
Cdd:cd03214 72 ARKIAYVPQA---------------LELLGLAHL--------------------ADRPFNE---LSGGERQRVLLARALA 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 165 TSPRIILLDEPTSALDPisAGKIeETLLLLKK-----DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03214 114 QEPPILLLDEPTSHLDI--AHQI-ELLELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-242 |
3.43e-39 |
|
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: 135.88 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTV 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SGLLPPR---SGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 dLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKgiRDKSILDHAVEsslkgasiwnEV-------KDRLHDSAVGLSGGQQ 154
Cdd:COG0410 76 -ARLGIGYVPEGRRIFPsLTVEENLLLGAYAR--RDRAEVRADLE----------RVyelfprlKERRRQRAGTLSGGEQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRtGFFLE-GDLLECGPTK 232
Cdd:COG0410 143 QMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR-AYVLErGRIVLEGTAA 221
|
250
....*....|
gi 489083979 233 AMFMNPKRKE 242
Cdd:COG0410 222 ELLADPEVRE 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-239 |
3.79e-39 |
|
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: 142.13 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmndLNPE--VTITGSIVYNGHNI 74
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGtveaVKGVSFDIAAGETLALVGESGSGKSVTALSILR---LLPDpaAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 75 --YSPRTdtvdLRK----EIGMVFQQP----NPFpMSIYENVVYGLRL-KGIRDKSILDHAVEsslkgasIWNEV----- 138
Cdd:COG4172 79 lgLSERE----LRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLhRGLSGAAARARALE-------LLERVgipdp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 139 KDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSMQQASRLSDR 216
Cdd:COG4172 147 ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLliTHDLGVVRRFADR 226
|
250 260
....*....|....*....|...
gi 489083979 217 TGFFLEGDLLECGPTKAMFMNPK 239
Cdd:COG4172 227 VAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-237 |
5.51e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.72 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ-----KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTD 80
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPT---SGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQP--NPFPMSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASiWNEVKDRlhdSAVGLSGGQQQRV 157
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmNIVGLD-YEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMF 235
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
..
gi 489083979 236 MN 237
Cdd:PRK13637 234 KE 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-249 |
7.49e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.87 E-value: 7.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPR-T 79
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVNGQTINLVRdK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 D----TVD------LRKEIGMVFQQPNPFP-MSIYENV------VYGLRLKGIRDKSILdhavesSLKGASIWNEVKDRL 142
Cdd:PRK10619 76 DgqlkVADknqlrlLRTRLTMVFQHFNLWShMTVLENVmeapiqVLGLSKQEARERAVK------YLAKVGIDERAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 143 hdsAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFL 221
Cdd:PRK10619 150 ---PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLH 226
|
250 260
....*....|....*....|....*...
gi 489083979 222 EGDLLECGPTKAMFMNPKRKETEDYISG 249
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-239 |
7.81e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.90 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEpiLQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndlnpevTIT-GSIVYNGHNIysprT 79
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIag------leDPTsGEILIGGRDV----T 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVEsslkgasiwnEVKDRLHDSAV------GLSGG 152
Cdd:COG3839 69 DLPPKDRNIAMVFQSYALYPhMTVYENIAFPLKLRKV-PKAEIDRRVR----------EAAELLGLEDLldrkpkQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPisagKI-EETLLLLKK-----DYTLAIVTRSMQQASRLSDRTGFFLEGDLL 226
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDA----KLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
250
....*....|...
gi 489083979 227 ECGPTKAMFMNPK 239
Cdd:COG3839 214 QVGTPEELYDRPA 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-216 |
9.85e-39 |
|
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: 134.87 E-value: 9.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIyspRTDTVDLR 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPT---SGSVLFDGEDI---TGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMV--FQQPNPFP-MSIYENVVYGLRLK---GIRDKSILDHAVESSLKGASIWNEVK--DRLHDSAVGLSGGQQQRV 157
Cdd:cd03219 73 ARLGIGrtFQIPRLFPeLTVLENVMVAAQARtgsGLLLARARREEREARERAEELLERVGlaDLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLK-KDYTLAIVTRSMQQASRLSDR 216
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADR 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-217 |
1.47e-38 |
|
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: 133.43 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIysprtdtVDLRK 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--LGLLKP---TSGSIRVFGKPL-------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 87 EIGMVFQQPN---PFPMSIYENVVYGLR-----LKGIR--DKSILDHAVESSlkGASiwnEVKDRLHDSavgLSGGQQQR 156
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGLYghkglFRRLSkaDKAKVDEALERV--GLS---ELADRQIGE---LSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRT 217
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-239 |
1.80e-38 |
|
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: 133.90 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVDLR 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKDI----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLA 164
Cdd:cd03300 72 RPVNTVFQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 165 TSPRIILLDEPTSALDPisagKIEETLLL----LKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:cd03300 147 NEPKVLLLDEPLGALDL----KLRKDMQLelkrLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
.
gi 489083979 239 K 239
Cdd:cd03300 223 A 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-248 |
3.42e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI-YSPRTDTVD- 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQFdFSQKPSEKAi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 --LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIRDKsildHAVEsslKGASIWNEVkdRLHDSA----VGLSGGQQQ 155
Cdd:COG4161 78 rlLRQKVGMVFQQYNLWPhLTVMENLIEApCKVLGLSKE----QARE---KAMKLLARL--RLTDKAdrfpLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDP-ISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGpTKAM 234
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPeITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASH 227
|
250
....*....|....
gi 489083979 235 FMNPKRKETEDYIS 248
Cdd:COG4161 228 FTQPQTEAFAHYLS 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
6.32e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 6.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIyspR 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPE---AGTITVGGMVL---S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTV-DLRKEIGMVFQQP-NPFPMSIYEN-VVYGLRLKGI-RDKSI--LDHAVEsslkgasiwnEV--KDRLHDSAVGLS 150
Cdd:PRK13635 73 EETVwDVRRQVGMVFQNPdNQFVGATVQDdVAFGLENIGVpREEMVerVDQALR----------QVgmEDFLNREPHRLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPIsaGKIE--ETLLLLKKDYTLAI--VTRSMQQASRlSDRTGFFLEGDLL 226
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKEQKGITVlsITHDLDEAAQ-ADRVIVMNKGEIL 219
|
....*....
gi 489083979 227 ECGPTKAMF 235
Cdd:PRK13635 220 EEGTPEEIF 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-216 |
1.58e-37 |
|
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: 132.55 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTdTVD 83
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEEN-LWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQP-NPFPMSIYEN-VVYGLRLKGI-RDKsiLDHAVESSLKGASIWnevkDRLHDSAVGLSGGQQQRVCIA 160
Cdd:TIGR04520 75 IRKKVGMVFQNPdNQFVGATVEDdVAFGLENLGVpREE--MRKRVDEALKLVGME----DFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSMQQASrLSDR 216
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVIsiTHDMEEAV-LADR 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-181 |
1.98e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 135.23 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKT-----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlnpEVTiTGSIVYNGHNIYS-PRTDTVDLR-KEIG 89
Cdd:COG4175 34 LEKTgqtvgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLI----EPT-AGEVLIDGEDITKlSKKELRELRrKKMS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 90 MVFQQ----PNpfpMSIYENVVYGLRLKGIRDKSILDHAVES----SLKGasiWnevKDRLHDSavgLSGGQQQRVCIAR 161
Cdd:COG4175 109 MVFQHfallPH---RTVLENVAFGLEIQGVPKAERRERAREAlelvGLAG---W---EDSYPDE---LSGGMQQRVGLAR 176
|
170 180
....*....|....*....|
gi 489083979 162 VLATSPRIILLDEPTSALDP 181
Cdd:COG4175 177 ALATDPDILLMDEAFSALDP 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-239 |
2.33e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.70 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYY--------NQKKTLK---DVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIV 68
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL------EEPTsGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 69 YNGHNIYS-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIRDKSildhavesslkgasiwnEVKDRLH 143
Cdd:COG4608 77 FDGQDITGlSGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKA-----------------ERRERVA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 144 D--SAVGL------------SGGQQQRVCIARVLATSPRIILLDEPTSALD-PISAGKIeeTLLL-LKKDYTLAI----- 202
Cdd:COG4608 139 EllELVGLrpehadryphefSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQVL--NLLEdLQDELGLTYlfish 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489083979 203 ---VTRSMqqasrlSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:COG4608 217 dlsVVRHI------SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-216 |
3.39e-37 |
|
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: 134.01 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVD 83
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDI----TRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGiRDKSILDHAVESSLkgasiwnEVKDrLHDSA----VGLSGGQQQRVC 158
Cdd:TIGR03265 74 QKRDYGIVFQSYALFPnLTVADNIAYGLKNRG-MGRAEVAERVAELL-------DLVG-LPGSErkypGQLSGGQQQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489083979 159 IARVLATSPRIILLDEPTSALDpisaGKIEETL------LLLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALD----ARVREHLrteirqLQRRLGVTTIMVTHDQEEALSMADR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-239 |
3.84e-37 |
|
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: 136.74 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTL-----------KDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNG 71
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLfrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIRFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 72 HNIYS-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLkgirdksildHAVEssLKGASIWNEVKDRLHDsa 146
Cdd:COG4172 347 QDLDGlSRRALRPLRRRMQVVFQDPfgslSP-RMTVGQIIAEGLRV----------HGPG--LSAAERRARVAEALEE-- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 147 VGL------------SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA---I-----VTRS 206
Cdd:COG4172 412 VGLdpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAylfIshdlaVVRA 491
|
250 260 270
....*....|....*....|....*....|...
gi 489083979 207 MqqasrlSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:COG4172 492 L------AHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-248 |
1.11e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 129.75 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI-YSPRTDTVD- 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNHFdFSKTPSDKAi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 --LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIRDKSILDHAVE--SSLKgasiWNEVKDR--LHdsavgLSGGQQQ 155
Cdd:PRK11124 78 reLRRNVGMVFQQYNLWPhLTVQQNLIEApCRVLGLSKDQALARAEKllERLR----LKPYADRfpLH-----LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDP-ISAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGpTKAM 234
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPeITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASC 227
|
250
....*....|....
gi 489083979 235 FMNPKRKETEDYIS 248
Cdd:PRK11124 228 FTQPQTEAFKNYLS 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-214 |
2.14e-36 |
|
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: 128.81 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNPF 98
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDIrdLNLR----WLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 99 PMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKDRLH--DSAVG-----LSGGQQQRVCIARVLATSPRIIL 171
Cdd:cd03249 90 DGTIAENIRYG-------KPDATDEEVEEAAKKANIHDFIMSLPDgyDTLVGergsqLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489083979 172 LDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTIVI------AHRLS 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-181 |
9.94e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.58 E-value: 9.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI--YSPRtdt 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPD---SGEVRLNGRPLadWSPA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 vDLRKEIGMVFQQPN-PFPMSIYEnVV----YGLRLKGIRDKSILDHAVESSlkGASiwnEVKDRLHDSavgLSGGQQQR 156
Cdd:PRK13548 73 -ELARRRAVLPQHSSlSFPFTVEE-VVamgrAPHGLSRAEDDALVAAALAQV--DLA---HLAGRDYPQ---LSGGEQQR 142
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 157 VCIARVLA------TSPRIILLDEPTSALDP 181
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALDL 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-235 |
2.28e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQkkTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysprTDT-VDL 84
Cdd:COG3840 2 LRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGF--LPPD---SGRILWNGQDL----TALpPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKeIGMVFQQPNPFP-MSIYENVVYGLR--LK-GIRDKSILDHAVES-SLKGasiwneVKDRLHDSavgLSGGQQQRVCI 159
Cdd:COG3840 71 RP-VSMLFQENNLFPhLTVAQNIGLGLRpgLKlTAEQRAQVEQALERvGLAG------LLDRLPGQ---LSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 160 ARVLATSPRIILLDEPTSALDPisaGKIEETLLLLK---KDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDP---ALRQEMLDLVDelcRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
.
gi 489083979 235 F 235
Cdd:COG3840 218 L 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-226 |
3.08e-35 |
|
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: 125.10 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 19 KTLKDVSLDL---YPNEITALIGPSGSGKSTLLRSINRMndLNPEVtitGSIVYNGHNIYSPRTDtVDL---RKEIGMVF 92
Cdd:cd03297 8 KRLPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGL--EKPDG---GTIVLNGTVLFDSRKK-INLppqQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQPNPFP-MSIYENVVYGLRLKgiRDKSILDHAvesslkgasiwNEVKDRLHDSAV------GLSGGQQQRVCIARVLAT 165
Cdd:cd03297 82 QQYALFPhLNVRENLAFGLKRK--RNREDRISV-----------DELLDLLGLDHLlnrypaQLSGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 166 SPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLSDRTGFFLEGDLL 226
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPviFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-192 |
4.96e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.74 E-value: 4.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLrsiNRMND-LNPEvtiTGSIVYNGHNIYSPR 78
Cdd:COG4525 2 SMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGfLAPS---SGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDtvdlRkeiGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVE-------SSLKGASIWNevkdrlhdsavgLS 150
Cdd:COG4525 76 AD----R---GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEEllalvglADFARRRIWQ------------LS 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLL 192
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLL 178
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-181 |
1.01e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.84 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmnDLNPEvtiTGSIVYNGHNI--YSPRtdtvD 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPLaaWSPW----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPN-PFPMSIYEnVV----YGLRLKGIRDKSILDHAVEssLKGASiwnEVKDRLHDSavgLSGGQQQRVC 158
Cdd:COG4559 73 LARRRAVLPQHSSlAFPFTVEE-VValgrAPHGSSAAQDRQIVREALA--LVGLA---HLAGRSYQT---LSGGEQQRVQ 143
|
170 180 190
....*....|....*....|....*....|
gi 489083979 159 IARVLA-------TSPRIILLDEPTSALDP 181
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-214 |
1.10e-34 |
|
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: 124.26 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ-KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTVD- 83
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI---REVTLDs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKdRL---HDSAVG-----LSGGQQQ 155
Cdd:cd03253 73 LRRAIGVVPQDTVLFNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIM-RFpdgYDTIVGerglkLSGGEKQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI------AHRLS 197
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-248 |
3.22e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.68 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLS-VYYNQKKT---LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYS-PRTDT 81
Cdd:PRK11153 3 ELKNISkVFPQGGRTihaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE--RPT---SGRVLVDGQDLTAlSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNpfPMS---IYENVVYGLRLKGIRDKSIlDHAVESSLK--GASiwnevkDRLHDSAVGLSGGQQQR 156
Cdd:PRK11153 78 RKARRQIGMIFQHFN--LLSsrtVFDNVALPLELAGTPKAEI-KARVTELLElvGLS------DKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPisagkieET----LLLLKK---DYTLAIV--TRSMQQASRLSDRTGFFLEGDLLE 227
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDP-------ATtrsiLELLKDinrELGLTIVliTHEMDVVKRICDRVAVIDAGRLVE 221
|
250 260
....*....|....*....|.
gi 489083979 228 CGPTKAMFMNPKRKETEDYIS 248
Cdd:PRK11153 222 QGTVSEVFSHPKHPLTREFIQ 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-203 |
5.27e-34 |
|
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: 122.84 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRt 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPT---SGRILFDGRDItgLPPH- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 dtvdlrkEI---GMV--FQQPNPFP-MSIYENVVYGLRLkgiRDKSILDHAVESSLKGASIWNEVKDR------------ 141
Cdd:COG0411 75 -------RIarlGIArtFQNPRLFPeLTVLENVLVAAHA---RLGRGLLAALLRLPRARREEREARERaeellervglad 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 142 -LHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:COG0411 145 rADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITIL 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-214 |
6.84e-34 |
|
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: 121.95 E-value: 6.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKT--LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTV- 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPpvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDV---RDYTLa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFPMSIYENVVYGLRlkgirdkSILDHAVESSLKGASIwNEVKDRL---HDSAVG-----LSGGQQ 154
Cdd:cd03251 73 SLRRQIGLVSQDVFLFNDTVAENIAYGRP-------GATREEVEEAARAANA-HEFIMELpegYDTVIGergvkLSGGQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVI------AHRLS 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-238 |
1.01e-33 |
|
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: 124.83 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 23 DVSLDLYPNEITALIGPSGSGKSTLLRSI---NRmndlnPEvtiTGSIVYNGHNIYSPRTDtVDL---RKEIGMVFQQPN 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER-----PD---SGRIRLGGEVLQDSARG-IFLpphRRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFP-MSIYENVVYGL-RLKGIRDKSILDHAVEsslkgasiWNEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDE 174
Cdd:COG4148 88 LFPhLSVRGNLLYGRkRAPRAERRISFDEVVE--------LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 175 PTSALDpiSAGKiEETLLLLKK--DyTLAI----VTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:COG4148 160 PLAALD--LARK-AEILPYLERlrD-ELDIpilyVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-230 |
1.12e-33 |
|
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: 128.15 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 20 TLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFP 99
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDLAG--LDVQAVRRQLGVVLQNGRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 100 MSIYENVVYGLRLKgirdksiLDHAVESsLKGASIWNEVKDR---LH----DSAVGLSGGQQQRVCIARVLATSPRIILL 172
Cdd:TIGR03797 541 GSIFENIAGGAPLT-------LDEAWEA-ARMAGLAEDIRAMpmgMHtvisEGGGTLSGGQRQRLLIARALVRKPRILLF 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 173 DEPTSALDPISAGKIEETLLLLKkdytlaiVTRsMQQASRLS-----DRTGFFLEGDLLECGP 230
Cdd:TIGR03797 613 DEATSALDNRTQAIVSESLERLK-------VTR-IVIAHRLStirnaDRIYVLDAGRVVQQGT 667
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-216 |
1.28e-33 |
|
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: 120.82 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLR 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGGRDV----TDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGiRDKSILDHAVESSLKGASIwNEVKDRLHDSavgLSGGQQQRVCIARVLA 164
Cdd:cd03301 72 RDIAMVFQNYALYPhMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQI-EHLLDRKPKQ---LSGGQRQRVALGRAIV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 165 TSPRIILLDEPTSALDpisAGKIEETLLLLKK-----DYTLAIVTRSMQQASRLSDR 216
Cdd:cd03301 147 REPKVFLMDEPLSNLD---AKLRVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADR 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-239 |
1.58e-33 |
|
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: 121.29 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLR 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGEDA----TDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIR---DKSILDHAVESSLKGASIwnevkDRLHDS-AVGLSGGQQQRVCIA 160
Cdd:cd03296 74 RNVGFVFQHYALFRhMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQL-----DWLADRyPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDpisaGKIEETL------LLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALD----AKVRKELrrwlrrLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
....*
gi 489083979 235 FMNPK 239
Cdd:cd03296 225 YDHPA 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-180 |
2.07e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTD 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI----TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCI 159
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKPHQ----LSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 489083979 160 ARVLATSPRIILLDEPTSALD 180
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-203 |
4.83e-33 |
|
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: 119.94 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYS-PRTDTVdl 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MGLLPVK---SGSIRLDGEDITKlPPHERA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVEsslkgasIWNEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:TIGR03410 74 RAGIAYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAIL 186
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-204 |
1.40e-32 |
|
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: 124.32 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQK-KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTV 82
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPT---EGSIAVNGVPL--ADADAD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFPMSIYENVvyglRLkGIRDKSilDHAVESSLKGASIWNEVKDR-------LHDSAVGLSGGQQQ 155
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENI----RL-ARPDAS--DAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQ 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT 514
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-204 |
1.71e-32 |
|
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: 117.58 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIyspRTDTVD 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPPS---AGEVLWNGEPI---RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIR-DKSILDHAVES-SLKGasiwnevkdRLHDSAVGLSGGQQQRVCIA 160
Cdd:COG4133 73 YRRRLAYLGHADGLKPeLTVRENLRFWAALYGLRaDREAIDEALEAvGLAG---------LADLPVRQLSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
1.86e-32 |
|
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: 118.31 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLrSInrMNDLnpEVTITGSIVYNGHNIys 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLL-GL--LAGL--DRPTSGTVRLAGQDL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 prtDTVD------LRKE-IGMVFQQ----PNpfpMSIYENVVYGLRLKGIRD-----KSILDhAVesslkGasiwneVKD 140
Cdd:COG4181 77 ---FALDedararLRARhVGFVFQSfqllPT---LTALENVMLPLELAGRRDararaRALLE-RV-----G------LGH 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 141 RLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRlSDRT 217
Cdd:COG4181 139 RLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRV 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-181 |
1.60e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.27 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIysprtDTVD-L 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRL-----TALPaE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYGL--RLKGIRDKSILDHAVES-SLKGASiwnevkDRlhDSAVgLSGGQQQRVCIA 160
Cdd:COG4136 75 QRRIGILFQDDLLFPhLSVGENLAFALppTIGRAQRRARVEQALEEaGLAGFA------DR--DPAT-LSGGQRARVALL 145
|
170 180
....*....|....*....|.
