|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-257 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 537.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSM-VNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNI 79
Cdd:COG1117 1 MTApASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 LTNTQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQ 159
Cdd:COG1117 81 YDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....*...
gi 490994015 240 FTKPAKKQTEDYITGRYG 257
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-256 |
4.69e-165 |
|
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: 456.37 E-value: 4.69e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNTQDIALL 89
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTE 249
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 490994015 250 DYITGRY 256
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-239 |
3.66e-144 |
|
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: 402.71 E-value: 3.66e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHqsGYSLSGGQQQRLCIARGIAI 170
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-257 |
2.88e-130 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 369.11 E-value: 2.88e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNIL 80
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 81 TNTQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ 160
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARI--NGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFM---------YLGELI 231
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLV 238
|
250 260
....*....|....*....|....*.
gi 490994015 232 EFSNTDDLFTKPAKKQTEDYITGRYG 257
Cdd:PRK14243 239 EFDRTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-257 |
1.57e-117 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 336.36 E-value: 1.57e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTED 250
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 490994015 251 YITGRYG 257
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-257 |
3.28e-104 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 302.53 E-value: 3.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKL--SRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKL-NGLvkSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
250
....*....|
gi 490994015 248 TEDYITGRYG 257
Cdd:PRK14267 244 TEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-255 |
1.62e-98 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 287.96 E-value: 1.62e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTntQDIALL 89
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK--MDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKL-SRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK14247 81 RRRVQMVFQIPNPIPnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*...
gi 490994015 248 TEDYITGR 255
Cdd:PRK14247 241 TEKYVTGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-257 |
1.84e-91 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 270.75 E-value: 1.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELI--TELKQDYTVVIVTHNMQQAARCSDHTAFMY-----LGELIEFSNTDDLFTKP 243
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 490994015 244 AKKQTEDYITGRYG 257
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-252 |
1.25e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 226.80 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQT 248
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
....
gi 490994015 249 EDYI 252
Cdd:COG1126 233 RAFL 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-257 |
1.17e-71 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 220.74 E-value: 1.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 4 VNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILtNT 83
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIF-NY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
250
....*....|....
gi 490994015 244 AKKQTEDYITGRYG 257
Cdd:PRK14271 254 KHAETARYVAGLSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-255 |
2.91e-71 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 219.15 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQ-RAEGEILLDGDNILTntQDIALL 89
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKiKVDGKVLYFGKDIFQ--IDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK14246 89 RKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQT 248
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....*..
gi 490994015 249 EDYITGR 255
Cdd:PRK14246 249 EKYVIGR 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-225 |
6.33e-69 |
|
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: 211.62 E-value: 6.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDIALLR 90
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFM 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-243 |
6.47e-67 |
|
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: 215.54 E-value: 6.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NTQ 84
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL-----LRPTSGSILFDGKDLTKlSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKL-HQsgysLSGGQQ 159
Cdd:COG1123 336 SLRELRRRVQMVFQDPYsslnPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHE----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTD 237
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
....*.
gi 490994015 238 DLFTKP 243
Cdd:COG1123 491 EVFANP 496
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-243 |
7.98e-66 |
|
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: 204.10 E-value: 7.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltNTQDIALL 89
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDI--TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:COG1122 74 RRKVGLVFQNPDDqlFAPTVEEDVAFGPENL-GLPREEIRERVEEALELVGLE----HLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-241 |
1.09e-65 |
|
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: 203.89 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNI--LTNTQDIAL 88
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPDS--GEVLIDGEDIsgLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lRAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03261 76 -RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-241 |
2.89e-63 |
|
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: 197.89 E-value: 2.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLDGDNILT-NTQDIALL 89
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI--IGLLRPD---SGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQRLCIARG 167
Cdd:COG1127 81 RRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMpSE----LSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-229 |
3.35e-62 |
|
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: 193.17 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILTNTQDIALLR 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIA 169
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
4.07e-62 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 198.78 E-value: 4.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVnatpgKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGd 77
Cdd:COG3842 1 MAMP-----ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagF--------ETPDSGRILLDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 78 niltntQDIALLRA---KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALtkaalwnetkDKLHQSGYS 153
Cdd:COG3842 67 ------RDVTGLPPekrNVGMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIRARVAELL----------ELVGLEGLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 ------LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHT 222
Cdd:COG3842 130 dryphqLSGGQQQRVALARALAPEPRVLLLDEPLSALDA---KLREEMREELRRlqrelGITFIYVTHDQEEALALADRI 206
|
250 260
....*....|....*....|..