gi 489083979 161 RVLATSPRIILLDEPTSALDP 181
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDA 166
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-181 |
1.81e-31 |
|
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: 114.98 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLyPNEITALIGPSGSGKSTLLRSInrmndlnpeVTIT----GSIVYNGHniySPRTDT 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRIL---------ATLTppssGTIRIDGQ---DVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWnevkDRLHDSAVGLSGGQQQRVCIA 160
Cdd:cd03264 68 QKLRRRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLG----DRAKKKIGSLSGGMRRRVGIA 142
|
170 180
....*....|....*....|.
gi 489083979 161 RVLATSPRIILLDEPTSALDP 181
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDP 163
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.88e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRT 79
Cdd:PRK13636 1 MEDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSILDHaVESSLKGASIwNEVKDRlhdSAVGLSGGQQQRV 157
Cdd:PRK13636 76 GLMKLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDEVRKR-VDNALKRTGI-EHLKDK---PTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKK--DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMF 235
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-204 |
4.27e-31 |
|
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: 114.61 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYN--QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYspRTDTVD 83
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPT---SGSVLLDGTDIR--QLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKD-------RLHDSAVGLSGGQQQR 156
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLG-------APLADDERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-247 |
5.05e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.01 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVD 83
Cdd:PRK11607 18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDL----SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHaVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARV 162
Cdd:PRK11607 89 YQRPINMMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIE-ETLLLLKK-DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKR 240
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
....*..
gi 489083979 241 KETEDYI 247
Cdd:PRK11607 244 RYSAEFI 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-234 |
1.02e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.34 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRtdtv 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQ---SGTVFLGDKPIsmLSSR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQ-PNPFPMSIYENVVYG----LRLKG---IRDKSILDHAVEsslkgASIWNEVKDRLHDSavgLSGGQQ 154
Cdd:PRK11231 73 QLARRLALLPQHhLTPEGITVRELVAYGrspwLSLWGrlsAEDNARVNQAME-----QTRINHLADRRLTD---LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDpisagkIEETLLLLK-------KDYTLAIVTRSMQQASRLSDRTGFFLEGDLLE 227
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLD------INHQVELMRlmrelntQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
....*...
gi 489083979 228 CG-PTKAM 234
Cdd:PRK11231 219 QGtPEEVM 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-220 |
1.11e-30 |
|
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: 112.64 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvTITGSIVYNGHNIYSPRtdtvdLRKEIGMVFQQPN 96
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL--AGRRTGL-GVSGEVLINGRPLDKRS-----FRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFP-MSIYENVVYGLRLKGIrdksildhavesslkgasiwnevkdrlhdsavglSGGQQQRVCIARVLATSPRIILLDEP 175
Cdd:cd03213 93 LHPtLTVRETLMFAAKLRGL----------------------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489083979 176 TSALDPISAGKIEETLLLLKKDYTLAIVTrsMQQASrlSDRTGFF 220
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICS--IHQPS--SEIFELF 179
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-243 |
1.30e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 119.19 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDL-------SVYYNQKK----TLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNG 71
Cdd:PRK10261 311 EPILQVRNLvtrfplrSGLLNRVTrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 72 HNIYS-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRL-HDs 145
Cdd:PRK10261 386 QRIDTlSPGKLQALRRDIQFIFQDPyaslDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHE- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 146 avgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLSDRTGFFLEG 223
Cdd:PRK10261 464 ---FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAylFISHDMAVVERISHRVAVMYLG 540
|
250 260
....*....|....*....|
gi 489083979 224 DLLECGPTKAMFMNPKRKET 243
Cdd:PRK10261 541 QIVEIGPRRAVFENPQHPYT 560
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-214 |
1.55e-30 |
|
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: 113.09 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKK-TLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSprTDTVDLR 85
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQ---KGQILIDGIDIRD--ISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKDRLH--DSAVG-----LSGGQQQRVC 158
Cdd:cd03254 77 SMIGVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLPNgyDTVLGenggnLSQGERQLLA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIII------AHRLS 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-229 |
3.93e-30 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 112.08 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIyspRTDTVDLR 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPT---SGRATVAGHDV---VREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRdKSILDHAVESSLKGASIWnEVKDRLhdsAVGLSGGQQQRVCIARVLA 164
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLYGVP-GAERRERIDELLDFVGLL-EAADRL---VKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-229 |
9.37e-30 |
|
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: 109.71 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmnDLNPEvtiTGSIVYNGHNIYSPRTdtvD 83
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLEK---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVvyglrlkGIRdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARVL 163
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL-------GRR--------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASRLsDRTGFFLEGDLLECG 229
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-229 |
9.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.52 E-value: 9.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVyNGHNIYsprtdtv 82
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRgRVKVMGREV-NAENEK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSILDHaVESSLKGASIWnevkDRLHDSAVGLSGGQQQRVCIA 160
Cdd:PRK13647 76 WVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLDKDEVERR-VEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-232 |
1.79e-29 |
|
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: 112.10 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 14 YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PRTdtvdLRKEIGMVF 92
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDVVRePRK----VRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQPNPFP-MSIYENVVYGLRLKGIRdKSILDHAVESSLKGASIWnEVKDRLhdsAVGLSGGQQQRVCIARVLATSPRIIL 171
Cdd:TIGR01188 73 QYASVDEdLTGRENLEMMGRLYGLP-KDEAEERAEELLELFELG-EAADRP---VGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 172 LDEPTSALDPISAGKIEETLLLLKK-DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTK 232
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-230 |
2.15e-29 |
|
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: 115.58 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDtvD 83
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDLADYTLA--S 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGlRLKGIRDKSILDHAVESSLKgaSIWNEVKDRLH----DSAVGLSGGQQQRVCI 159
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYG-RTEQADRAEIERALAAAYAQ--DFVDKLPLGLDtpigENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS-----DRTGFFLEGDLLECGP 230
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI------AHRLStiekaDRIVVMDDGRIVERGT 550
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-196 |
2.74e-29 |
|
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: 109.65 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQK-KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PRTDTV 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA--LTPS---RGQVRIAGEDVNRlRGRQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKgasiWNEVKDRLHDSAVGLSGGQQQRVCIAR 161
Cdd:TIGR02673 76 LLRRRIGVVFQDFRLLPdRTVYENVALPLEVRGKKEREI-QRRVGAALR----QVGLEHKADAFPEQLSGGEQQRVAIAR 150
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 162 VLATSPRIILLDEPTSALDPISAgkiEETLLLLKK 196
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLS---ERILDLLKR 182
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-238 |
3.03e-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: 112.90 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 23 DVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEVtitGSIVYNGHNIYSPRTDtVDL---RKEIGMVFQQPNPFP 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL--TRPDE---GEIVLNGRTLFDSRKG-IFLppeKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 100 -MSIYENVVYGLRLKGIRDKSILDHAVESSLKgasiwnevKDRLHDSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTS 177
Cdd:TIGR02142 89 hLSVRGNLRYGMKRARPSERRISFERVIELLG--------IGHLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 178 ALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPIlyVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-212 |
3.24e-29 |
|
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: 109.87 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQK---KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRT 79
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPI--SQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlKGIRDKSILDHAVES------SLKGASIWNEVKDRlhdsAVGLSGGQ 153
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGL--QSCSFECVKEAAQKAhahsfiSELASGYDTEVGEK----GSQLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMQQASR 212
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-216 |
3.52e-29 |
|
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: 115.35 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRT-DTV 82
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL--LGLYQP---TEGSVLLDGVDI---RQiDPA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFPMSIYENVVYGLRLkgIRDKSILDHA--------VESSLKGAsiwnevkDR-LHDSAVGLSGGQ 153
Cdd:TIGR03375 536 DLRRNIGYVPQDPRLFYGTLRDNIALGAPY--ADDEEILRAAelagvtefVRRHPDGL-------DMqIGERGRSLSGGQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSMqQASRLSDR 216
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRT-SLLDLVDR 668
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-203 |
4.08e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 108.88 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSV-YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIySPRtdtvDLR 85
Cdd:cd03226 1 RIENISFsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPI-KAK----ERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNP--FPMSIYENVVYGLRLKgirDKSILDhaVESSLKGASIWnEVKDRL-HDsavgLSGGQQQRVCIARV 162
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKEL---DAGNEQ--AETVLKDLDLY-ALKERHpLS----LSGGQKQRLAIAAA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIV 181
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
5.27e-29 |
|
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: 114.38 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTD 80
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 tvDLRKEIGMVFQQPNPFPMSIYENvvygLRLkGIRDKSilDHAVESSLKGASIWNEVKDRLH--DSAVG-----LSGGQ 153
Cdd:TIGR02868 406 --EVRRRVSVCAQDAHLFDTTVREN----LRL-ARPDAT--DEELWAALERVGLADWLRALPDglDTVLGeggarLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRS 206
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-239 |
6.16e-29 |
|
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: 111.43 E-value: 6.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 36 LIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKG 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 115 IrDKSILDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL 194
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489083979 195 KKDY--TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:TIGR01187 147 QEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
6.91e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYN--QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNP---EVTITGsIVYNGHNIYsp 77
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPqsgEIKIDG-ITISKENLK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 rtdtvDLRKEIGMVFQQP-NPF-PMSIYENVVYGLRLKGIRDKSILDHAVESSLKgasiwNEVKDRLHDSAVGLSGGQQQ 155
Cdd:PRK13632 80 -----EIRKKIGIIFQNPdNQFiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKK-----VGMEDYLDKEPQNLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKK--DYTLAIVTRSMQQASrLSDRTGFFLEGDLLECGPTKA 233
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKE 228
|
....*....
gi 489083979 234 MFMNPKRKE 242
Cdd:PRK13632 229 ILNNKEILE 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-231 |
7.12e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 109.63 E-value: 7.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmnDLNPEvtiTGSIVYNGHNiySPRTD 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRD--GQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDL---------RKEIGMVFQQP-NPFPMSIYE--NVvyGLRLKG--------IRDKsildhavesslkgASIW-NEVK 139
Cdd:PRK11701 75 LYALseaerrrllRTEWGFVHQHPrDGLRMQVSAggNI--GERLMAvgarhygdIRAT-------------AGDWlERVE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 140 ---DRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLS 214
Cdd:PRK11701 140 idaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAvvIVTHDLAVARLLA 219
|
250
....*....|....*..
gi 489083979 215 DRTGFFLEGDLLECGPT 231
Cdd:PRK11701 220 HRLLVMKQGRVVESGLT 236
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-248 |
7.32e-29 |
|
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: 109.53 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVY-----NGHNIYS- 76
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPD---HGTATYimrsgAELELYQl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 PRTDTVDL-RKEIGMVFQQP-NPFPMSIYENVVYGLRLK--GIRDKSILDHAVESSLKGASIwneVKDRLHDSAVGLSGG 152
Cdd:TIGR02323 76 SEAERRRLmRTEWGFVHQNPrDGLRMRVSAGANIGERLMaiGARHYGNIRATAQDWLEEVEI---DPTRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLSDRTGFFLEGDLLECGP 230
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAviIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
250
....*....|....*...
gi 489083979 231 TKAMFMNPKRKETEDYIS 248
Cdd:TIGR02323 233 TDQVLDDPQHPYTQLLVS 250
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-216 |
9.40e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.82 E-value: 9.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQ---KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIyspR 78
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAE---SGQIIIDGDLL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTV-DLRKEIGMVFQQP-NPFPMSIYEN-VVYGLRLKGIRDKSILDHAVES-SLKGASiwnEVKDRlhdSAVGLSGGQQ 154
Cdd:PRK13650 73 EENVwDIRHKIGMVFQNPdNQFVGATVEDdVAFGLENKGIPHEEMKERVNEAlELVGMQ---DFKER---EPARLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPisAGKIE--ETLLLLKKDYTLAI--VTRSMQQASrLSDR 216
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYQMTVisITHDLDEVA-LSDR 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-217 |
1.49e-28 |
|
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: 107.49 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 13 VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEIGMV 91
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 92 FQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIwnevKDRLHDSAVGLSGGQQQRVCIARVLATSPRII 170
Cdd:cd03292 84 FQDFRLLPdRNVYENVAFALEVTGVPPREI-RKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489083979 171 LLDEPTSALDPISAGKIEETLlllkKDYTLAIVTRSM-QQASRLSDRT 217
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLL----KKINKAGTTVVVaTHAKELVDTT 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-214 |
1.97e-28 |
|
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: 112.99 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-----SGRILIDGQDI---RDVTQAsLRAAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 100 MSIYENVVYGlRLkgirDKSilDHAVESSLKGASIWNEVkDRL---HDSAVG-----LSGGQQQRVCIARVLATSPRIIL 171
Cdd:COG5265 446 DTIAYNIAYG-RP----DAS--EEEVEAAARAAQIHDFI-ESLpdgYDTRVGerglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489083979 172 LDEPTSALDPISAGKIEETLLLLKKDYT-LAIvtrsmqqASRLS 214
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTtLVI-------AHRLS 554
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-229 |
2.47e-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: 107.57 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPM 100
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF-----YVPENGRVLVDGHDLAL--ADPAWLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENVVY---GLRLKGIRDKSILDHAVESSLKGASIWNEVkdrLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTS 177
Cdd:cd03252 91 SIRDNIALadpGMSMERVIEAAKLAGAHDFISELPEGYDTI---VGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 178 ALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS-----DRTGFFLEGDLLECG 229
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIII------AHRLStvknaDRIIVMEKGRIVEQG 218
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-216 |
2.63e-28 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 107.11 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI----YSPRtdtVDLRKE-IGMV 91
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLD-----SGSLTLAGKEVtnlsYSQK---IILRRElIGYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 92 FQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHaVESSLKGASIWNevkdRLHDSAVGLSGGQQQRVCIARVLATSPRII 170
Cdd:NF038007 89 FQSFNLIPhLSIFDNVALPLKYRGVAKKERIER-VNQVLNLFGIDN----RRNHKPMQLSGGQQQRVAIARAMVSNPALL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489083979 171 LLDEPTSALDPISAGKIEETLLLL-KKDYTLAIVTRSmQQASRLSDR 216
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNR 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-194 |
3.12e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.86 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTdtvdl 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF--VPYQ---HGSITLDGKPVEGPGA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 rkEIGMVFQQPNPFP-MSIYENVVYGLRLKGI----RDKSILDHAVESSLKGAS---IWNevkdrlhdsavgLSGGQQQR 156
Cdd:PRK11248 71 --ERGVVFQNEGLLPwRNVQDNVAFGLQLAGVekmqRLEIAHQMLKKVGLEGAEkryIWQ------------LSGGQRQR 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL 194
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
3.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQ-KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTVD 83
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPT---SGEVLIKGEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNP--FPMSIYENVVYG-LRLKGIRDKsiLDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIA 160
Cdd:PRK13639 76 VRKTVGIVFQNPDDqlFAPTVEEDVAFGpLNLGLSKEE--VEKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLL-KKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-181 |
4.43e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVTIT-GSIVYNGHNiYSPRTD 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTL------MKILSGVYQPDsGEILLDGEP-VRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYG---LRLKGIRDKSILDHAvesslkgasiwNEVKDRLH-----DSAVG-LS 150
Cdd:COG1129 74 RDAQAAGIAIIHQELNLVPnLSVAENIFLGrepRRGGLIDWRAMRRRA-----------RELLARLGldidpDTPVGdLS 142
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDP 181
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-239 |
4.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIySPRTDTV---DLRKEIGMVFQ 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHI-TPETGNKnlkKLRKKVSLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 94 QPNP--FPMSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIWNEVKDRlhdSAVGLSGGQQQRVCIARVLATSPRIIL 171
Cdd:PRK13641 93 FPEAqlFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 172 LDEPTSALDPISagkiEETLLLLKKDY-----TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:PRK13641 169 LDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-216 |
1.23e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.25 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDlr 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-----SGHIRFHGTDV--SRLHARD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIR---DKSILDHAVESSLKGASIwNEVKDRLHDSavgLSGGQQQRVCIAR 161
Cdd:PRK10851 74 RKVGFVFQHYALFRhMTVFDNIAFGLTVLPRRerpNAAAIKAKVTQLLEMVQL-AHLADRYPAQ---LSGGQKQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD--YTLAIVTRSMQQASRLSDR 216
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEAMEVADR 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-238 |
1.39e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQK-----KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEV-TITGSIVYNGHNIYSPR 78
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGL--IKSKYgTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTVD----------LRKEIGMVFQQP--NPFPMSIYENVVYGLRLKGIrdksildHAVESSLKGASIWNEV---KDRLH 143
Cdd:PRK13631 99 LITNPyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGV-------KKSEAKKLAKFYLNKMgldDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 144 DSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPisAGKIEETLLLL---KKDYTLAIVTRSMQQASRLSDRTGFF 220
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP--KGEHEMMQLILdakANNKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*...
gi 489083979 221 LEGDLLECGPTKAMFMNP 238
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-238 |
1.72e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 8 IRDLSVYYN-----QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNP---EVTITGSIVYNGHNiyspRT 79
Cdd:PRK13634 5 FQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPtsgTVTIGERVITAGKK----NK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASiwnevKDRLHDSAVGLSGGQQQR 156
Cdd:PRK13634 79 KLKPLRKKVGIVFQFPEHqlFEETVEKDICFGPMNFGVSEEDAKQKAREMiELVGLP-----EELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL--KKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
....
gi 489083979 235 FMNP 238
Cdd:PRK13634 234 FADP 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-216 |
1.74e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.73 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysprtdTVDL 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGILAPD---SGEVLWDGEPL------DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIG-MvfqqpnpfP--------MSIYENVVYGLRLKGIrDKSILDHAVESslkgasiWNE---VKDRLHDSAVGLSGG 152
Cdd:COG4152 70 RRRIGyL--------PeerglypkMKVGEQLVYLARLKGL-SKAEAKRRADE-------WLErlgLGDRANKKVEELSKG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTlAIV--TRSMQQASRLSDR 216
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIfsSHQMELVEELCDR 198
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-216 |
1.85e-27 |
|
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: 104.67 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI-YSPRTDTVDL 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGKPLdIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMvfqqpnpFP-MSIYENVVYGLRLKGIRDKSILdHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVL 163
Cdd:cd03269 76 PEERGL-------YPkMKVIDQLVYLAQLKGLKKEEAR-RRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLK-KDYTLAIVTRSMQQASRLSDR 216
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDR 197
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
2.03e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.71 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQI--RDLSVYYNQK-----KTLKDVSLDLYPNEITALIGPSGSGKSTLlrsINRMNDLN-PEvtiTGSIVYNGHN---- 73
Cdd:PRK13651 1 MQIkvKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTF---IEHLNALLlPD---TGTIEWIFKDeknk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 74 --------------IYSPRTDTV----DLRKEIGMVFQ--QPNPFPMSIYENVVYGLRLKGIRDKsildHAVESSLKGAS 133
Cdd:PRK13651 75 kktkekekvleklvIQKTRFKKIkkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 134 IWNEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISagkIEETLLLLKKDY----TLAIVTRSMQQ 209
Cdd:PRK13651 151 LVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFDNLNkqgkTIILVTHDLDN 227
|
250 260
....*....|....*....|..
gi 489083979 210 ASRLSDRTGFFLEGDLLECGPT 231
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDT 249
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-191 |
2.12e-27 |
|
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: 104.88 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNI--YSPRtdt 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDIskIGLH--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 vDLRKEIGMVFQQPNPFPMSIYENvvygLRLKGIRDksilDHAVESSLKGASIWNEVK-------DRLHDSAVGLSGGQQ 154
Cdd:cd03244 75 -DLRSRISIIPQDPVLFSGTIRSN----LDPFGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-191 |
2.41e-27 |
|
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: 103.66 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 14 YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVFQ 93
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQ---SGAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 94 QPNP--FPMSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLATSPRIIL 171
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNLGLSEAEV-ERRVREALTAVGASGLRERPTHC----LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180
....*....|....*....|
gi 489083979 172 LDEPTSALDPISAGKIEETL 191
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAIL 170
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-223 |
2.55e-27 |
|
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: 104.50 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 32 EITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI-YSPRTDtvdlrKEIGMVFQQPNPFP-MSIYENVVYG 109
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGF-----ETPQSGRVLINGVDVtAAPPAD-----RPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 110 lRLKGIRDKSILDHAVESSLKGASIWNEVKdRLHDSavgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEE 189
Cdd:cd03298 95 -LSPGLKLTAEDRQAIEVALARVGLAGLEK-RLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 489083979 190 TLLLLKKD--YTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:cd03298 170 LVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-181 |
3.29e-27 |
|
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: 104.44 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTePILQIRDLS---VYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTiTGSIVYN--G 71
Cdd:COG4778 1 MT-TLLEVENLSktfTLHLQGGKrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG----NYLPD-SGSILVRhdG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 72 HNI----YSPRtDTVDLRK-EIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVE--SSLkgasiwnEVKDRLH 143
Cdd:COG4778 75 GWVdlaqASPR-EILALRRrTIGYVSQFLRVIPrVSALDVVAEPLLERGVDREEARARAREllARL-------NLPERLW 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 489083979 144 DSA-VGLSGGQQQRVCIARVLATSPRIILLDEPTSALDP 181
Cdd:COG4778 147 DLPpATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-203 |
3.61e-27 |
|
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: 104.78 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMN--DLNPEVTITGsIVYNGHNIYsprtd 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFG-ERRGGEDVW----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 tvDLRKEIGMV---FQQPNPFPMSIYENVVYGLRlkgirdksildhavesslkgASI--WNEVKDRLHDSAV-------- 147
Cdd:COG1119 75 --ELRKRIGLVspaLQLRFPRDETVLDVVLSGFF--------------------DSIglYREPTDEQRERARellellgl 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 148 ---------GLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:COG1119 133 ahladrpfgTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLV 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-244 |
4.49e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLK----DVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYs 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 pRTDTVDLRK----EIGMVFQQP----NPF---PMSIYENVVY--GLRLKGIRDKSIldhaveSSLKGASIWNEVKdRLH 143
Cdd:PRK15134 80 -HASEQTLRGvrgnKIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRREAARGEIL------NCLDRVGIRQAAK-RLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 144 DSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFL 221
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLlfITHNLSIVRKLADRVAVMQ 231
|
250 260
....*....|....*....|...
gi 489083979 222 EGDLLECGPTKAMFMNPKRKETE 244
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-229 |
5.88e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.90 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTVD-L 84
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--PQ---SGRILIDGTDI---RTVTRAsL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFPMSIYENvvygLRLkGIRDKSilDHAVESSLKGASIWN--EVKDRLHDSAVG-----LSGGQQQRV 157
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDN----IRV-GRPDAT--DEEMRAAAERAQAHDfiERKPDGYDTVVGergrqLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS-----DRTGFFLEGDLLECG 229
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFII------AHRLStvrnaDRILVFDNGRVVESG 551
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-227 |
6.28e-27 |
|
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: 103.07 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNP---EVTITGSIVYNGHNIYsprtdtv 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII--LGLIKPdsgEITFDGKSYQKNIEAL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 dlrKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIldhavesslkgASIWNEV--KDRLHDSAVGLSGGQQQRVCI 159
Cdd:cd03268 72 ---RRIGALIEAPGFYPnLTARENLRLLARLLGIRKKRI-----------DEVLDVVglKDSAKKKVKGFSLGMKQRLGI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEGDLLE 227
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-181 |
9.31e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDL----NPEvtiTGSIVYNGH--NI 74
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKILyglyQPD---SGEILIDGKpvRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 75 YSPRtDTVDLRkeIGMVFQQPNPFP-MSIYENVVYGL--RLKGIRDKSILDHAVEsslkgasiwnEVKDRLH-----DSA 146
Cdd:COG3845 72 RSPR-DAIALG--IGMVHQHFMLVPnLTVAENIVLGLepTKGGRLDRKAARARIR----------ELSERYGldvdpDAK 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 489083979 147 VG-LSGGQQQRVCIARVLATSPRIILLDEPTSALDP 181
Cdd:COG3845 139 VEdLSVGEQQRVEILKALYRGARILILDEPTAVLTP 174
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-216 |
1.95e-26 |
|
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: 100.58 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVTIT-GSIVYNGH--NIYSPRtDTV 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTL------MKILSGLYKPDsGEILVDGKevSFASPR-DAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRkeIGMVFQqpnpfpmsiyenvvyglrlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARV 162
Cdd:cd03216 74 RAG--IAMVYQ-------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDR 216
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-217 |
1.96e-26 |
|
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: 101.92 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 8 IRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTVD--LR 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFD-----SGQVYLNGQETPPLNSKKASkfRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQpnpFPM----SIYENVVYGLRLKGIRDKSILDHAVESsLKGASIWNEVKDRLHDsavgLSGGQQQRVCIAR 161
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGLKYKKLSKKEKREKKKEA-LEKVGLNLKLKQKIYE----LSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRlSDRT 217
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLeLNDEGKTIIIVTHDPEVAKQ-ADRV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-214 |
4.54e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 106.26 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKT--LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdt 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDLrdYTLA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 vDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKSI----LDHAVEsslkgasIWNEVKDRLhDSAVG-----LSGG 152
Cdd:PRK11176 414 -SLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEeaarMAYAMD-------FINKMDNGL-DTVIGengvlLSGG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI------AHRLS 540
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-240 |
5.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ-----KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTD 80
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKPT---TGTVTVDDITITHKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TV--DLRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSILDHAVESSLK-GASiwnevKDRLHDSAVGLSGGQQQ 155
Cdd:PRK13646 78 KYirPVRKRIGMVFQFPESqlFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDlGFS-----RDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKA 233
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
....*..
gi 489083979 234 MFMNPKR 240
Cdd:PRK13646 233 LFKDKKK 239
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-242 |
1.12e-25 |
|
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: 100.81 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYS-PrtdtVD 83
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGL--VRPD---AGKILIDGQDITHlP----MH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVF--QQPNPF-PMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIwnevKDRLHDSAVGLSGGQQQRVCIA 160
Cdd:TIGR04406 72 ERARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLLLLK-KDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKeRGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
...
gi 489083979 240 RKE 242
Cdd:TIGR04406 228 VRR 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-181 |
1.38e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.93 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYspRTDTVDLRK 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRL--LPPD---SGEVLVDGLDVA--TTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 87 EIGmVFQQPNPFPM--SIYENVVYGL------RLKGiRDKSILDHAVES-SLkgasiwNEVKDRLHDSavgLSGGQQQRV 157
Cdd:COG4604 76 RLA-ILRQENHINSrlTVRELVAFGRfpyskgRLTA-EDREIIDEAIAYlDL------EDLADRYLDE---LSGGQRQRA 144
|
170 180
....*....|....*....|....
gi 489083979 158 CIARVLATSPRIILLDEPTSALDP 181
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-214 |
1.39e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 100.28 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKK----TLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS 76
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 -PRTDTVDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIwnevKDRLHDSAVGLSGGQ 153
Cdd:PRK11629 76 lSSAAKAELRnQKLGFIYQFHHLLPdFTALENVAMPLLIGKKKPAEINSRALEM-LAAVGL----EHRANHRPSELSGGE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLS 214
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-240 |
1.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.32 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVFQQP 95
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP----SEGKVYVDGLDTSDEENLWDIRNKAGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 -NPFPMSIYE-NVVYGLRLKGIRDKSILDHaVESSLKGASIWNEVKDRLHdsavGLSGGQQQRVCIARVLATSPRIILLD 173
Cdd:PRK13633 95 dNQIVATIVEeDVAFGPENLGIPPEEIRER-VDESLKKVGMYEYRRHAPH----LLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 174 EPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRlSDRTGFFLEGDLLECGPTKAMFMNPKR 240
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEM 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-203 |
1.82e-25 |
|
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: 98.44 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSprTDTVD 83
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-----LGLLRPTSGRVRLDGADISQ--WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVvyglrlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARVL 163
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIV 151
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-204 |
1.86e-25 |
|
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: 99.14 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTiTGSIVYNGHNIysprTD-TVDL 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVT-EGEILFKGEDI----TDlPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 R--KEIGMVFQQPNPFPmsiyenvvyglrlkGIRdksildhavesslkgasiwneVKDRLHDSAVGLSGGQQQRVCIARV 162
Cdd:cd03217 74 RarLGIFLAFQYPPEIP--------------GVK---------------------NADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489083979 163 LATSPRIILLDEPTSALDpISAGKIEETLL--LLKKDYTLAIVT 204
Cdd:cd03217 119 LLLEPDLAILDEPDSGLD-IDALRLVAEVInkLREEGKSVLIIT 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-248 |
2.03e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.09 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQK----------KTLK---DVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTIT-GSIV 68
Cdd:PRK15079 6 KVLLEVADLKVHFDIKdgkqwfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGL------VKATdGEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 69 YNGHNIYSPRTDTV-DLRKEIGMVFQQP----NPfPMSIYENVVYGLRlkgirdksildhAVESSLKGAsiwnEVKDRLH 143
Cdd:PRK15079 80 WLGKDLLGMKDDEWrAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLR------------TYHPKLSRQ----EVKDRVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 144 D--SAVGL------------SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSM 207
Cdd:PRK15079 143 AmmLKVGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIfiAHDL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489083979 208 QQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETEDYIS 248
Cdd:PRK15079 223 AVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMS 263
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-234 |
2.06e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 25 SLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiyspRTDTVDLRKEIGMVFQQPNPFP-MSIY 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGF--LTPA---SGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFShLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 104 ENVVYGLRlKGIRdksiLDHAVESSLKgaSIWNEVK-----DRLHDSavgLSGGQQQRVCIARVLATSPRIILLDEPTSA 178
Cdd:PRK10771 90 QNIGLGLN-PGLK----LNAAQREKLH--AIARQMGiedllARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 179 LDPisAGKiEETLLLLK-----KDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAM 234
Cdd:PRK10771 160 LDP--ALR-QEMLTLVSqvcqeRQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-181 |
2.49e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 2.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKK--TLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSpr 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYNNQAITD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTVDLRKEIGMVFQQP-NPFPMSIYE-NVVYGLRlkgirdksilDHAVESSlKGASIWNEV------KDRLHDSAVGLS 150
Cdd:PRK13648 76 DNFEKLRKHIGIVFQNPdNQFVGSIVKyDVAFGLE----------NHAVPYD-EMHRRVSEAlkqvdmLERADYEPNALS 144
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDP 181
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-180 |
3.82e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 8 IRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI---------------NRMNDLNPEvtitgsivyngh 72
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigeKRMNDVPPA------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 73 niysprtdtvdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVesslkgasiwNEVKDRLHDSAV---- 147
Cdd:PRK11000 74 ------------ERGVGMVFQSYALYPhLSVAENMSFGLKLAGA-KKEEINQRV----------NQVAEVLQLAHLldrk 130
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 148 --GLSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK11000 131 pkALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-229 |
5.11e-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: 98.50 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPevTITGSIVYNGhniySPRT-DTVdlRKEIGMVFQQ 94
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--TTSGQILFNG----QPRKpDQF--QKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 95 PNPFP-MSIYENVVYG--LRLKGIRDKSILDHAVESSLKGasiwnevkdRLHDSAVG------LSGGQQQRVCIARVLAT 165
Cdd:cd03234 90 DILLPgLTVRETLTYTaiLRLPRKSSDAIRKKRVEDVLLR---------DLALTRIGgnlvkgISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 166 SPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT----RSmqQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTihqpRS--DLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-249 |
5.94e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLR----KEIGMVFQQPN 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEP---TRGQVLIDGVDI--AKISDAELRevrrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFP-MSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIWNEVkdrlHDSAVGLSGGQQQRVCIARVLATSPRIILLDEP 175
Cdd:PRK10070 117 LMPhMTVLDNTAFGMELAGINAEERREKALDA-LRQVGLENYA----HSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 176 TSALDPISAGKIEETLLLL--KKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETEDYISG 249
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
36-239 |
8.73e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 36 LIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIysprTDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKG 114
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAGLE--KPT---EGQIFIDGEDV----THRSIQQRDICMVFQSYALFPhMSLGENVGYGLKMLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 115 IRDKSILDHAVES----SLKGasiwneVKDRLHDSavgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEET 190
Cdd:PRK11432 108 VPKEERKQRVKEAlelvDLAG------FEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489083979 191 LLLLKK--DYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNPK 239
Cdd:PRK11432 179 IRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-223 |
9.65e-25 |
|
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: 97.62 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 13 VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLRKEIGMVF 92
Cdd:TIGR01277 6 VRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF-----IEPASGSIKVNDQSH----TGLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQPNPFP-MSIYENVVYG----LRLKGIRDKSILDHAVESSLkgasiwNEVKDRLHDSavgLSGGQQQRVCIARVLATSP 167
Cdd:TIGR01277 77 QENNLFAhLTVRQNIGLGlhpgLKLNAEQQEKVVDAAQQVGI------ADYLDRLPEQ---LSGGQRQRVALARCLVRPN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 168 RIILLDEPTSALDPISAgkiEETLLLLK-----KDYTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:TIGR01277 148 PILLLDEPFSALDPLLR---EEMLALVKqlcseRQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-238 |
9.89e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 9.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEVTITGSIVYNGHNIYSpr 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 tDTV-DLRKEIGMVFQQP-NPF-PMSIYENVVYGLRLKGI-RDKSIldHAVESSLKGASIWNEVKDRlhdsAVGLSGGQQ 154
Cdd:PRK13640 77 -KTVwDIREKVGIVFQNPdNQFvGATVGDDVAFGLENRAVpRPEMI--KIVRDVLADVGMLDYIDSE----PANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSMQQASrLSDRTGFFLEGDLLECGPTK 232
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsiTHDIDEAN-MADQVLVLDDGKLLAQGSPV 228
|
....*.
gi 489083979 233 AMFMNP 238
Cdd:PRK13640 229 EIFSKV 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
1.04e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.03 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTiTGSIVYNGHNIYSPRTD 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG----DPRAT-SGRIVFDGKDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVdLRKEIGMVFQQPNPFP-MSIYENVVYGlrlKGIRDKSILDHAVEsslKGASIWNEVKDRLHDSAVGLSGGQQQRVCI 159
Cdd:PRK11614 76 KI-MREAVAIVPEGRRVFSrMTVEENLAMG---GFFAERDQFQERIK---WVYELFPRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRtGFFLE 222
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADR-GYVLE 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-238 |
1.20e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.11 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY---NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTV 82
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQPT---GGQVLLDGVPL--VQYDHH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRKEIGMVFQQPNPFPMSIYENVVYGLRLKgiRDKSILDHAVESslkGASIWNEVKDRLHDSAVG-----LSGGQQQRV 157
Cdd:TIGR00958 552 YLHRQVALVGQEPVLFSGSVRENIAYGLTDT--PDEEIMAAAKAA---NAHDFIMEFPNGYDTEVGekgsqLSGGQKQRI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 158 CIARVLATSPRIILLDEPTSALDpisaGKIEETLLLLK--KDYTLAIVTRSMQQASRlSDRTGFFLEGDLLECGPTKAMF 235
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLM 701
|
...
gi 489083979 236 MNP 238
Cdd:TIGR00958 702 EDQ 704
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
1.93e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYN-----QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNI-YSP- 77
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA--GSLPPD---SGSILIDGKDVtKLPe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 --RTdtvdlrKEIGMVFQqpNPF----P-MSIYENVV--------YGLRLkGIRDKSIlDHAVE--SSLKgasiwNEVKD 140
Cdd:COG1101 76 ykRA------KYIGRVFQ--DPMmgtaPsMTIEENLAlayrrgkrRGLRR-GLTKKRR-ELFREllATLG-----LGLEN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 141 RLHDsAVG-LSGGQQQrvCIARVLAT--SPRIILLDEPTSALDPISAGKIEE-TLLLLKKDYTLAI-VTRSMQQASRLSD 215
Cdd:COG1101 141 RLDT-KVGlLSGGQRQ--ALSLLMATltKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLmVTHNMEQALDYGN 217
|
..