gi 490994015 223 AFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-245 |
1.55e-59 |
|
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: 196.28 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRAEGEILLDGDNILTntQDIAL 88
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL--MGLLPHGGRISGEVLLDGRDLLE--LSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:COG1123 81 RGRRIGMVFQDPMTqlNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 490994015 245 K 245
Cdd:COG1123 236 A 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-233 |
1.76e-59 |
|
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: 187.34 E-value: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltntQDIALLR 90
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-225 |
2.67e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 188.37 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 5 NATPGKLSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGd 77
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagL--------EKPTSGEVLVDG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 78 niltntQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwNETKDKL-HQsgysLS 155
Cdd:COG1116 73 ------KPVTGPGPDRGVVFQEPALLPwLTVLDNVALGLEL-RGVPKAERRERARELLELVGL-AGFEDAYpHQ----LS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFM 225
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLADRVVVL 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-230 |
1.07e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNTQDIALLR 90
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-----DPPTSGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEklsRTDMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRE---RKFDRERALELLERLGL---PPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-239 |
2.03e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 185.27 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNTQDIallR 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPT---SGEVRVLGEDVARDPAEV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLY-GLPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-225 |
2.98e-58 |
|
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: 184.21 E-value: 2.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFH--ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNTQDIALL 89
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDL--TKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKP-TPFPM-SIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03225 74 RRKVGLVFQNPdDQFFGpTVEEEVAFGLENL-GLPEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-243 |
1.15e-57 |
|
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: 184.96 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK-----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNT-Q 84
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITAKKkK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRL 162
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGL---DEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 490994015 241 TKP 243
Cdd:TIGR04521 232 SDV 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-252 |
3.39e-57 |
|
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: 182.50 E-value: 3.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltNTQDIALL 89
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE--PT---SGEIFIDGEDI--REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSRTDMDERVQWALTKAALwnETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIAL-VPKLLKWPKEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*.
gi 490994015 247 QTEDYI 252
Cdd:cd03295 231 FVAEFV 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-241 |
3.48e-57 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 182.94 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDNILT-NTQDIAll 89
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKP---SSGEVLLDGRDLASlSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 rAKVGMVFQKPT-PFPMSIYDNIAFG----VRLFEKLSRTDmDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCI 164
Cdd:COG1120 75 -RRIAYVPQEPPaPFGLTVRELVALGryphLGLFGRPSAED-REAVEEALERTGLE----HLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-233 |
2.35e-56 |
|
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: 180.01 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDI 86
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL-----LKPTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAK-VGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAAlwNETKDKLHQSGYSLSGGQQQR 161
Cdd:cd03257 77 RKIRRKeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-244 |
5.70e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 182.65 E-value: 5.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfelypeqrA------EGEILLDGDNILTN-- 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII-----------AgletpdSGRIVLNGRDLFTNlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 83 TQDiallRaKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERV-QWaLTKAALwnetkDKL-----HQsgysLS 155
Cdd:COG1118 72 PRE----R-RVGFVFQHYALFPhMTVAENIAFGLRV-RPPSKAEIRARVeEL-LELVQL-----EGLadrypSQ----LS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250
....*....|.
gi 490994015 234 SNTDDLFTKPA 244
Cdd:COG1118 216 GTPDEVYDRPA 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-244 |
8.51e-56 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 182.19 E-value: 8.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGdniltntQD 85
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagL--------EDPTSGEILIGG-------RD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALtkaalwnetkDKLHQSGY------SLS 155
Cdd:COG3839 67 VTDLPPKdrnIAMVFQSYALYPhMTVYENIAFPLKL-RKVPKAEIDRRVREAA----------ELLGLEDLldrkpkQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPIStgRiEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKL--R-VEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
250
....*....|....
gi 490994015 231 IEFSNTDDLFTKPA 244
Cdd:COG3839 213 QQVGTPEELYDRPA 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-243 |
4.81e-54 |
|
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: 174.61 E-value: 4.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEqrAEGEILLDGDNIltNTQDI 86
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRA---LAGLERP--WSGEVTFDGRPV--TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPT----PFpMSIYDNIAFGVRLfekLSRTDMDERVQWALTKAALWNETKDKL-HQsgysLSGGQQQR 161
Cdd:COG1124 75 KAFRRRVQMVFQDPYaslhPR-HTVDRILAEPLRI---HGLPDREERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
....
gi 490994015 240 FTKP 243
Cdd:COG1124 227 LAGP 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-221 |
6.01e-54 |
|
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: 173.43 E-value: 6.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG----KFHALKNINLDITKNQVTAFIGPSGCGKSTLLR---TFnkmfelypEQRAEGEILLDGdniltnt 83
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiaGL--------ERPTSGEVLVDG------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQR 161
Cdd:cd03293 66 EPVTGPGPDRGYVFQQDALLPwLTVLDNVALGLEL-QGVPKAEARERAEELLELVGL-SGFENAYpHQ----LSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDH 221
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-218 |
1.21e-53 |
|
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: 172.67 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG----KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNTQ 84
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-----DRPTSGEVRVDGTDIskLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPL-LLAGVPKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARC 218
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYA 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-232 |
1.36e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.92 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG----KFHALKNINLDITKNQVTAFIGPSGCGKSTLLR--------TfnkmfelypeqraEGEILLDGDN 78
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilggldrpT-------------SGEVLIDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 79 ILT-NTQDIALLRA-KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLS 155
Cdd:COG1136 72 ISSlSERELARLRRrHIGFVFQFFNLLPeLTALENVALPLLL-AGVSRKERRERARELLERVGL----GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-244 |
2.86e-53 |
|
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: 174.86 E-value: 2.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQRAEGEILLDGDNILTNTQ-D 85
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDLLKLSEkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAK-VGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwNETKDKL----HQsgysLSG 156
Cdd:COG0444 80 LRKIRGReIQMIFQDPMtslnPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLdrypHE----LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|
gi 490994015 235 NTDDLFTKPA 244
Cdd:COG0444 234 PVEELFENPR 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-244 |
7.06e-53 |
|
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: 171.27 E-value: 7.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGDNILtntqDIA 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLiagF--------ETPTSGEILLDGKDIT----NLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03300 69 PHKRPVNTVFQNYALFPhLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 GIAIRPEVLLLDEPCSALDPistgRI-EELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDL----KLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
....
gi 490994015 241 TKPA 244
Cdd:cd03300 220 EEPA 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-225 |
3.43e-52 |
|
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: 167.17 E-value: 3.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG--KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNTQDIAL 88
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 168
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFM 225
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DRIIVL 167
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-182 |
6.76e-52 |
|
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: 165.90 E-value: 6.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNTQDIALLRAKVGMVFQKPTPFP- 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL-----LSPTEGTILLDGQDL--TDDERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 105 MSIYDNIAFGVRLFEkLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:pfam00005 74 LTVRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-252 |
1.25e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 171.03 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NTQD 85
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ERPTSGSVLVDGVDLTAlSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKptpFP-MS---IYDNIAFGVRLfEKLSRTDMDERVqwaltkaalwNET------KDKLHQsgY--S 153
Cdd:COG1135 77 LRAARRKIGMIFQH---FNlLSsrtVAENVALPLEI-AGVPKAEIRKRV----------AELlelvglSDKADA--YpsQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|.
gi 490994015 232 EFSNTDDLFTKPAKKQTEDYI 252
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFL 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-244 |
1.33e-51 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 170.27 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTntQDIALLRAKVGMVFQ 98
Cdd:COG1125 11 YPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEP-----TSGRILIDGEDIRD--LDPVELRRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNET-KDKL-HQsgysLSGGQQQRLCIARGIAIRPEVL 175
Cdd:COG1125 84 QIGLFPhMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEEyRDRYpHE----LSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 176 LLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-239 |
2.80e-51 |
|
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: 177.72 E-value: 2.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGKFH--ALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltNTQDI 86
Cdd:COG2274 472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKL---LLGLYEPT--SGRILIDGIDL--RQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTDM-DERVQWALTKAALWNETKD-------KLHQSGYSLSGGQ 158
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLG--------DPDAtDEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDD 238
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEE 695
|
.