gi 489083979 216 RT 217
Cdd:COG1101 218 RL 219
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-229 |
1.95e-24 |
|
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: 101.74 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYN-QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDTVDL 84
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLL--VGFFQAR---SGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIRDKsiLDHAVESslkgASIWNEVKD-------RLHDSAVGLSGGQQQRV 157
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLLLGAKENVSQDE--IWAACEI----AEIKDDIENmplgyqtELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLkKDYTLAIVTRSMQQASRlSDRTGFFLEGDLLECG 229
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-229 |
2.01e-24 |
|
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: 97.05 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGhniYSPRTD 80
Cdd:cd03266 1 MITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPD---AGFATVDG---FDVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDksildHAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCI 159
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDrLTARENLEYFAGLYGLKG-----DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV-TRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-216 |
2.20e-24 |
|
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: 97.15 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYSPRTDTVdlrkeigMVFQQPNPFP- 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA--QPT---SGGVILEGKQITEPGPDRM-------VVFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 100 MSIYENV------VYGLRLKGIRDKSILDHAVESSLKGASiwnevkdrlHDSAVGLSGGQQQRVCIARVLATSPRIILLD 173
Cdd:TIGR01184 69 LTVRENIalavdrVLPDLSKSERRAIVEEHIALVGLTEAA---------DKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489083979 174 EPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDR 216
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDR 184
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-227 |
2.43e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSP 77
Cdd:PRK10584 3 AENIVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-----SGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTDT-VDLR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIwnevKDRLHDSAVGLSGGQQ 154
Cdd:PRK10584 78 DEEArAKLRaKHVGFVFQSFMLIPtLNALENVELPALLRGESSRQSRNGAKAL-LEQLGL----GKRLDHLPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRlSDRTGFFLEGDLLE 227
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-180 |
3.22e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.50 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQK----------KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYN 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI-----ETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 71 GHNIYSPRTDTV-DLRKEIGMVFQQP----NPfpmsiyenvvyglrlkgiRDK--SILDH--AVESSLKGAsiwnEVKDR 141
Cdd:PRK11308 76 GQDLLKADPEAQkLLRQKIQIVFQNPygslNP------------------RKKvgQILEEplLINTSLSAA----ERREK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 142 LHD--SAVGL------------SGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK11308 134 ALAmmAKVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-204 |
3.39e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.69 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKD-VSLDLYPNEITALIGPSGSGKSTLLrsinrmNDLNPEVTITGSIVYNGHNIYSprTDTVDL 84
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIELRE--LDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFPMSIYENVVYGlrlkgirDKSILDHAVESSLKGASIWNEVKDRLH-------DSAVGLSGGQQQRV 157
Cdd:PRK11174 422 RKHLSWVGQNPQLPHGTLRDNVLLG-------NPDASDEQLQQALENAWVSEFLPLLPQgldtpigDQAAGLSVGQAQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT 541
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-214 |
3.87e-24 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.97 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY--TPQ---HGQVLVDGVDL--AIADPAWLRRQMGVVLQENVLFSR 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENVvyGLRLKGIRDKSILdHAveSSLKGASIWNEVKDRLHDSAVG-----LSGGQQQRVCIARVLATSPRIILLDEP 175
Cdd:TIGR01846 546 SIRDNI--ALCNPGAPFEHVI-HA--AKLAGAHDFISELPQGYNTEVGekganLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190
....*....|....*....|....*....|....*....
gi 489083979 176 TSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICRGRTVIII------AHRLS 653
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
3.97e-24 |
|
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: 96.46 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYNGHNIYSPRTDTVDL- 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFY------------MIVGLVKPDSGKILLDGQDITKLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 -----RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIrDKSILDHAVESSLKGASIwNEVKDRLhdsAVGLSGGQQQRVC 158
Cdd:cd03218 69 mhkraRLGIGYLPQEASIFrKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKK--------DY----TLAIVtrsmqqasrlsDRTGFFLEGDLL 226
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrgigvlitDHnvreTLSIT-----------DRAYIIYEGKVL 212
|
250
....*....|....*..
gi 489083979 227 ECGPTKAMFMNPKRKET 243
Cdd:cd03218 213 AEGTPEEIAANELVRKV 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-208 |
6.35e-24 |
|
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: 95.23 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKK-----TLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHniysprtd 80
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEK---LSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 tvdlrkeIGMVFQQPNPFPMSIYENVVYGLRLkgirDKSILDHAVES-SLKgasiwnevKD--RLHD---SAVG-----L 149
Cdd:cd03250 68 -------IAYVSQEPWIQNGTIRENILFGKPF----DEERYEKVIKAcALE--------PDleILPDgdlTEIGekginL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLL--LKKDYTLAIVTRSMQ 208
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILglLLNNKTRILVTHQLQ 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-180 |
7.04e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNdlNPEVTIT-GSIVYNGHNIysprTD-TVD 83
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MG--HPKYEVTsGSILLDGEDI----LElSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LR--KEIGMVFQQPNPFPmsiyenvvyglrlkGIRDKSILDHAVESSLKGASIWNEVKDRLHDSA--------------- 146
Cdd:COG0396 73 ERarAGIFLAFQYPVEIP--------------GVSVSNFLRTALNARRGEELSAREFLKLLKEKMkelgldedfldryvn 138
|
170 180 190
....*....|....*....|....*....|....
gi 489083979 147 VGLSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:COG0396 139 EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-206 |
9.21e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysprtdTv 82
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI--VGLVKPD---SGRIFLDGEDI------T- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DL------RKEIGMVFQQPNPF-PMSIYENV-----VYGLRLKGIRDKsildhaVESSLKGASIwNEVKDRLhdsAVGLS 150
Cdd:COG1137 69 HLpmhkraRLGIGYLPQEASIFrKLTVEDNIlavleLRKLSKKEREER------LEELLEEFGI-THLRKSK---AYSLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKK--------DY----TLAIVTRS 206
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErgigvlitDHnvreTLGICDRA 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-235 |
9.26e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.74 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 19 KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGSIVYNGHNI--YSPRTDTVDLRKEIGMVFQQPN 96
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 P--FPMSIYENVVYGLRLKGIRDKSILDHAVESsLKGASIWNEVKDRlhdSAVGLSGGQQQRVCIARVLATSPRIILLDE 174
Cdd:PRK13649 96 SqlFEETVLKDVAFGPQNFGVSQEEAEALAREK-LALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 175 PTSALDPisAGKiEETLLLLKKDY----TLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMF 235
Cdd:PRK13649 172 PTAGLDP--KGR-KELMTLFKKLHqsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-235 |
1.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 19 KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGhniYSPRTDTVDLRKEIGMVFQQPNP- 97
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS---TSKQKEIKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 98 -FPMSIYENVVYGLRLKGIRDKSILDHAVES-SLKGASiwnevKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEP 175
Cdd:PRK13643 97 lFEETVLKDVAFGPQNFGIPKEKAEKIAAEKlEMVGLA-----DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 176 TSALDP---ISAGKIEETllLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMF 235
Cdd:PRK13643 172 TAGLDPkarIEMMQLFES--IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-243 |
1.55e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYY-----------NQKKTLKDVSLDLYPNEITALIGPSGSGKST----LLRSINRmndlnpevtiTGS 66
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS----------QGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 67 IVYNGHNIYS-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLkgirdksildHavESSLKGASIWNEVKDR 141
Cdd:PRK15134 342 IWFDGQPLHNlNRRQLLPVRHRIQVVFQDPnsslNP-RLNVLQIIEEGLRV----------H--QPTLSAAQREQQVIAV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 142 LHDsaVGL------------SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSM 207
Cdd:PRK15134 409 MEE--VGLdpetrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAylFISHDL 486
|
250 260 270
....*....|....*....|....*....|....*.
gi 489083979 208 QQASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKET 243
Cdd:PRK15134 487 HVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-237 |
2.47e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.85 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 10 DLSVYYNQK-----KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI---YSPRTDT 81
Cdd:PRK13645 11 NVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL-----IISETGQTIVGDYAIpanLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQP--NPFPMSIYENVVYGLRLKGiRDKSILDHAVESSLKGASIWNEVKDRlhdSAVGLSGGQQQRVCI 159
Cdd:PRK13645 86 KRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYT--LAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMN 237
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-185 |
3.50e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.83 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYS-PRTD 80
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPD---HGEILFDGENIPAmSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAV-----ESSLKGASiwnevkdRLHDSAvgLSGGQQ 154
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHSTVmmkleAVGLRGAA-------KLMPSE--LSGGMA 149
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAG 185
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-176 |
3.57e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVyynqKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI---NRMndlnpevtITGSIVYNGH--NIYSP 77
Cdd:COG1129 254 EVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgaDPA--------DSGEIRLDGKpvRIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RtDTVDL--------RKEIGMVFqqpnpfPMSIYENVVYGlRLKGIRDKSILDHAVESSLkgAsiwNEVKDRLH------ 143
Cdd:COG1129 322 R-DAIRAgiayvpedRKGEGLVL------DLSIRENITLA-SLDRLSRGGLLDRRRERAL--A---EEYIKRLRiktpsp 388
|
170 180 190
....*....|....*....|....*....|....
gi 489083979 144 DSAVG-LSGGQQQRVCIARVLATSPRIILLDEPT 176
Cdd:COG1129 389 EQPVGnLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-238 |
4.01e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVD 83
Cdd:PRK13652 3 LIETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPT---SGSVLIRGEPI--TKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIrDKSILDHAVESSLKGASIwNEVKDRLHDSavgLSGGQQQRVCIAR 161
Cdd:PRK13652 76 VRKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV--TRSMQQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-180 |
4.73e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTE--PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YS 76
Cdd:PRK10247 1 MQEnsPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPT---SGTLLFEGEDIstLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 PRTdtvdLRKEIGMVFQQPNPFPMSIYENVV--YGLRLKGIRDKSILDHAVESSLKgasiwnevKDRLHDSAVGLSGGQQ 154
Cdd:PRK10247 76 PEI----YRQQVSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLERFALP--------DTILTKNIAELSGGEK 143
|
170 180
....*....|....*....|....*.
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-191 |
6.59e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEVTITGSIVYNGHNIYSPRTDTV 82
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLRK---EIGMVFQQPNPFP-MSIYENVVYGlrlkgirdksildhavesSLKGASIWN--------EVKDR--------- 141
Cdd:PRK09984 80 DIRKsraNTGYIFQQFNLVNrLSVLENVLIG------------------ALGSTPFWRtcfswftrEQKQRalqaltrvg 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489083979 142 ----LHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:PRK09984 142 mvhfAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-238 |
6.93e-23 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 94.12 E-value: 6.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPE-----VTITGSIVYNGHNIYspRT 79
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGGgaprgARVTGDVTLNGEPLA--AI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMVFQQPNP-FPMSIYENVVYG----LRLKG---IRDKSILDHAVESSLKGASIWNEVkdrlhdsaVGLSG 151
Cdd:PRK13547 77 DAPRLARLRAVLPQAAQPaFAFSAREIVLLGryphARRAGaltHRDGEIAWQALALAGATALVGRDV--------TTLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 152 GQQQRVCIARVLA---------TSPRIILLDEPTSALDPISAGKIEETLLLLKKDY---TLAIVtRSMQQASRLSDRTGF 219
Cdd:PRK13547 149 GELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWnlgVLAIV-HDPNLAARHADRIAM 227
|
250
....*....|....*....
gi 489083979 220 FLEGDLLECGPTKAMfMNP 238
Cdd:PRK13547 228 LADGAIVAHGAPADV-LTP 245
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-207 |
1.49e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 14 YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMVF 92
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDITRLKNREVPfLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQPNPF-PMSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWNEVKDrlhdSAVGLSGGQQQRVCIARVLATSPRIIL 171
Cdd:PRK10908 86 QDHHLLmDRTVYDNVAIPLIIAGASGDDI-RRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489083979 172 LDEPTSALDpisaGKIEETLLLLKKDYTLAIVTRSM 207
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEFNRVGVTVLM 192
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-235 |
1.91e-22 |
|
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: 92.56 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYY---------NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIY 75
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 76 S-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSavgLS 150
Cdd:TIGR02769 77 QlDRKQRRAFRRDVQLVFQDSpsavNP-RMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLA--IVTRSMQQASRLSDRTGFFLEGDLLEC 228
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAylFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
....*..
gi 489083979 229 GPTKAMF 235
Cdd:TIGR02769 233 CDVAQLL 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
9.55e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSP 77
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLNGQPIadYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTdtvdLRKEIGMVFQQPNPFPMSIYENVVYGL------RLKGIRDKSILDHAVESSlKGASIWnevkdrLHDSAVGLSG 151
Cdd:PRK11160 410 AA----LRQAISVVSQRVHLFSATLRDNLLLAApnasdeALIEVLQQVGLEKLLEDD-KGLNAW------LGEGGRQLSG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 152 GQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT 531
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-191 |
1.05e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 15 YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGsivynghnIYSPRTDTVDLR--KEIGMVF 92
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLK------------VLAG--------VLRPTSGTVRRAggARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQ---PNPFPMSIYENVVYGL--RLKGIRDKSILDHA-VESSLKGASIwnevkDRLHDSAVG-LSGGQQQRVCIARVLAT 165
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGRwaRRGLWRRLTRDDRAaVDDALERVGL-----ADLAGRQLGeLSGGQRQRALLAQGLAQ 136
|
170 180
....*....|....*....|....*.
gi 489083979 166 SPRIILLDEPTSALDPISAGKIEETL 191
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALL 162
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-225 |
1.32e-21 |
|
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: 89.38 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiYSPRtdtvDLR 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRPT---SGEIIFDGHP-WTRK----DLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KeIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIldhavESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLA 164
Cdd:TIGR03740 71 K-IGSLIESPPLYEnLTARENLKVHTTLLGLPDSRI-----DEVLNIVDLTNTGKKKAKQ----FSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEGDL 225
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-252 |
1.48e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIR--DLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPR 78
Cdd:PRK10253 1 MTESVARLRgeQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHI--QH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTVDLRKEIGMVFQQPN-PFPMSIYENVVYGLRLKG---IRDKSILDHAVESSLKGASIwnevKDRLHDSAVGLSGGQQ 154
Cdd:PRK10253 74 YASKEVARRIGLLAQNATtPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI----THLADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL--KKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPtk 232
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-- 227
|
250 260
....*....|....*....|
gi 489083979 233 amfmnPKRKETEDYISGKFG 252
Cdd:PRK10253 228 -----PKEIVTAELIERIYG 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-213 |
2.18e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTVDL 84
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNP--FPMSIYENVVYGLRLKGIRDKSI---LDHAVesSLKGASIWNevkdrlHDSAVGLSGGQQQRVCI 159
Cdd:PRK13638 76 RQQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPEAEItrrVDEAL--TLVDAQHFR------HQPIQCLSHGQKKRVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489083979 160 ARVLATSPRIILLDEPTSALDPisAGKIEetllllkkdyTLAIVTRSMQQASRL 213
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDP--AGRTQ----------MIAIIRRIVAQGNHV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-232 |
2.36e-21 |
|
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: 92.56 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYY-----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSP 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--AGVLEPT---SGEVNVRVGDEWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTDT-VDLR----KEIGMVFQQPNPFP-MSIYENVVYGLRLK-----GIRDKSILDHAVESSLKGASiwnEVKDRLHDSa 146
Cdd:TIGR03269 352 MTKPgPDGRgrakRYIGILHQEYDLYPhRTVLDNLTEAIGLElpdelARMKAVITLKMVGFDEEKAE---EILDKYPDE- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 147 vgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDRTGFFLEGD 224
Cdd:TIGR03269 428 --LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*...
gi 489083979 225 LLECGPTK 232
Cdd:TIGR03269 506 IVKIGDPE 513
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-180 |
2.43e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYY--------NQKKT-LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNI 74
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkHQHQTvLNNVSLSLKSGETVALLGRSGCGKSTLARLL-----VGLESPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 75 YS-PRTDTVDLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSavgL 149
Cdd:PRK10419 77 AKlNRAQRKAFRRDIQMVFQDSisavNP-RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---L 152
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-222 |
2.61e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.78 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTL---KDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTI------------------- 63
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 64 ------------------------------TGSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNPFPMSIYENVVYGlr 111
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDIcdYNLK----DLRNLFSIVSQEPMLFNMSIYENIKFG-- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 112 lkgiRDKSILDHaVESSLKGASIwNEVKDRL---HDSAVG-----LSGGQQQRVCIARVLATSPRIILLDEPTSALDPIS 183
Cdd:PTZ00265 1320 ----KEDATRED-VKRACKFAAI-DEFIESLpnkYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489083979 184 AGKIEETLLLLKKDYTLAIVT-----RSMQQASRL-----SDRTGFFLE 222
Cdd:PTZ00265 1394 EKLIEKTIVDIKDKADKTIITiahriASIKRSDKIvvfnnPDRTGSFVQ 1442
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
3.02e-21 |
|
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: 87.49 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVyynqKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGH--NIYSPRtD 80
Cdd:cd03215 2 EPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL--FGLRPPA---SGEITLDGKpvTRRSPR-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDL--------RKEIGMVFQqpnpfpMSIYENVVYGLRlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGG 152
Cdd:cd03215 72 AIRAgiayvpedRKREGLVLD------LSVAENIALSSL-------------------------------------LSGG 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 153 QQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDyTLAI--VTRSMQQASRLSDR 216
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVllISSELDELLGLCDR 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-238 |
3.78e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYnqkKT-------LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHN 73
Cdd:PRK09473 8 QADALLDVKDLRVTF---STpdgdvtaVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 74 IYS-PRTDTVDLR-KEIGMVFQQP----NPFpMSIYENVVYGLRL-KGIrDKSildHAVESSLK--GASIWNEVKDRLHD 144
Cdd:PRK09473 83 ILNlPEKELNKLRaEQISMIFQDPmtslNPY-MRVGEQLMEVLMLhKGM-SKA---EAFEESVRmlDAVKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 145 SAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGFFLE 222
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGICDKVLVMYA 237
|
250
....*....|....*.
gi 489083979 223 GDLLECGPTKAMFMNP 238
Cdd:PRK09473 238 GRTMEYGNARDVFYQP 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-180 |
4.11e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSP--RTDTVD 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPA---AGTIKLDGGDIDDPdvAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMvfqqpNPFpMSIYENVVYGLRLKGIRDKSIlDHAVESSlkgasiwnEVKDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK13539 78 LGHRNAM-----KPA-LTVAENLEFWAAFLGGEELDI-AAALEAV--------GLAPLAHLPFGYLSAGQKRRVALARLL 142
|
170
....*....|....*..