gi 490994015 239 L 239
Cdd:COG2274 696 L 696
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-252 |
9.77e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.04 E-value: 9.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDIALLRAKV 93
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 94 GMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRP 172
Cdd:PRK09493 80 GMVFQQFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 173 EVLLLDEPCSALDPistgrieELITE-LK--QD-----YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:PRK09493 156 KLMLFDEPTSALDP-------ELRHEvLKvmQDlaeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
....*...
gi 490994015 245 KKQTEDYI 252
Cdd:PRK09493 229 SQRLQEFL 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
9.77e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 163.34 E-value: 9.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVNAtpgkLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGdnil 80
Cdd:COG1121 1 MMMMPA----IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVRLFG---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 81 tntQDIALLRAKVGMVFQKPT---PFPMSIYDNIAFG----VRLFEKLSRTDmDERVQWALTKAALWnetkDKLHQSGYS 153
Cdd:COG1121 68 ---KPPRRARRRIGYVPQRAEvdwDFPITVRDVVLMGrygrRGLFRRPSRAD-REAVDEALERVGLE----DLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMyLGELIE 232
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLL-NRGLVA 218
|
....*....
gi 490994015 233 FSNTDDLFT 241
Cdd:COG1121 219 HGPPEEVLT 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-210 |
1.20e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 171.50 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 7 TPGKLSVRNLNFYYGKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltntQD 85
Cdd:COG1132 336 VRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD--PT---SGRILIDGVDI----RD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IAL--LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeKLSRTDmdERVQWALTKAALW---NETKDKLH----QSGYSLSG 156
Cdd:COG1132 407 LTLesLRRQIGVVPQDTFLFSGTIRENIRYG-----RPDATD--EEVEEAAKAAQAHefiEALPDGYDtvvgERGVNLSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-243 |
2.08e-49 |
|
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: 162.37 E-value: 2.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 21 GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIlTNTQDIAL--LRAKVGMVFQ 98
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGTDL-TLLSGKELrkARRRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KptpFPM----SIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:cd03258 90 H---FNLlssrTVFENVALPLEI-AGVPKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 175 LLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-239 |
3.83e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 162.60 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILT--NTQDI 86
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDeeNLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 allRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfE--KLSRTDMDERVQWALTKAALWnetkDKLHQSGYSL 154
Cdd:TIGR04520 76 ---RKKVGMVFQNP--------DNqfvgatveddVAFGL---EnlGVPREEMRKRVDEALKLVGME----DFRDREPHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIstGRIE--ELITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLGEL 230
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK--GRKEvlETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKI 214
|
250
....*....|....*.
gi 490994015 231 IE-------FSNTDDL 239
Cdd:TIGR04520 215 VAegtpreiFSQVELL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-252 |
6.00e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 161.33 E-value: 6.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI----LTNTQDI 86
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQFdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCI 164
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENlIEAPCKVL-GLSKEQAREKAMKLLARLRL----TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSnTDDLFTKP 243
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
....*....
gi 490994015 244 AKKQTEDYI 252
Cdd:COG4161 232 QTEAFAHYL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-253 |
1.17e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI----LTNTQDI 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNHFdfskTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRTDMDERVQWALTKAALwNETKDK--LHqsgysLSGGQQQRL 162
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNlIEAPCRVL-GLSKDQALARAEKLLERLRL-KPYADRfpLH-----LSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEfSNTDDLFT 241
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFT 229
|
250
....*....|..
gi 490994015 242 KPAKKQTEDYIT 253
Cdd:PRK11124 230 QPQTEAFKNYLS 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-229 |
1.27e-47 |
|
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: 157.21 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIlTNTQDIALLR 90
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKT---IMGLLP--PRSGSIRFDGRDI-TGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfekLSRTDMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03224 75 AGIGYVPEGRRIFPeLTVEENLLLGAYA---RRRAKRKARLERVY---ELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-239 |
1.98e-47 |
|
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: 165.32 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNTQ 84
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTDM-DERVQWALTKAALWNETKD-------KLHQSGYSLSG 156
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAGTIRENLRLG--------RPDAsDEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNT 236
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTH 555
|
...