gi 489083979 164 ATSPRIILLDEPTSALD 180
Cdd:PRK13539 143 VSNRPIWILDEPTAALD 159
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-216 |
4.20e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYNGHNIYSPRTDTVDLR 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR------------LLAGLETPSAGELLAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVvyGLRLKG-IRDKSIldHAVESSlkGASiwnevkDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNV--GLGLKGqWRDAAL--QALAAV--GLA------DRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 164 ATSPRIILLDEPTSALDPISagKIEETLLL----LKKDYTLAIVTRSMQQASRLSDR 216
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALT--RIEMQDLIeslwQQHGFTVLLVTHDVSEAVAMADR 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-203 |
7.18e-21 |
|
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: 87.08 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDTVD 83
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDIST--IPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVvyglrlkgirdkSILDHAVESSLKGASiwnevkdRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNL------------DPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTI 180
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-232 |
7.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.61 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQK---KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSprTDT 81
Cdd:PRK13642 4 ILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTA--ENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQP-NPF-PMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIwnEVKDRlhdSAVGLSGGQQQRVCI 159
Cdd:PRK13642 77 WNLRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTR---EPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRlSDRTGFFLEGDLL-ECGPTK 232
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVlsITHDLDEAAS-SDRILVMKAGEIIkEAAPSE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-229 |
8.60e-21 |
|
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: 91.02 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPevtITGSIVYN--------------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 71 --------GHNIYSPRTD--------TVDLRKEIGMVFQQPnpFPM----SIYENVVYGLRLKGIRDKSILDHAVEsslk 130
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDfwnlsdklRRRIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAVD---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 131 gasIWNEVK--DRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVTRSM- 207
Cdd:TIGR03269 152 ---LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHw 228
|
250 260
....*....|....*....|...
gi 489083979 208 -QQASRLSDRTGFFLEGDLLECG 229
Cdd:TIGR03269 229 pEVIEDLSDKAIWLENGEIKEEG 251
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-213 |
1.16e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTePILQIRDLSVYY----NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDL----NPEvtiTGSIVYNGH 72
Cdd:PRK10535 1 MT-ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL------MNILgcldKPT---SGTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 73 NIYSPRTDTV-DLRKE-IGMVFQQPNPFP-MSIYENV----VYGlrlkGIRDKSILDHAVESSLKGAsiwneVKDRLHDS 145
Cdd:PRK10535 71 DVATLDADALaQLRREhFGFIFQRYHLLShLTAAQNVevpaVYA----GLERKQRLLRAQELLQRLG-----LEDRVEYQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 146 AVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAgkiEETLLLLK----KDYTLAIVTRSMQ---QASRL 213
Cdd:PRK10535 142 PSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG---EEVMAILHqlrdRGHTVIIVTHDPQvaaQAERV 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-203 |
1.23e-20 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 90.58 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndlnpeV----TITGSIVYNGHNIYS-PR 78
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL---------VgvwpPTAGSVRLDGADLSQwDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDtvdLRKEIGMVFQQPNPFPMSIYENVVyglRLKGIRDKSILDHAvesSLKGAsiwNEVKDRL---HDSAVG-----LS 150
Cdd:COG4618 402 EE---LGRHIGYLPQDVELFDGTIAENIA---RFGDADPEKVVAAA---KLAGV---HEMILRLpdgYDTRIGeggarLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIV 203
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVV 522
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-216 |
1.51e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 15 YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGhniySPRTDTVDL-RKEIGMVFQ 93
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT--SPD---AGKITVLG----VPVPARARLaRARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 94 QPNPFP-MSIYEN-VVYGlRLKGIRDKSIlDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLATSPRIIL 171
Cdd:PRK13536 122 FDNLDLeFTVRENlLVFG-RYFGMSTREI-EAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489083979 172 LDEPTSALDPISAGKIEETL-LLLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-252 |
2.39e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSprTDTVD 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTPT---AGTVLVAGDDVEA--LSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPN-PFPMSIYENVVYGL-----RLKGIRDKSilDHAVESSLKGASIwnevkDRLHDSAV-GLSGGQQQR 156
Cdd:PRK09536 75 ASRRVASVPQDTSlSFEFDVRQVVEMGRtphrsRFDTWTETD--RAAVERAMERTGV-----AQFADRPVtSLSGGERQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT-RSMQQASRLSDRTGFFLEGDLLECGPtkamf 235
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDLAARYCDELVLLADGRVRAAGP----- 222
|
250
....*....|....*..
gi 489083979 236 mnPKRKETEDYISGKFG 252
Cdd:PRK09536 223 --PADVLTADTLRAAFD 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-180 |
4.13e-20 |
|
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: 88.94 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYspRTDTVDLRKEIGMVFQQPN 96
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----VGIWPPTSGSVRLDGADLK--QWDRETFGKHIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFPMSIYENVVyglRL-KGIRDKSILDHAVessLKGAsiwNEVKDRL---HDSAVG-----LSGGQQQRVCIARVLATSP 167
Cdd:TIGR01842 403 LFPGTVAENIA---RFgENADPEKIIEAAK---LAGV---HELILRLpdgYDTVIGpggatLSGGQRQRIALARALYGDP 473
|
170
....*....|...
gi 489083979 168 RIILLDEPTSALD 180
Cdd:TIGR01842 474 KLVVLDEPNSNLD 486
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-180 |
1.69e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.05 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVynghNIYSPRtdtvd 83
Cdd:PRK11650 4 LKLQAVRkSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSgEIWIGGRVV----NELEPA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 lRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIrDKSILDHAVEsslKGASIWnEVKDRLHDSAVGLSGGQQQRVCIARV 162
Cdd:PRK11650 75 -DRDIAMVFQNYALYPhMSVRENMAYGLKIRGM-PKAEIEERVA---EAARIL-ELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 489083979 163 LATSPRIILLDEPTSALD 180
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-192 |
2.80e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVY-YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGsivynghnIYSPRTDTVDL 84
Cdd:COG4178 363 LALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLR------------AIAG--------LWPYGSGRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVF--QQPNpFPM-SIYENVVYGLRlkgirDKSILDHAVESSLKgasiwnEV-----KDRLHDSAV---GLSGGQ 153
Cdd:COG4178 423 PAGARVLFlpQRPY-LPLgTLREALLYPAT-----AEAFSDAELREALE------AVglghlAERLDEEADwdqVLSLGE 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLL 192
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-192 |
3.40e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYnGHNIysprtdtvd 83
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPD---SGTVKL-GETV--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 lrkEIGMVFQQPNPFP--MSIYENVVYGLRlkGIRDKSILDHaVESSL-KGASIWNEVKDrlhdsavgLSGGQQQRVCIA 160
Cdd:COG0488 379 ---KIGYFDQHQEELDpdKTVLDELRDGAP--GGTEQEVRGY-LGRFLfSGDDAFKPVGV--------LSGGEKARLALA 444
|
170 180 190
....*....|....*....|....*....|..
gi 489083979 161 RVLATSPRIILLDEPTSALDPISAGKIEETLL 192
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALD 476
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-180 |
3.99e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 8 IRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGhniysprtdtvDLRke 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEPD---SGEVSIPK-----------GLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 88 IGMVFQQPNPFP-MSIYENVVYGLR--LKGIRDKSILDHAVESSLKGASIWNEVKDRL---------------------- 142
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGDAelRALEAELEELEAKLAEPDEDLERLAELQEEFealggweaearaeeilsglgfp 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489083979 143 ---HDSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:COG0488 143 eedLDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
4.34e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNI--YSPR 78
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML-----LGLTHPDAGSISLCGEPVpsRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TdtvdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSIlDHAVESSLKGASIWNEVkdrlhDSAVG-LSGGQQQR 156
Cdd:PRK13537 78 A-----RQRVGVVPQFDNLDPdFTVRENLLVFGRYFGLSAAAA-RALVPPLLEFAKLENKA-----DAKVGeLSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRsLLARGKTILLTTHFMEEAERLCDR 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-204 |
5.36e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYSPRtdtvdLRKEIGMVFQQP 95
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPIDAKE-----MRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 NPFPM-SIYENVVYG--LRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAV--GLSGGQQQRVCIARVLATSPRII 170
Cdd:TIGR00955 109 LFIPTlTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....
gi 489083979 171 LLDEPTSALDPISAGKIEETLLLLKKDYTLAIVT 204
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
1.51e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTD 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--YKPT---GGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVdLRKEIGMVFQQPNPF-PMSIYEN--VVYGLRLK-----GIRDKSILDHAVESSLKGASIWNEV---KDRLHDSAVGL 149
Cdd:PRK11300 76 QI-ARMGVVRTFQHVRLFrEMTVIENllVAQHQQLKtglfsGLLKTPAFRRAESEALDRAATWLERvglLEHANRQAGNL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDR 216
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVllIEHDMKLVMGISDR 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-214 |
1.58e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI--YSPRTdtv 82
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLT---EGEIRLDGRPLssLSHSV--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 dLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiRDksILDHAVESSLKG---ASIWNEVKDRLHdSAVG-----LSGGQQ 154
Cdd:PRK10790 413 -LRQGVAMVQQDPVVLADTFLANVTLG------RD--ISEEQVWQALETvqlAELARSLPDGLY-TPLGeqgnnLSVGQK 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 155 QRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS 214
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI------AHRLS 536
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-204 |
4.37e-18 |
|
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: 78.26 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIvynghniysprtdTVDLR 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEP---DEGIV-------------TWGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGmVFQQpnpfpmsiyenvvyglrlkgirdksildhavesslkgasiwnevkdrlhdsavgLSGGQQQRVCIARVLAT 165
Cdd:cd03221 63 VKIG-YFEQ------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489083979 166 SPRIILLDEPTSALDPISAGKIEETLlllkKDY--TLAIVT 204
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEAL----KEYpgTVILVS 124
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-237 |
9.67e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 24 VSLDLYPNEITALIGPSGSGKSTLLrSInrMNDLNPEVTitGSIVYNGHNIyspRTDTVDLRKEIGMVFQQPNPFP-MSI 102
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTL-SI--LTGLLPPTS--GTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFHhLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 103 YENVVYGLRLKGiRDKSILDHAVESSLKGASIWNEVKDRLHDsavgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPI 182
Cdd:TIGR01257 1021 AEHILFYAQLKG-RSWEEAQLEMEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 183 SAGKIEETLLLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLeCGPTKAMFMN 237
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLY-CSGTPLFLKN 1149
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-214 |
1.10e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvDLRK 86
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD--SWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 87 EIGMVFQQPNPFPMSIYENVVYGlRLKGIRDKsildhaVESSLKGASIWNEVKdRL---HDSAVG-----LSGGQQQRVC 158
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNIALG-RPDATQQE------IEHVARLASVHDDIL-RLpqgYDTEVGergvmLSGGQKQRIS 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIvtrsmqQASRLS 214
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVII------SAHRLS 511
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
16-216 |
1.25e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKD----VSLDLYPNEITALIGPSGSGKSTLlrsINRMNDL-NPEvtiTGSIVYNGHNIYSPRTD---TVDLRKe 87
Cdd:PRK11144 5 NFKQQLGDlcltVNLTLPAQGITAIFGRSGAGKTSL---INAISGLtRPQ---KGRIVLNGRVLFDAEKGiclPPEKRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 88 IGMVFQQPNPFP-MSIYENVVYGLRLKgirDKSILDHAV-----ESSLkgasiwnevkDRLHDSavgLSGGQQQRVCIAR 161
Cdd:PRK11144 78 IGYVFQDARLFPhYKVRGNLRYGMAKS---MVAQFDKIVallgiEPLL----------DRYPGS---LSGGEKQRVAIGR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 162 VLATSPRIILLDEPTSALD-PisaGKIEetlLL-----LKKDYTLAI--VTRSMQQASRLSDR 216
Cdd:PRK11144 142 ALLTAPELLLMDEPLASLDlP---RKRE---LLpylerLAREINIPIlyVSHSLDEILRLADR 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-243 |
1.31e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYyNQKKTLKDVSLDLYPNEITALIGPSGSGKStlLRSINRMNDLNPEVTIT-GSIVYNGHNIySPRtdtvDL 84
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTaGRVLLDGKPV-APC----AL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 R-KEIGMVFQQP----NPFpMSIYENVVYGLRLKGI-RDKSILDHAVEsslkgASIWNEVKDRLHDSAVGLSGGQQQRVC 158
Cdd:PRK10418 77 RgRKIATIMQNPrsafNPL-HTMHTHARETCLALGKpADDATLTAALE-----AVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETL--LLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPTKAMFM 236
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
....*..
gi 489083979 237 NPKRKET 243
Cdd:PRK10418 231 APKHAVT 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-241 |
1.60e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndlnpeVTI----TGSIVYNGHNIySPRTD 80
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV---------VGIvprdAGNIIIDDEDI-SLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRlkgIRDksilDHAVESSLKGAsiwNEVKDRLHDSAV------GLSGGQ 153
Cdd:PRK10895 73 HARARRGIGYLPQEASIFRrLSVYDNLMAVLQ---IRD----DLSAEQREDRA---NELMEEFHIEHLrdsmgqSLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLkKDYTLA--IVTRSMQQASRLSDRTGFFLEGDLLECGPT 231
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGvlITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
250
....*....|
gi 489083979 232 KAMFMNPKRK 241
Cdd:PRK10895 222 TEILQDEHVK 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-213 |
1.98e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI-NRMNDLNpevtITGSIVYNGhniyspRTDTVDLR 85
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNN----FTGTILANN------RKPTKQIL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYG--LRLKGI---RDKSILDHAVESSLKGASIWNEVkdrLHDSAV-GLSGGQQQRVC 158
Cdd:PLN03211 140 KRTGFVTQDDILYPhLTVRETLVFCslLRLPKSltkQEKILVAESVISELGLTKCENTI---IGNSFIrGISGGERKRVS 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 159 IARVLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTlaIVTRSMQQASRL 213
Cdd:PLN03211 217 IAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGsLAQKGKT--IVTSMHQPSSRV 270
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-180 |
4.06e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVyynqKKTLKDVSLDLYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEvtiTGSIVYNGHNI--YSPRtdtvD 83
Cdd:COG4138 1 LQLNDVAV----AGRLGPISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLPG---QGEILLNGRPLsdWSAA----E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQ-PNPFPMSIYEnvvYgLRLKGirdksildHAVESSLKGASIWNEV------KDRLHDSAVGLSGGQQQR 156
Cdd:COG4138 67 LARHRAYLSQQqSPPFAMPVFQ---Y-LALHQ--------PAGASSEAVEQLLAQLaealglEDKLSRPLTQLSGGEWQR 134
|
170 180 190
....*....|....*....|....*....|.
gi 489083979 157 VCIARVL-----ATSP--RIILLDEPTSALD 180
Cdd:COG4138 135 VRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-208 |
5.59e-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: 76.99 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 20 TLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVDLRKEIGMVF--QQPNP 97
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 98 FPMSIYENVVYGLRLKGIRDKSILDHAV---ESSLKGASIWNEVKDRlhdsAVGLSGGQQQRVCIARVLATSPRIILLDE 174
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSlqpDIDLLPFGDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 489083979 175 PTSALD-PISAGKIEETLLLLKKD--YTLAIVTRSMQ 208
Cdd:cd03290 167 PFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-245 |
6.31e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTL---KDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN-GHNIysprtDT 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINdSHNL-----KD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDL---RKEIGMVFQQPNPFPMSIYENVVYGL------------------------------RLKGIRDKSILDHAVESS 128
Cdd:PTZ00265 453 INLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 129 --LKGASIWNEVKDR----------LHD---------------SAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDP 181
Cdd:PTZ00265 533 elIEMRKNYQTIKDSevvdvskkvlIHDfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 182 ISAGKIEETLLLLKKD---YTLAIVTR--SMQQASR---LSDR-TGFFLEGDLLECGPTKAMFMNPKRKETED 245
Cdd:PTZ00265 613 KSEYLVQKTINNLKGNenrITIIIAHRlsTIRYANTifvLSNReRGSTVDVDIIGEDPTKDNKENNNKNNKDD 685
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-184 |
6.51e-17 |
|
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: 76.53 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQQP 95
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIPY---KEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 NPFP-MSIYENVVYGLRLKGirdksildhavesslkgasiwnevkdrlHDSAVGLSGGQQQRVCIARVLATSPRIILLDE 174
Cdd:cd03233 93 VHFPtLTVRETLDFALRCKG----------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170
....*....|
gi 489083979 175 PTSALDPISA 184
Cdd:cd03233 145 STRGLDSSTA 154
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-235 |
6.89e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSIVYNG--HNI-- 74
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQAlqKNLva 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 75 YSPRTDTVDLRkeigmvfqqpnpFPMsIYENVV----YG----LRLKGIRDKSILDHAVESSlkgasiwnEVKDRLHDSA 146
Cdd:PRK15056 82 YVPQSEEVDWS------------FPV-LVEDVVmmgrYGhmgwLRRAKKRDRQIVTAALARV--------DMVEFRHRQI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 147 VGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTgFFLEGDL 225
Cdd:PRK15056 141 GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYT-VMVKGTV 219
|
250
....*....|
gi 489083979 226 LECGPTKAMF 235
Cdd:PRK15056 220 LASGPTETTF 229
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-238 |
1.57e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.64 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQK----KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGS-IVYNGHNI--YS 76
Cdd:COG4170 2 PLLDIRNLTIEIDTPqgrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTADrFRWNGIDLlkLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 PRTDTVDLRKEIGMVFQQPNPF--PMsiyenvvyglrlkgirdKSILDHAVES----SLKGaSIWNEVKDR-------LH 143
Cdd:COG4170 80 PRERRKIIGREIAMIFQEPSSCldPS-----------------AKIGDQLIEAipswTFKG-KWWQRFKWRkkraielLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 144 dsAVG--------------LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSM 207
Cdd:COG4170 142 --RVGikdhkdimnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDL 219
|
250 260 270
....*....|....*....|....*....|.