gi 490994015 237 DDL 239
Cdd:COG4988 556 EEL 558
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-220 |
2.35e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.53 E-value: 2.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNF-YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILT-NTQDIAL 88
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL--VEP---TSGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKptpFP----MSIYDNIAFGvRL---------FEKLSRTDMdERVQWALTKAALwnetKDKLHQSGYSLS 155
Cdd:COG3638 78 LRRRIGMIFQQ---FNlvprLSVLTNVLAG-RLgrtstwrslLGLFPPEDR-ERALEALERVGL----ADKAYQRADQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSD 220
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-254 |
4.48e-47 |
|
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: 157.42 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNI--LTNTQDIALLRAKVGMVFQKPTP 102
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--P---TSGKVLIDGQDIaaMSRKELRELRRKKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 FP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:cd03294 114 LPhRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 182 SALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITG 254
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-254 |
5.48e-47 |
|
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: 160.02 E-value: 5.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNIlTNTQDIALL---RAKVGMVFQKPT 101
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIE--P---TAGQIFIDGENI-MKQSPVELRevrRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 PFP-MSIYDNIAFGVrlfeKLSRTDMDERVQWALTKAALWNeTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:TIGR01186 82 LFPhMTILQNTSLGP----ELLGWPEQERKEKALELLKLVG-LEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 181 CSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITG 254
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-231 |
6.15e-47 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 156.06 E-value: 6.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLlrtFNKMFELYPeqRAEGEILLDGDNIlTNTQDIALLR 90
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTL---FNLISGFLR--PTSGSVLFDGEDI-TGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLS---------RTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQ 160
Cdd:cd03219 75 LGIGRTFQIPRLFPeLTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLA----DLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-229 |
7.94e-47 |
|
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: 153.17 E-value: 7.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGDNILTNtqDIALLRA 91
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI--AGLLKP---TSGEILIDGKDIAKL--PLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQkptpfpmsiydniafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAIR 171
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 172 PEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-252 |
1.02e-46 |
|
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: 155.79 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltnTQDIALLR 90
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL--LKPD---SGSILIDGEDV---RKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPtPFP--MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGI 168
Cdd:COG4555 74 RQIGVLPDER-GLYdrLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
....*
gi 490994015 248 TEDYI 252
Cdd:COG4555 228 LEDAF 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-230 |
2.13e-46 |
|
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: 152.55 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNTQDIallR 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKKEPEEV---K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgySLSGGQQQRLCIARGIA 169
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENL-----------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY-TVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-213 |
6.64e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.90 E-value: 6.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNILT-NTQDIALLRAKVGMV 96
Cdd:COG2884 11 YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKL------LYGEERPtSGQVLVNGQDLSRlKRREIPYLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 97 FQKptpFP----MSIYDNIAFGVRLFEKlSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRP 172
Cdd:COG2884 85 FQD---FRllpdRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490994015 173 EVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQ 213
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLE 198
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-252 |
2.76e-45 |
|
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: 155.19 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltntQDIALL- 89
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGG-------RDITRLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 --RAKVGMVFQKPTPFP-MSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALWNeTKDKlhqsgY--SLSGGQQQRLCI 164
Cdd:TIGR03265 73 pqKRDYGIVFQSYALFPnLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPG-SERK-----YpgQLSGGQQQRVAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDpistGRI-EELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:TIGR03265 146 ARALATSPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
250
....*....|....
gi 490994015 239 LFTKPAKKQTEDYI 252
Cdd:TIGR03265 222 IYRHPATPFVADFV 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-243 |
4.20e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 151.88 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 3 MVNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT- 81
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL-----ETPDSGEIRVGGEEIRLk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 ----------NTQDIALLRAKVGMVFQKptpFP----MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWnetkDKL 147
Cdd:COG4598 76 pdrdgelvpaDRRQLQRIRTRLGMVFQS---FNlwshMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA----DKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 148 HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistgrieELITE-LK--QDY-----TVVIVTHNMQQAARCS 219
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmRDLaeegrTMLVVTHEMGFARDVS 221
|
250 260
....*....|....*....|....