gi 489083979 208 QQASRLSDRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:COG4170 220 ESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-180 |
2.00e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVY-YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNI--YSPRT 79
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL--RPPA---SGSIRLDGEDItgLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 -----------DtvdlRKEIGMVfqqPNpfpMSIYENVVYG------------LRLKGIRDKSilDHAVES-SLKGASIW 135
Cdd:COG3845 330 rrrlgvayipeD----RLGRGLV---PD---MSVAENLILGryrrppfsrggfLDRKAIRAFA--EELIEEfDVRTPGPD 397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489083979 136 NEVKdrlhdsavGLSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:COG3845 398 TPAR--------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-191 |
2.12e-16 |
|
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: 74.97 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSI-NRMNDlnpeVTITGSIVYNGhniySPR 78
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTA----GVITGEILING----RPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTvdLRKEIGMVFQQPNPFPMSiyenvvyglrlkgirdksildhavesslkgasiwnEVKDRLHDSAV--GLSGGQQQR 156
Cdd:cd03232 74 DKN--FQRSTGYVEQQDVHSPNL-----------------------------------TVREALRFSALlrGLSVEQRKR 116
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-191 |
5.45e-16 |
|
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: 75.28 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKT--LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSivynghniyspRTDTVD 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNavLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGV-----------SWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 L---RKEIGMVFQQPNPFPMSIYENV-VYGLRlkgiRDKSILDHAVESSLKgaSIWNEVKDRLH----DSAVGLSGGQQQ 155
Cdd:cd03289 72 LqkwRKAFGVIPQKVFIFSGTFRKNLdPYGKW----SDEEIWKVAEEVGLK--SVIEQFPGQLDfvlvDGGCVLSHGHKQ 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 489083979 156 RVCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL 181
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-252 |
1.23e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYY---------NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHN 73
Cdd:PRK15112 2 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPT---SGELLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 74 I----YSPRTdtvdlrKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIwnevkdrLHDS 145
Cdd:PRK15112 77 LhfgdYSYRS------QRIRMIFQDPstslNP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL-------LPDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 146 AV----GLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDRTGF 219
Cdd:PRK15112 143 ASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYiyVTQHLGMMKHISDQVLV 222
|
250 260 270
....*....|....*....|....*....|...
gi 489083979 220 FLEGDLLECGPTKAMFMNPKRKETEDYISGKFG 252
Cdd:PRK15112 223 MHQGEVVERGSTADVLASPLHELTKRLIAGHFG 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-179 |
1.26e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiYSPRTD 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNIN-YNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQPNPF-PMSIYENVVYG-LRLKGIRDKSILDHAvESSLKGASIWNEV--KDRLHDSAVGLSGGQQQR 156
Cdd:PRK09700 75 KLAAQLGIGIIYQELSVIdELTVLENLYIGrHLTKKVCGVNIIDWR-EMRVRAAMMLLRVglKVDLDEKVANLSISHKQM 153
|
170 180
....*....|....*....|...
gi 489083979 157 VCIARVLATSPRIILLDEPTSAL 179
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-191 |
1.71e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.80 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY-NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmnDLNPevtitgsiVYNGhNIYSPRtdtvdl 84
Cdd:cd03223 1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLWP--------WGSG-RIGMPE------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNpFPmsiyenvvyglrlkgirdksildhavESSLKGASI--WNEVkdrlhdsavgLSGGQQQRVCIARV 162
Cdd:cd03223 63 GEDLLFLPQRPY-LP--------------------------LGTLREQLIypWDDV----------LSGGEQQRLAFARL 105
|
170 180
....*....|....*....|....*....
gi 489083979 163 LATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-180 |
2.46e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSprTDT 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPLES--WSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQ-PNPFPMSIYENVVYG-------LRLKGIRDKSILDHAVesSLKGASiwnEVKDRLHDSavgLSGGQ 153
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLK---PLAHRLVDS---LSGGE 152
|
170 180
....*....|....*....|....*..
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-229 |
2.51e-15 |
|
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: 72.57 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGsivynghnIYSPRTDTVDLRK------EIGMVFqQ 94
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLR------------LLAG--------IYPPDSGTVTVRGrvssllGLGGGF-N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 95 PNpfpMSIYENVVYGLRLKGIRDKSILDHAVEsslkgasIW--NEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILL 172
Cdd:cd03220 97 PE---LTGRENIYLNGRLLGLSRKEIDEKIDE-------IIefSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 173 DEPTSALDPI----SAGKIEEtllLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECG 229
Cdd:cd03220 167 DEVLAVGDAAfqekCQRRLRE---LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-232 |
2.87e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEpILQIRDLSVYY---------------NQKKT-------LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLN 58
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllRRRRTrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 59 PEvtiTGSIVYNGhNIYSPrtdtvdLrkEIGMVFqQPNpfpMSIYENV-----VYGLRLKGIRDKsiLDHAVESSlkgas 133
Cdd:COG1134 78 PT---SGRVEVNG-RVSAL------L--ELGAGF-HPE---LTGRENIylngrLLGLSRKEIDEK--FDEIVEFA----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 134 iwnEVKDRLhDSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALDPI----SAGKIEEtllLLKKDYTLAIVTRSMQ 208
Cdd:COG1134 135 ---ELGDFI-DQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE---LRESGRTVIFVSHSMG 207
|
250 260
....*....|....*....|....*
gi 489083979 209 QASRLSDRtGFFLE-GDLLECGPTK 232
Cdd:COG1134 208 AVRRLCDR-AIWLEkGRLVMDGDPE 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-244 |
3.47e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKK----TLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpeVTITGSIVYNGHNIYSP 77
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRL------LEQAGGLVQCDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 78 RTDTV-DLRK------------EIGMVFQQP----NP-FPMSiyENVVYGLRL-KGIRDKSILDHAvESSLKGASIwNEV 138
Cdd:PRK10261 83 RSRQViELSEqsaaqmrhvrgaDMAMIFQEPmtslNPvFTVG--EQIAESIRLhQGASREEAMVEA-KRMLDQVRI-PEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 139 KDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAI--VTRSMQQASRLSDR 216
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEIADR 238
|
250 260
....*....|....*....|....*...
gi 489083979 217 TGFFLEGDLLECGPTKAMFMNPKRKETE 244
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-231 |
3.69e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNiYSPRTDTVD 83
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-----VPPDSGTLEIGGNP-CARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRlKGIRDKSILDH---AVESSLKgasiwnevkdrLHDSAVGLSGGQQQRVCI 159
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPnLSVKENILFGLP-KRQASMQKMKQllaALGCQLD-----------LDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISA----GKIEEtllLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPT 231
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETerlfSRIRE---LLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-216 |
5.01e-15 |
|
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: 71.98 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 15 YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGhniYSPRTDTVDLRKEIGMVFQQ 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPT---SGEVRVAG---LVPWKRRKKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 95 PNPF-----PMSIYENVVYGLRLKGIRDKSILDHAVESSlkgasiwnEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRI 169
Cdd:cd03267 103 KTQLwwdlpVIDSFYLLAAIYDLPPARFKKRLDELSELL--------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489083979 170 ILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDR 216
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARR 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-224 |
6.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 14 YYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPrTDTVDLRKEIGMVFQ 93
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQ---KGKVLVSGIDTGDF-SKLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 94 QPNP--FPMSIYENVVYG---LRLKGIRDKSILDHAV-ESSLKgasiwnevKDRlHDSAVGLSGGQQQRVCIARVLATSP 167
Cdd:PRK13644 85 NPETqfVGRTVEEDLAFGpenLCLPPIEIRKRVDRALaEIGLE--------KYR-HRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 168 RIILLDEPTSALDPISAGKIEETLLLL-KKDYTLAIVTRSMQQ---ASRL--SDRTGFFLEGD 224
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEElhdADRIivMDRGKIVLEGE 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-191 |
6.15e-15 |
|
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: 74.18 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ--KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGsIVYNGHNIYSprtdtvd 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG-VSWNSVTLQT------- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKgirDKSILDHAVESSLKgaSIWNEVKDRLH----DSAVGLSGGQQQRVCI 159
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLDPYEQWS---DEEIWKVAEEVGLK--SVIEQFPDKLDfvlvDGGYVLSNGHKQLMCL 1364
|
170 180 190
....*....|....*....|....*....|..
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-247 |
6.69e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.91 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQK----KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITgsivynghniySPRT 79
Cdd:PRK15093 2 PLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTAD-----------RMRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDL--------RKEIG----MVFQQP----NP-----------FPMSIYENVVYGlRLKGIRDKSI-LDHAVesSLKg 131
Cdd:PRK15093 71 DDIDLlrlsprerRKLVGhnvsMIFQEPqsclDPservgrqlmqnIPGWTYKGRWWQ-RFGWRKRRAIeLLHRV--GIK- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 132 asiwnEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD--YTLAIVTRSMQQ 209
Cdd:PRK15093 147 -----DHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQM 221
|
250 260 270
....*....|....*....|....*....|....*...
gi 489083979 210 ASRLSDRTGFFLEGDLLECGPTKAMFMNPKRKETEDYI 247
Cdd:PRK15093 222 LSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-179 |
9.39e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGH--NIYSPRT 79
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD-----AGSILYLGKevTFNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTvdlRKEIGMVFQQPNPFP-MSIYENVVYGlrlkgiRDKsildhaveSSLKGASIWNEV---KDRL-------HDS--A 146
Cdd:PRK10762 76 SQ---EAGIGIIHQELNLIPqLTIAENIFLG------REF--------VNRFGRIDWKKMyaeADKLlarlnlrFSSdkL 138
|
170 180 190
....*....|....*....|....*....|....
gi 489083979 147 VG-LSGGQQQRVCIARVLATSPRIILLDEPTSAL 179
Cdd:PRK10762 139 VGeLSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-212 |
1.17e-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: 73.41 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVdlrkeigmvfqqpnpFPM 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSGRISFSPQTSWI---------------MPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENVVYGLRLKGIRDKSILDhAVESSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:TIGR01271 502 TIKDNIIFGLSYDEYRYTSVIK-ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 489083979 181 PISAGKI-EETLLLLKKDYTLAIVTRSMQQASR 212
Cdd:TIGR01271 581 VVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-197 |
2.25e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTITGSIVYNG-----HNIy 75
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV---LSGVYPHGTYEGEIIFEGeelqaSNI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 76 sprTDTVdlRKEIGMVFQQ----PNpfpMSIYENVVYG--LRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDsavgL 149
Cdd:PRK13549 77 ---RDTE--RAGIAIIHQElalvKE---LSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN----L 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALdpiSAGKIeETLLLLKKD 197
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASL---TESET-AVLLDIIRD 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-204 |
2.35e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI-NRMNDLnpevtitgsivynghniysPRTDTVDLrkeigmvfqQ 94
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLaGALKGT-------------------PVAGCVDV---------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 95 PNPFPmsiyenvvyglrlkgiRDKSILDHAvessLKGASIwNEVKDRLHdsAVG-------------LSGGQQQRVCIAR 161
Cdd:COG2401 93 DNQFG----------------REASLIDAI----GRKGDF-KDAVELLN--AVGlsdavlwlrrfkeLSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489083979 162 VLATSPRIILLDEPTSALDPISAGKIEETLLLL--KKDYTLAIVT 204
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVAT 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-223 |
2.71e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGhniySPR--T 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILS--GNYQPD---AGSILIDG----QEMrfA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVD-LRKEIGMVFQQPNPFP-MSIYENVVYGlRLK---GIRDKSILDHAVESSLKGASIwnevkDRLHDSAVG-LSGGQ 153
Cdd:PRK11288 72 STTAaLAAGVAIIYQELHLVPeMTVAENLYLG-QLPhkgGIVNRRLLNYEAREQLEHLGV-----DIDPDTPLKyLSIGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALdpiSAGKIEETLLL---LKKDYTLAI-VTRSMQQASRLSDRTGFFLEG 223
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSL---SAREIEQLFRVireLRAEGRVILyVSHRMEEIFALCDAITVFKDG 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-181 |
2.91e-14 |
|
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: 69.31 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDtvdLR 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRPD---SGEVRWNGTPLAEQRDE---PH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVESSLKGASiwnevkdrlHDSAVGLSGGQQQRVCIARVLA 164
Cdd:TIGR01189 73 ENILYLGHLPGLKPeLSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE---------DLPAAQLSAGQQRRLALARLWL 143
|
170
....*....|....*..
gi 489083979 165 TSPRIILLDEPTSALDP 181
Cdd:TIGR01189 144 SRRPLWILDEPTTALDK 160
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-184 |
3.23e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSvyynqKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTitGSIVYNGHNIyspRTDTVD 83
Cdd:PRK15439 267 PVLTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAET---LYGLRPARG--GRIMLNGKEI---NALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVF-----QQPNPF-PMSIYENVV------YGLRLKGIRDKSILD---HAVESSLKGAsiwnevkdrlhDSAV- 147
Cdd:PRK15439 334 QRLARGLVYlpedrQSSGLYlDAPLAWNVCalthnrRGFWIKPARENAVLEryrRALNIKFNHA-----------EQAAr 402
|
170 180 190
....*....|....*....|....*....|....*..
gi 489083979 148 GLSGGQQQRVCIARVLATSPRIILLDEPTSALDpISA 184
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-VSA 438
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-244 |
1.80e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT----LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLnPEVTITGSIVYNGHNI--YSPR 78
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGQDLqrISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 TDTVDLRKEIGMVFQQP----NPFPMSIYEnVVYGLRL-KGIRDKSILDHAVESsLKGASIwNEVKDRLHDSAVGLSGGQ 153
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPmtslNPCYTVGFQ-IMEAIKVhQGGNKKTRRQRAIDL-LNQVGI-PDPASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLL--KKDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECGPT 231
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250
....*....|...
gi 489083979 232 KAMFMNPKRKETE 244
Cdd:PRK11022 239 HDIFRAPRHPYTQ 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-180 |
2.18e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvd 83
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAPD---EGVIKRNGK----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRkeIGMVFQQPN---PFPMSiyenVVYGLRLK-GIRDKSILdhaveSSLKGASiwnevKDRLHDSAV-GLSGGQQQRVC 158
Cdd:PRK09544 67 LR--IGYVPQKLYldtTLPLT----VNRFLRLRpGTKKEDIL-----PALKRVQ-----AGHLIDAPMqKLSGGETQRVL 130
|
170 180
....*....|....*....|..
gi 489083979 159 IARVLATSPRIILLDEPTSALD 180
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-191 |
2.98e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 66.36 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDtvdLR 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL--SPPL---AGRVLLNGGPLDFQRDS---IA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KEIGMVFQQPN-PFPMSIYENVVYGLRLKGirDKSILDHAVESSLKGasiwnevkdrLHDSAVG-LSGGQQQRVCIARVL 163
Cdd:cd03231 73 RGLLYLGHAPGiKTTLSVLENLRFWHADHS--DEQVEEALARVGLNG----------FEDRPVAqLSAGQQRRVALARLL 140
|
170 180
....*....|....*....|....*...
gi 489083979 164 ATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-179 |
4.77e-13 |
|
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: 67.93 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTITGSIVYNGHNIYSPRTDTVDl 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKI---LSGVYPHGTWDGEIYWSGSPLKASNIRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQPNPFP-MSIYENVVYG--LRLKGIRDksildHAVESSLKGASIWNEVK-DRLHDS-AVG-LSGGQQQRVC 158
Cdd:TIGR02633 77 RAGIVIIHQELTLVPeLSVAENIFLGneITLPGGRM-----AYNAMYLRAKNLLRELQlDADNVTrPVGdYGGGQQQLVE 151
|
170 180
....*....|....*....|.
gi 489083979 159 IARVLATSPRIILLDEPTSAL 179
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSL 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-238 |
5.67e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNPF 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREIgaYGLR----ELRRQFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 99 PMSIYENV----------VY-GLRLKGIRDKsildhaVESSLKGasiwneVKDRLHDSAVGLSGGQQQRVCIAR-VLATS 166
Cdd:PTZ00243 1397 DGTVRQNVdpfleassaeVWaALELVGLRER------VASESEG------IDSRVLEGGSNYSVGQRQLMCMARaLLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 167 PRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS-----DRTGFFLEGDLLECGPTKAMFMNP 238
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITI------AHRLHtvaqyDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6-180 |
9.50e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVyynqKKTLKDVSLDLYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEvtiTGSIVYNGHNI--YSPRtdtvD 83
Cdd:PRK03695 1 MQLNDVAV----STRLGPLSAEVRAGEILHLVGPNGAGKSTLL---ARMAGLLPG---SGSIQFAGQPLeaWSAA----E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNP-FPMSIYEnvvY-GLRLKGIRDKSILDHAVE---SSLKgasiwneVKDRLHDSAVGLSGGQQQRVC 158
Cdd:PRK03695 67 LARHRAYLSQQQTPpFAMPVFQ---YlTLHQPDKTRTEAVASALNevaEALG-------LDDKLGRSVNQLSGGEWQRVR 136
|
170 180
....*....|....*....|....*....
gi 489083979 159 IARV-LATSPRI------ILLDEPTSALD 180
Cdd:PRK03695 137 LAAVvLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-192 |
1.17e-12 |
|
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: 66.88 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNghniysprtDTVDL 84
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ-----EQPDSGTIEIG---------ETVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 rkeiGMVFQQ-----PNPfpmSIYENVVYGLRLKGIRDKSILDHAVESS--LKGASIWNEVKDrlhdsavgLSGGQQQRV 157
Cdd:TIGR03719 388 ----AYVDQSrdaldPNK---TVWEEISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQKKVGQ--------LSGGERNRV 452
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLL 192
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-187 |
1.33e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTIT-GSIVYNGHNIYSprt 79
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG----HPAYKILeGDILFKGESILD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIG--MVFQQPNPFPMSIYEN---VVYGLRLKgIRDKSILDhavesSLKGASIWNEVKDRLHDSAV------- 147
Cdd:CHL00131 76 LEPEERAHLGifLAFQYPIEIPGVSNADflrLAYNSKRK-FQGLPELD-----PLEFLEIINEKLKLVGMDPSflsrnvn 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489083979 148 -GLSGGQQQRVCIARVLATSPRIILLDEPTSALDpISAGKI 187
Cdd:CHL00131 150 eGFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKI 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-203 |
2.32e-12 |
|
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: 66.11 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 13 VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsInrMNDLNPEvtitgsivYNGHNIYSPRTdtvdlrkEIGMVF 92
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-I--MAGVDKD--------FNGEARPQPGI-------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 93 QQPNPFP-MSIYENVVYGLR-LKGIRDK--------------------------SILDHA----VESSLKGASiwnevkD 140
Cdd:TIGR03719 75 QEPQLDPtKTVRENVEEGVAeIKDALDRfneisakyaepdadfdklaaeqaelqEIIDAAdawdLDSQLEIAM------D 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 141 RLH----DSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLlllkKDYTLAIV 203
Cdd:TIGR03719 149 ALRcppwDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVV 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-187 |
2.61e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLnpEVTiTGSIVYNGHniysprtDTVDL 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVT-GGTVEFKGK-------DLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKE------IGMVFQQP-------NPFPMSIYENVVYGLRLKGIRDKSILDHAVESSLKgasIWNEVKDRLHDSA-VGLS 150
Cdd:PRK09580 71 SPEdragegIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIA---LLKMPEDLLTRSVnVGFS 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 489083979 151 GGQQQRVCIARVLATSPRIILLDEPTSALDpISAGKI 187
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKI 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-227 |
2.64e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKktLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIySPRTDT 81
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPRSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDLRKEIGMVFQQPNP---FP-MSIYENVVYGLRLKGIRDKS---ILDHAVES----------SLKGASIWNEVKDrlhd 144
Cdd:PRK09700 334 DAVKKGMAYITESRRDngfFPnFSIAQNMAISRSLKDGGYKGamgLFHEVDEQrtaenqrellALKCHSVNQNITE---- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 145 savgLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKD-YTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:PRK09700 410 ----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEG 485
|
....
gi 489083979 224 DLLE 227
Cdd:PRK09700 486 RLTQ 489
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-212 |
3.39e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.88 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVdlrkeigmvfqqpnpFPM 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSGRISFSSQFSWI---------------MPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENVVYGLRLKGIRDKSILD--HAVESSLKGASIWNEVkdrLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSA 178
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKSVVKacQLEEDITKFPEKDNTV---LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 179 LDPISAGKI-EETLLLLKKDYTLAIVTRSMQQASR 212
Cdd:cd03291 190 LDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-237 |
3.94e-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: 65.23 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYY---NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNPEvtitGSIVYNGHNIySPRT 79
Cdd:TIGR02633 255 DVILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFE----GNVFINGKPV-DIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 DTVDLRKEIGMV---FQQPNPFP-MSIYENVVYGLrLKGIRDKSILDHAVESSLKGASIWN-EVKDRLHDSAVG-LSGGQ 153
Cdd:TIGR02633 330 PAQAIRAGIAMVpedRKRHGIVPiLGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRlKVKTASPFLPIGrLSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL-LLLKKDYTLAIVTRSMQQASRLSDRTGFFLEGDLlecgptK 232
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL------K 482
|
....*
gi 489083979 233 AMFMN 237
Cdd:TIGR02633 483 GDFVN 487
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-228 |
4.62e-12 |
|
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: 64.16 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYY--NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTDTvd 83
Cdd:cd03288 20 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIRDKSILDHAVESSLKGASIWNEVKDR-------LHDSAVGLSGGQQQR 156
Cdd:cd03288 93 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 157 VCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTlaIVTRSMQQASRLS-DRTGFFLEGDLLEC 228
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRT--VVTIAHRVSTILDaDLVLVLSRGILVEC 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-248 |
7.11e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlNPEVTITGSIVYNGHniySPRTDTVDLRKEIGMVFQQPNPFP- 99
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTD-GFHIGVEGVITYDGI---TPEEIKKHYRGDVVYNAETDVHFPh 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 100 MSIYENVVY-------GLRLKGIRDKSILDHAVESSLK--GASIWNEVKDRlHDSAVGLSGGQQQRVCIARVLATSPRII 170
Cdd:TIGR00956 153 LTVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMAtyGLSHTRNTKVG-NDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 171 LLDEPTSALDPISAGKIEETL----LLLKKDYTLAIVTRSmQQASRLSDRTGFFLEGDLLECGP---TKAMFMN-----P 238
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALktsaNILDTTPLVAIYQCS-QDAYELFDKVIVLYEGYQIYFGPadkAKQYFEKmgfkcP 310
|
250
....*....|
gi 489083979 239 KRKETEDYIS 248
Cdd:TIGR00956 311 DRQTTADFLT 320
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-180 |
9.15e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtitgsivynghniyspRTDTVDLRKEIGMVFQQPN 96
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHA-----------------ETSSVVIRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFPMSIYENVVYGLRLKGIR-----DKSILDHAVEssLKGASIWNEVKDRlhdsAVGLSGGQQQRVCIARVLATSPRIIL 171
Cdd:PLN03232 690 IFNATVRENILFGSDFESERywraiDVTALQHDLD--LLPGRDLTEIGER----GVNISGGQKQRVSMARAVYSNSDIYI 763
|
....*....
gi 489083979 172 LDEPTSALD 180
Cdd:PLN03232 764 FDDPLSALD 772
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-191 |
1.01e-11 |
|
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: 64.58 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQ--KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVD 83
Cdd:TIGR00957 1285 VEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI--AKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPF---------PMSIY--ENVVYGLRLKGIrdksildHAVESSLKgasiwnevkDRL-HDSAVG--- 148
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFsgslrmnldPFSQYsdEEVWWALELAHL-------KTFVSALP---------DKLdHECAEGgen 1421
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489083979 149 LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-179 |
1.44e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDLN---PEVTITGSIVYNG-----HNIY- 75
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTL------MKVLSgvyPHGSYEGEILFDGevcrfKDIRd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 76 SPRTDTVDLRKEIGMVfqqpnPFpMSIYENVVYGlrlkgirdksildhaVESSLKGASIWNEVKDR---------LHDSA 146
Cdd:NF040905 75 SEALGIVIIHQELALI-----PY-LSIAENIFLG---------------NERAKRGVIDWNETNRRarellakvgLDESP 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 489083979 147 VGLSG----GQQQRVCIARVLATSPRIILLDEPTSAL 179
Cdd:NF040905 134 DTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-207 |
1.50e-11 |
|
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: 64.20 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 20 TLKDVSLDLYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVHMKGSVAY---------------------VPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 99 PMSIYENVVYGLRLKGIRDKSILDH-AVESSLKGASIWNEVKdrLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTS 177
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVLEAcALLPDLEILPSGDRTE--IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190
....*....|....*....|....*....|...
gi 489083979 178 ALDPISAGKIEETLL---LLKKDYTLAIVTRSM 207
Cdd:TIGR00957 790 AVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGI 822
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-182 |
2.60e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSIN------RMNDLnpevTITGSIVYNGHNIYs 76
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgYSNDL----TLFGRRRGSGETIW- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 77 prtdtvDLRKEIGMVfqqPNPFPMSiYE------NVVyglrLKGIRDkSI-LDHAVESSL-KGASIWnevKDRLH-DSAV 147
Cdd:PRK10938 333 ------DIKKHIGYV---SSSLHLD-YRvstsvrNVI----LSGFFD-SIgIYQAVSDRQqKLAQQW---LDILGiDKRT 394
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489083979 148 G------LSGGQQQRVCIARVLATSPRIILLDEPTSALDPI 182
Cdd:PRK10938 395 AdapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-180 |
5.89e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLS-VYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsInrMNDLNPEvtitgsivYNGHNIYSPRT 79
Cdd:PRK11819 2 MAQYIYTMNRVSkVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-I--MAGVDKE--------FEGEARPAPGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 80 dtvdlrkEIGMVFQQP--NPfPMSIYENVVYGLR-LKGIRDK--------------------------SILDHA----VE 126
Cdd:PRK11819 71 -------KVGYLPQEPqlDP-EKTVRENVEEGVAeVKAALDRfneiyaayaepdadfdalaaeqgelqEIIDAAdawdLD 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 127 SSLKGASiwnevkDRLH----DSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK11819 143 SQLEIAM------DALRcppwDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-180 |
1.13e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYY---NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI-----NRMndlnpevtiTGSIVYNGH-- 72
Cdd:PRK13549 257 EVILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRW---------EGEIFIDGKpv 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 73 NIYSPRtDTVDL--------RKEIGMVFQqpnpfpMSIYENVVYGLrLKGIRDKSILDHAVESSLKGASIwnevkDRLH- 143
Cdd:PRK13549 328 KIRNPQ-QAIAQgiamvpedRKRDGIVPV------MGVGKNITLAA-LDRFTGGSRIDDAAELKTILESI-----QRLKv 394
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489083979 144 -----DSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK13549 395 ktaspELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-247 |
1.27e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGH--NIYSPRTDTVDLRK---EIGMvfqqp 95
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLAL--AGKLDPSLKVSGEITYNGYrlNEFVPRKTSAYISQndvHVGV----- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 npfpMSIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWNE--------------VKDRL--------------HDSAV 147
Cdd:PLN03140 254 ----MTVKETLDFSARCQGVGTRYDLLSELARREKDAGIFPEaevdlfmkatamegVKSSLitdytlkilgldicKDTIV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 148 ------GLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKdYTLAIVTRSMQQAS----RLSDRT 217
Cdd:PLN03140 330 gdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH-LTEATVLMSLLQPApetfDLFDDI 408
|
250 260 270
....*....|....*....|....*....|....*...
gi 489083979 218 GFFLEGDLLECGPTKAM--------FMNPKRKETEDYI 247
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHIleffescgFKCPERKGTADFL 446
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-216 |
1.41e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 15 YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLR---SInrmndLNPEvtiTGSIVYNGHNiysPRTDTVDLRKEIGMV 91
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltGI-----LVPT---SGEVRVLGYV---PFKRRKEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 92 FQQPN------P----FPM--SIYE--NVVYGLRLKGIRDksILDhavesslkgasiwneVKDRLHDSAVGLSGGQQQRV 157
Cdd:COG4586 101 FGQRSqlwwdlPaidsFRLlkAIYRipDAEYKKRLDELVE--LLD---------------LGELLDTPVRQLSLGQRMRC 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLLLLKKDY--TLAIVTRSMQQASRLSDR 216
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDR 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-180 |
1.50e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 16 NQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPevTITGSIVYNGHNIYSPRTDTVdlrkeigmvfqqp 95
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASVVIRGTVAYVPQVSWI------------- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 npFPMSIYENVVYGLRLKGIR-----DKSILDHAVESsLKGASIwNEVKDRlhdsAVGLSGGQQQRVCIARVLATSPRII 170
Cdd:PLN03130 691 --FNATVRDNILFGSPFDPERyeraiDVTALQHDLDL-LPGGDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDVY 762
|
170
....*....|
gi 489083979 171 LLDEPTSALD 180
Cdd:PLN03130 763 IFDDPLSALD 772
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-180 |
2.48e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVY---YNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI-------NrmndlnpevtITGSIVYNGH 72
Cdd:NF040905 255 EVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrN----------ISGTVFKDGK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 73 NIyspRTDTVDL------------RKEIGMVFQQpnpfpmSIYENVVYGlRLKGIRDKSILDHAVEsslkgASIWNEVKD 140
Cdd:NF040905 325 EV---DVSTVSDaidaglayvtedRKGYGLNLID------DIKRNITLA-NLGKVSRRGVIDENEE-----IKVAEEYRK 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489083979 141 RLH------DSAVG-LSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:NF040905 390 KMNiktpsvFQKVGnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-180 |
4.29e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIySPRTDTVDL----------RKEIGM 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVL--YGALPRT---SGYVTLDGHEV-VTRSPQDGLangivyisedRKRDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 91 VFQqpnpfpMSIYENvvygLRLKGIRDKS----ILDHAVESSLKGASI--WNeVKDRLHDSAVG-LSGGQQQRVCIARVL 163
Cdd:PRK10762 342 VLG------MSVKEN----MSLTALRYFSraggSLKHADEQQAVSDFIrlFN-IKTPSMEQAIGlLSGGNQQKVAIARGL 410
|
170
....*....|....*..
gi 489083979 164 ATSPRIILLDEPTSALD 180
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD 427
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-215 |
9.06e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINR---MNDlnpevtitGSIVYNghniysprTDTVDLRkeigmvFQQ--P 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD--------GRIIYE--------QDLIVAR------LQQdpP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 96 NPFPMSIYENVVYGLRLKG--IRDKSILDHAVESS---------------LKGASIW------NEVKDRLHDSA----VG 148
Cdd:PRK11147 77 RNVEGTVYDFVAEGIEEQAeyLKRYHDISHLVETDpseknlnelaklqeqLDHHNLWqlenriNEVLAQLGLDPdaalSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489083979 149 LSGGQQQRVCIARVLATSPRIILLDEPTSALDpISAgkIE--ETLLllkKDYTLAIV--------TRSMqqASRLSD 215
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEwlEGFL---KTFQGSIIfishdrsfIRNM--ATRIVD 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-191 |
3.23e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLrsinrmNDLNPEVT---IT-GSIVYNGHniysPRTDTvdLRKEIGMVFQQPN 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLL------NVLAERVTtgvITgGDRLVNGR----PLDSS--FQRSIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 97 PFPMS-IYENVVYGLRLKgiRDKSIL----DHAVESSLKGASIwnevkDRLHDSAVGLSGG-----QQQRVCIARVLATS 166
Cdd:TIGR00956 847 HLPTStVRESLRFSAYLR--QPKSVSksekMEYVEEVIKLLEM-----ESYADAVVGVPGEglnveQRKRLTIGVELVAK 919
|
170 180
....*....|....*....|....*.
gi 489083979 167 PRIIL-LDEPTSALDPISAGKIEETL 191
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLM 945
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-180 |
5.30e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTVDLR 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR--PD---AGEVLWQGEPI---RRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 86 KE---IGmvfQQPNPFP-MSIYENVVYGLRLKGIRDKSILDHAVES-SLKGasiwnevkdRLHDSAVGLSGGQQQRVCIA 160
Cdd:PRK13538 74 QDllyLG---HQPGIKTeLTALENLRFYQRLHGPGDDEALWEALAQvGLAG---------FEDVPVRQLSAGQQRRVALA 141
|
170 180
....*....|....*....|
gi 489083979 161 RVLATSPRIILLDEPTSALD 180
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAID 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-216 |
1.04e-08 |
|
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: 54.34 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 14 YYNQKKTLKDVSL-----DLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVtitGSIVYNGHNI-YSPRTDTVDlrke 87
Cdd:cd03237 3 YPTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKML--AGVLKPDE---GDIEIELDTVsYKPQYIKAD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 88 igmvfqqpnpFPMSIYENVvyglrlkgirdKSILDHAVESSLKGASIWNEVK-DRLHDSAV-GLSGGQQQRVCIARVLAT 165
Cdd:cd03237 74 ----------YEGTVRDLL-----------SSITKDFYTHPYFKTEIAKPLQiEQILDREVpELSGGELQRVAIAACLSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489083979 166 SPRIILLDEPTSALDpisagkIEETLL--------LLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:cd03237 133 DADIYLLDEPSAYLD------VEQRLMaskvirrfAENNEKTAFVVEHDIIMIDYLADR 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-226 |
1.08e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 1 MTEPILQIRDLSvyynqkKTLKDVSLD-----LYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYNGHNI 74
Cdd:COG1245 337 EEETLVEYPDLT------KSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILaGVLKPDEGEVDEDLKISYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 75 YSPRTDTVD--LRKEIGmvfqqpNPFPMSIYEN-VVYGLRLKGIRDKsildhavesslkgasiwnEVKDrlhdsavgLSG 151
Cdd:COG1245 411 SPDYDGTVEefLRSANT------DDFGSSYYKTeIIKPLGLEKLLDK------------------NVKD--------LSG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 152 GQQQRVCIARVLATSPRIILLDEPTSALDpisagkIEETLlllkkdytlaIVTRSMQQASRLSDRTGFFLEGDLL 226
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLD------VEQRL----------AVAKAIRRFAENRGKTAMVVDHDIY 517
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-216 |
1.19e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 3 EPILQIRDLSVYyNQKkTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTD-- 80
Cdd:PRK10982 248 EVILEVRNLTSL-RQP-SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKKINNHNANea 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 -------TVDLRKEIGMVFQQPNPFPmSIYENV-----VYGLrLKGIRDKSILDHAVESSlkgasiwnEVKDRLHDSAVG 148
Cdd:PRK10982 321 inhgfalVTEERRSTGIYAYLDIGFN-SLISNIrnyknKVGL-LDNSRMKSDTQWVIDSM--------RVKTPGHRTQIG 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 149 -LSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDR 216
Cdd:PRK10982 391 sLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAeLAKKDKGIIIISSEMPELLGITDR 460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-189 |
1.59e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.03 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIyspRTDTVDL 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--LNPE---KGEILFERQSI---KKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 RKEIGMVFQQP--NPFpMSIYENVVYGLrlkgirdksildHAVESSLKGASIWNEVK-DRLHDSAVG-LSGGQQQRVCIA 160
Cdd:PRK13540 73 QKQLCFVGHRSgiNPY-LTLRENCLYDI------------HFSPGAVGITELCRLFSlEHLIDYPCGlLSSGQKRQVALL 139
|
170 180 190
....*....|....*....|....*....|...
gi 489083979 161 RVLATSPRIILLDEPTSALDPIS----AGKIEE 189
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSlltiITKIQE 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-223 |
3.35e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKT--LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITG-SIVYNGHNI-----Y 75
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpaVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSgDATVAGkSILTNISDVhqnmgY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 76 SPRTDTVDlrkEIgmvfqqpnpfpMSIYENVVYGLRLKGIRDKSIlDHAVESSLK--GASIWnevKDRLhdsAVGLSGGQ 153
Cdd:TIGR01257 2017 CPQFDAID---DL-----------LTGREHLYLYARLRGVPAEEI-EKVANWSIQslGLSLY---ADRL---AGTYSGGN 2075
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 154 QQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVTRSMQQASRLSDRTGFFLEG 223
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVsIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-180 |
3.75e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 18 KKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSinrmndLNPEVTITGSIVYnghniysprtdtvdLRKEIGMVFQQPNP 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQS------LLSQFEISEGRVW--------------AERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 98 FPMSIYENVVY-----GLRLKGIRDKSILDHAVesSLKGASIWNEVKDRlhdsAVGLSGGQQQRVCIARVLATSPRIILL 172
Cdd:PTZ00243 733 MNATVRGNILFfdeedAARLADAVRVSQLEADL--AQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLL 806
|
....*...
gi 489083979 173 DEPTSALD 180
Cdd:PTZ00243 807 DDPLSALD 814
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-227 |
5.05e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENvvyglrlkgirdksiLDHAVESSlkGASIWN-----EVKDRLHDSAVGL-----------SGGQQQRVCIARVLA 164
Cdd:PLN03232 1325 TVRFN---------------IDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 165 TSPRIILLDEPTSALDPISAGKIEETLLLLKKDYTLAIVtrsmqqASRLS-----DRTGFFLEGDLLE 227
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI------AHRLNtiidcDKILVLSSGQVLE 1449
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-206 |
7.68e-08 |
|
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: 52.83 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 36 LIGPSGSGKSTLLRSINrmnDLNPevtitgsiVYNGhniysprTDTVDLRKEIGMVFQQPNpfpMS--------IYENVV 107
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILG---ELWP--------VYGG-------RLTKPAKGKLFYVPQRPY---MTlgtlrdqiIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 108 YGLRLKGIRDKSI--------LDHAVESSLKGASI--WNEVkdrlhdsavgLSGGQQQRVCIARVLATSPRIILLDEPTS 177
Cdd:TIGR00954 542 EDMKRRGLSDKDLeqildnvqLTHILEREGGWSAVqdWMDV----------LSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180
....*....|....*....|....*....
gi 489083979 178 ALDPisagKIEETLLLLKKDYTLAIVTRS 206
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGITLFSVS 636
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-180 |
9.07e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 101 SIYENvvyglrlkgirdksiLDHAVESSlkGASIWN-----EVKDRLHDSAVGL-----------SGGQQQRVCIARVLA 164
Cdd:PLN03130 1328 TVRFN---------------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALL 1390
|
170
....*....|....*.
gi 489083979 165 TSPRIILLDEPTSALD 180
Cdd:PLN03130 1391 RRSKILVLDEATAAVD 1406
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-191 |
2.23e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVT---ITGSIVYNGhniYSPRTDTvd 83
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTL------MDVLAGRKTggyIEGDIRISG---FPKKQET-- 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPNPFP-MSIYENVVYG--LRLK---GIRDKSILdhaVESSLKGASIwnevkDRLHDSAVGLSG------ 151
Cdd:PLN03140 951 FARISGYCEQNDIHSPqVTVRESLIYSafLRLPkevSKEEKMMF---VDEVMELVEL-----DNLKDAIVGLPGvtglst 1022
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489083979 152 GQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-183 |
2.26e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLL------RSINrmndlnpevtiTGSIVYNGHNIYSPR 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQ-----------QGRVEVLGGDMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 79 tdtvdLRKEIG-----MvfqqP-----NPFP-MSIYENVVYGLRLKGI----RDKSIldhavesslkgasiwnevkDRLH 143
Cdd:NF033858 70 -----HRRAVCpriayM----PqglgkNLYPtLSVFENLDFFGRLFGQdaaeRRRRI-------------------DELL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489083979 144 DS----------AVGLSGGQQQRV--CIArvLATSPRIILLDEPTSALDPIS 183
Cdd:NF033858 122 RAtglapfadrpAGKLSGGMKQKLglCCA--LIHDPDLLILDEPTTGVDPLS 171
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-180 |
2.86e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 24 VSLDLYPNEITALIGPSGSGKSTLLRSI---NRMNDlnpevtitGSIVYNGH--NIYSPRtDTVDL--------RKEIGM 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRRTA--------GQVYLDGKpiDIRSPR-DAIRAgimlcpedRKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 91 VfqqpnpfPM-SIYENVVYGLRLKGIRDKSILDHAVESSLKGASIWN-EVKDRLHDSAVG-LSGGQQQRVCIARVLATSP 167
Cdd:PRK11288 343 I-------PVhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSlNIKTPSREQLIMnLSGGNQQKAILGRWLSEDM 415
|
170
....*....|...
gi 489083979 168 RIILLDEPTSALD 180
Cdd:PRK11288 416 KVILLDEPTRGID 428
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-226 |
3.29e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 11 LSVYYNQKKTLKDVSLD-----LYPNEITALIGPSGSGKSTLLRSINrmNDLNP---EVTITGSIVYNGHNIYSPRTDTV 82
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLA--GVLKPdegEVDPELKISYKPQYIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 83 DLrkeigMVFQQPNPFPMSIYEN-VVYGLRLkgirdksildhavesslkgasiwnevkDRLHDSAVG-LSGGQQQRVCIA 160
Cdd:PRK13409 418 ED-----LLRSITDDLGSSYYKSeIIKPLQL---------------------------ERLLDKNVKdLSGGELQRVAIA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489083979 161 RVLATSPRIILLDEPTSALDpisagkIEETLlllkkdytlaIVTRSMQQASRLSDRTGFFLEGDLL 226
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLD------VEQRL----------AVAKAIRRIAEEREATALVVDHDIY 515
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-180 |
5.85e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTL-KDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSI---------VYNGHN 73
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS--GELQP---SSGTVfrsakvrmaVFSQHH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 74 IysprtDTVDLrkeigmvfqQPNPfpmsiyenVVYGLR-LKGIRDKSILDH----AVESSLKGASIWNevkdrlhdsavg 148
Cdd:PLN03073 582 V-----DGLDL---------SSNP--------LLYMMRcFPGVPEQKLRAHlgsfGVTGNLALQPMYT------------ 627
|
170 180 190
....*....|....*....|....*....|..
gi 489083979 149 LSGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-179 |
1.87e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 19 KTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIySPRTDTVDLRKEIGMVFQQPNPF 98
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD-----SGSILFQGKEI-DFKSSKEALENGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 99 -PMSIYENVVYG-LRLKGIrdksILDHavesslkgASIWNEVK---DRL------HDSAVGLSGGQQQRVCIARVLATSP 167
Cdd:PRK10982 86 lQRSVMDNMWLGrYPTKGM----FVDQ--------DKMYRDTKaifDELdididpRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170
....*....|..
gi 489083979 168 RIILLDEPTSAL 179
Cdd:PRK10982 154 KIVIMDEPTSSL 165
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-192 |
2.40e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNghniysprtDTVDL 84
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ-----EQPDSGTIKIG---------ETVKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 85 rkeiGMVFQQ-----PNPfpmSIYENVVYGLRLKGIRDKSILDHAVESS--LKGASIWNEVKDrlhdsavgLSGGQQQRV 157
Cdd:PRK11819 390 ----AYVDQSrdaldPNK---TVWEEISGGLDIIKVGNREIPSRAYVGRfnFKGGDQQKKVGV--------LSGGERNRL 454
|
170 180 190
....*....|....*....|....*....|....*
gi 489083979 158 CIARVLATSPRIILLDEPTSALDPISAGKIEETLL 192
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-216 |
2.72e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVY--NGHNIYSPRTDTVD 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKWseNANIGYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGmVFQQpnpfpMSIYenvvyglrlkgiRDKSILDHAVESSLkGASIWNEvkDRLHDSAVGLSGGQQQRVCIARVL 163
Cdd:PRK15064 395 FENDLT-LFDW-----MSQW------------RQEGDDEQAVRGTL-GRLLFSQ--DDIKKSVKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489083979 164 ATSPRIILLDEPTSALDPISagkIEETLLLLKK-DYTLAIVTRSMQQASRLSDR 216
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSHDREFVSSLATR 504
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-181 |
2.98e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.77 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 2 TEPILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGH-NIYSPRTD 80
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGL--LHVE---SGQIQIDGKtATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 81 TVDLRKEIGMVFQQpnpfpMSIYENVVYGLRLKGIRDKSILDHAVesSLKGASIWNEVKDRlhdsavGLSGGQQQRVCIA 160
Cdd:PRK13543 83 FMAYLGHLPGLKAD-----LSTLENLHFLCGLHGRRAKQMPGSAL--AIVGLAGYEDTLVR------QLSAGQKKRLALA 149
|
170 180
....*....|....*....|.
gi 489083979 161 RVLATSPRIILLDEPTSALDP 181
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-180 |
9.24e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 5 ILQIRDLSVYYNQKkTLKDVSLDLYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVY---NGHNIYSPRTDT 81
Cdd:PRK13541 1 MLSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIA--GIMQPS---SGNIYYkncNINNIAKPYCTY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 82 VDlrKEIGMVFQqpnpfpMSIYENVVYGlrlkgirdKSILDHAveSSLKGASIWNEVKDRLHDSAVGLSGGQQQRVCIAR 161
Cdd:PRK13541 75 IG--HNLGLKLE------MTVFENLKFW--------SEIYNSA--ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIAR 136
|
170
....*....|....*....
gi 489083979 162 VLATSPRIILLDEPTSALD 180
Cdd:PRK13541 137 LIACQSDLWLLDEVETNLS 155
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
145-214 |
2.56e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 145 SAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKI-EETLLLLKKDYTLAIVTRSMQQASRLS 214
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLA 211
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-203 |
4.23e-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: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTL-------------LRSI-----NRMNDLN-PEVT-ITG-----SIVYN--GHN 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLsayarQFLGQMDkPDVDsIEGlspaiAIDQKttSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 74 iysPRTdTVDLRKEIgmvfqqpNPFPMSIYENVVYGLRLKGIRDKSiLDHAvesslkgasiwnevkdRLHDSAVGLSGGQ 153
Cdd:cd03270 91 ---PRS-TVGTVTEI-------YDYLRLLFARVGIRERLGFLVDVG-LGYL----------------TLSRSAPTLSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489083979 154 QQRVCIARVLAT--SPRIILLDEPTSALDPISAGKIEETLLLLK-KDYTLAIV 203
Cdd:cd03270 143 AQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVV 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-197 |
4.63e-05 |
|
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: 42.36 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 30 PNEITALIGPSGSGKSTLLRSInrmndlnpevtitgsivynghniysprtdtvdlrkeigmvfqqpnpfpmsiyenvvyg 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL---------------------------------------------------------- 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 110 LRLKGIRDKSILDHAVESSLKGASIWNEVKDRLHDSAVGlSGGQQQRVCIARVLATSPRIILLDEPTSALDPISAGKIEE 189
Cdd:smart00382 23 ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASG-SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
....*...
gi 489083979 190 TLLLLKKD 197
Cdd:smart00382 102 LEELRLLL 109
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-180 |
6.22e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 4 PILQIRDLSVYYNQKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIvynghniySPRTDTVD 83
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIK------------LLAGEL--------APVSGEIG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGM-VFQQPnpfpmsiyenvvyglRLKGIR-DKSILDHAV-------ESSLK---GASIWNevKDRLHDSAVGLSG 151
Cdd:PRK10636 371 LAKGIKLgYFAQH---------------QLEFLRaDESPLQHLArlapqelEQKLRdylGGFGFQ--GDKVTEETRRFSG 433
|
170 180
....*....|....*....|....*....
gi 489083979 152 GQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-51 |
6.66e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.89 E-value: 6.66e-05
10 20 30
....*....|....*....|....*....|..
gi 489083979 20 TLKDVSLDLYPNEITALIGPSGSGKSTLLRSI 51
Cdd:pfam13555 11 TFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAI 42
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-57 |
9.76e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 9.76e-05
10 20 30
....*....|....*....|....*....|....*....
gi 489083979 19 KTLKDVSLDLypNEITALIGPSGSGKSTLLRSINRMNDL 57
Cdd:COG4637 11 KSLRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDA 47
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
147-204 |
1.36e-04 |
|
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: 41.19 E-value: 1.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489083979 147 VGLSGGQQQRVCIARVLA---TSPR-IILLDEPTSALDPISAGKIEETLL-LLKKDYTLAIVT 204
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVIT 138
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-78 |
2.05e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 2.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 19 KTLKDVSLDLYPNeITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPR 78
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPE 70
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-180 |
3.72e-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: 41.31 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 30 PNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYN-GHNIYSPRTDTVdLRKEIGMVFQQpnpfpmsiyenvvY 108
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK------------ILSGELKPNlGDYDEEPSWDEV-LKRFRGTELQD-------------Y 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 109 glrLKGIRDKSI---------------LDHAVESSLKGA---SIWNEVKDRLH-----DSAVG-LSGGQQQRVCIARVLA 164
Cdd:COG1245 152 ---FKKLANGEIkvahkpqyvdlipkvFKGTVRELLEKVderGKLDELAEKLGlenilDRDISeLSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 489083979 165 TSPRIILLDEPTSALD 180
Cdd:COG1245 229 RDADFYFFDEPSSYLD 244
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-204 |
4.07e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 6 LQIRDLSVYYNQkktlkdVSLDLyPNEITALIGPSGSGKSTLLRSI----------------NRMNDLNPEVTITGSIVY 69
Cdd:COG0419 5 LRLENFRSYRDT------ETIDF-DDGLNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEASVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 70 NGHNIYSPR----------TDTVDLRKEIGMVFQqpnpfpMSIYENVvyglrlkgIRDKSILDHAVESSLKGASIWNEVK 139
Cdd:COG0419 78 GGKRYRIERrqgefaefleAKPSERKEALKRLLG------LEIYEEL--------KERLKELEEALESALEELAELQKLK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489083979 140 DRLH------DSAVGLSGGQQQRVCIARVLAtspriILLDepTSALDPISAGKIEETLlllkkdYTLAIVT 204
Cdd:COG0419 144 QEILaqlsglDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDAL------EELAIIT 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-180 |
4.18e-04 |
|
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: 40.81 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 30 PNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGS------IV--YNG---HNIYSP-RTDTVDLRKEIGMVFQQPNP 97
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILA--GKLKPNLGKFDDppdwdeILdeFRGselQNYFTKlLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 98 FPMSIYENvvyglrLKGIRDKSILDHAVES-SLKGasiwneVKDRLHDSavgLSGGQQQRVCIARVLATSPRIILLDEPT 176
Cdd:cd03236 103 VKGKVGEL------LKKKDERGKLDELVDQlELRH------VLDRNIDQ---LSGGELQRVAIAAALARDADFYFFDEPS 167
|
....
gi 489083979 177 SALD 180
Cdd:cd03236 168 SYLD 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-180 |
5.19e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 30 PNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYN-GHNIYSPRTDTVdLRKEIGMVFQQpnpfpmsiyenvvY 108
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVK------------ILSGELIPNlGDYEEEPSWDEV-LKRFRGTELQN-------------Y 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 109 glrLKGIRDKSI---------------LDHAVESSLKGA---SIWNEVKDRLHDSAV------GLSGGQQQRVCIARVLA 164
Cdd:PRK13409 152 ---FKKLYNGEIkvvhkpqyvdlipkvFKGKVRELLKKVderGKLDEVVERLGLENIldrdisELSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 489083979 165 TSPRIILLDEPTSALD 180
Cdd:PRK13409 229 RDADFYFFDEPTSYLD 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-117 |
5.51e-04 |
|
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: 40.45 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 33 ITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLRKEIGMVFQqpnpFPMSIYENVVYGLRL 112
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFE----ISEFLEDGVRYRYGL 76
|
....*
gi 489083979 113 KGIRD 117
Cdd:pfam13304 77 DLERE 81
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
14-88 |
9.09e-04 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 39.61 E-value: 9.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489083979 14 YYNQKKTLKDVS--LDLYPNEITALIGPSGSGKSTLLR-SINRMNDLNPEVtitgSIVYNGHNIYSPRTDTVDLRKEI 88
Cdd:pfam01637 1 FVDREKELKELEewAERGPNLIYVIYGPEGCGKTALLReSIENLLDLGYYV----IYYDPLRRYFISKLDRFEEVRRL 74
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
149-208 |
9.31e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 9.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 149 LSGGQQQRVCIARVLATSPRIILLDEPTSALDPisagkieETLLLLKK---DY--TLAIVTRSMQ 208
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV-------ETLELLEElldSYqgTVLLVSHDRQ 498
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-67 |
9.91e-04 |
|
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: 39.30 E-value: 9.91e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489083979 31 NEITALIGPSGSGKSTLLrsinrmNDLNPEVTI-TGSI 67
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLL------NALLPELVLaTGEI 116
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
135-220 |
1.48e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.32 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 135 WNEVKDRLHDSAVGLSGGQQQRVCIARVLATSPRIILLDEPTSALDpisagkIEETL--------LLLKKDYTLAIVTRS 206
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD------IEQRLnaarairrLSEEGKKTALVVEHD 131
|
90
....*....|....
gi 489083979 207 MQQASRLSDRTGFF 220
Cdd:cd03222 132 LAVLDYLSDRIHVF 145
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
31-67 |
1.83e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.65 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489083979 31 NEITALIGPSGSGKSTLLrsinrmNDLNPEVTI-TGSI 67
Cdd:PRK00098 164 GKVTVLAGQSGVGKSTLL------NALAPDLELkTGEI 195
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-47 |
1.93e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.93e-03
10 20
....*....|....*....|....*..
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTL 47
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
141-191 |
1.94e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 1.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489083979 141 RLHDSAVGLSGGQQQR---VCIARVLA----------TSPRIILLDEPTSALDPISAGKIEETL 191
Cdd:pfam13558 25 ETYRRSGGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
31-67 |
2.11e-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: 37.91 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489083979 31 NEITALIGPSGSGKSTLLrsinrmNDLNPEVTI-TGSI 67
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLL------NALLPELDLrTGEI 137
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-191 |
2.20e-03 |
|
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: 37.69 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489083979 149 LSGGQQQRVCIARVLATSPR--IILLDEPTSALDPISAGKIEETL 191
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-52 |
2.24e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|....*
gi 489083979 19 KTLKDVSLDL-YPNEITALIGPSGSGKSTLLRSIN 52
Cdd:COG3950 12 RGFEDLEIDFdNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-179 |
2.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489083979 141 RLHDSAVGLSGGQQQRVCIARVL---ATSPRIILLDEPTSAL 179
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL 863
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
150-180 |
2.78e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 2.78e-03
10 20 30
....*....|....*....|....*....|.
gi 489083979 150 SGGQQQRVCIARVLATSPRIILLDEPTSALD 180
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
33-97 |
3.92e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 3.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489083979 33 ITALIGPSGSGKSTLLRSInrMNDLNPEVTitgsIVYnghnIYSPRTDTVDLRKEIGMVFQQPNP 97
Cdd:COG3267 45 FVVLTGEVGTGKTTLLRRL--LERLPDDVK----VAY----IPNPQLSPAELLRAIADELGLEPK 99
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
27-66 |
3.95e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 38.18 E-value: 3.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489083979 27 DLYPNEITALIGPSGSGKSTLLRSINR------MNDLNPEVTITGS 66
Cdd:COG5192 65 DLPPPFIVAVVGPPGTGKSTLIRSLVRrftkqtIDEIRGPITVVSG 110
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-51 |
4.00e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 4.00e-03
10 20 30
....*....|....*....|....*....|....*
gi 489083979 17 QKKTLKDVSLDLYPNEITALIGPSGSGKSTLLRSI 51
Cdd:TIGR00630 620 RENNLKNITVSIPLGLFTCITGVSGSGKSTLINDT 654
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
19-54 |
4.59e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 37.96 E-value: 4.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489083979 19 KTLKDVSLDLyPNEITALIGPSGSGKSTLLRSINRM 54
Cdd:pfam13175 12 RCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-244 |
4.94e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.49 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 7 QIRDLSVYYNQKKT---LKDVSLDLYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIvynghniySPRTDTVD 83
Cdd:PRK13546 23 RMKDALIPKHKNKTffaLDDISLKAYEGDVIGLVGINGSGKSTLSN------------IIGGSL--------SPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 84 LRKEIGMVFQQPN-PFPMSIYENVVYGLRLKGIRDKSI---LDHAVESSLKGASIWNEVKDrlhdsavgLSGGQQQRVCI 159
Cdd:PRK13546 83 RNGEVSVIAISAGlSGQLTGIENIEFKMLCMGFKRKEIkamTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489083979 160 ARVLATSPRIILLDEPTSALDPISAGKIEETLLLLK-KDYTLAIVTRSMQQASRLSDRTGFFLEGDLLECG------PTK 232
Cdd:PRK13546 155 SINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGelddvlPKY 234
|
250
....*....|..
gi 489083979 233 AMFMNPKRKETE 244
Cdd:PRK13546 235 EAFLNDFKKKSK 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
21-47 |
5.37e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 5.37e-03
10 20
....*....|....*....|....*..
gi 489083979 21 LKDVSLDLYPNEITALIGPSGSGKSTL 47
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-51 |
6.68e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.68e-03
10 20 30
....*....|....*....|....*....|...
gi 489083979 19 KTLKDVSLDLYPNeITALIGPSGSGKSTLLRSI 51
Cdd:pfam13476 7 RSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
32-49 |
7.18e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.96 E-value: 7.18e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-179 |
8.47e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 489083979 145 SAVGLSGGQQQRVCIARVLA---TSPRIILLDEPTSAL 179
Cdd:COG0178 823 PATTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTGL 860
|
|
| |