gi 490994015 220 DHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-252 |
7.52e-45 |
|
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: 150.56 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHaLKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNIlTNTQDIallR 90
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNGKDI-TNLPPE---K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVqwaLTKAALWNETKdKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKK-RKVDKKEIERKV---LEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*
gi 490994015 248 TEDYI 252
Cdd:cd03299 226 VAEFL 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
21-252 |
2.27e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 152.65 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 21 GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NTQDIALLRAKVGMVFQK 99
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQDLTAlSEKELRKARRQIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 ptpFPM----SIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVL 175
Cdd:PRK11153 91 ---FNLlssrTVFDNVALPLEL-AGTPKAEIKARVTELLELVGL----SDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 176 LLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYI 252
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-244 |
1.06e-43 |
|
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: 147.87 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltntQDIALLRAK 92
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGEDA----TDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVFQKPTPFP-MSIYDNIAFGVRL---FEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGI 168
Cdd:cd03296 76 VGFVFQHYALFRhMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ----LSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 169 AIRPEVLLLDEPCSALDpisTGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:cd03296 152 AVEPKVLLLDEPFGALD---AKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
.
gi 490994015 244 A 244
Cdd:cd03296 229 A 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-230 |
1.66e-43 |
|
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: 146.63 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltntQDIALLR 90
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGG-------RDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03301 69 PKdrdIAMVFQNYALYPhMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 167 GIAIRPEVLLLDEPCSALDpiSTGRIeELITELK-----QDYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLD--AKLRV-QMRAELKrlqqrLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-223 |
8.62e-43 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 144.60 E-value: 8.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGdniltntQDIALLRA 91
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKA---ILGLLK--PTSGSIRVFG-------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQK---PTPFPMSIYDNIAFG----VRLFEKLSRTDMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCI 164
Cdd:cd03235 69 RIGYVPQRrsiDRDFPISVRDVVLMGlyghKGLFRRLSKADK-AKVDEALERVGL----SELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTA 223
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-252 |
1.01e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 149.22 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPgKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltntQD 85
Cdd:PRK11607 16 LTP-LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDG-------VD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALL---RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQR 161
Cdd:PRK11607 83 LSHVppyQRPINMMFQSYALFPhMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIE-ELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
250
....*....|...
gi 490994015 240 FTKPAKKQTEDYI 252
Cdd:PRK11607 238 YEHPTTRYSAEFI 250
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-231 |
1.62e-42 |
|
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: 142.96 E-value: 1.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILT-NTQDIALLR 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-----SSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVfqkptpfpmsiydniafgvrlfekLSRTDMDervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:cd03214 76 AYVPQA------------------------LELLGLA-----------------HLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-252 |
1.77e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.89 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVnatpgklSVRNLNfyyGKFHA---LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGD 77
Cdd:PRK11264 1 MSAI-------EVKNLV---KKFHGqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 78 NILTNTQD-IALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNEtkdklhQSGY--S 153
Cdd:PRK11264 71 RSLSQQKGlIRQLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK------ETSYprR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|
gi 490994015 233 FSNTDDLFTKPAKKQTEDYI 252
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFL 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-254 |
2.50e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.11 E-value: 2.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNkmfelYPEQRAEGEILLDGDNI---------- 79
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-----FLEKPSEGSIVVNGQTInlvrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 -LTNTQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetkDKLHQSGY--SLS 155
Cdd:PRK10619 80 kVADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI-----DERAQGKYpvHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
250 260
....*....|....*....|
gi 490994015 235 NTDDLFTKPAKKQTEDYITG 254
Cdd:PRK10619 235 APEQLFGNPQSPRLQQFLKG 254
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-239 |
3.24e-42 |
|
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: 143.83 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKST----LLRTFNkmfelyPEqraEGEILLDGDNIltNTQDIALLRAKVGMVFQKPT 101
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTvvslLERFYD------PT---SGEILLDGVDI--RDLNLRWLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 PFPMSIYDNIAFGvrlfeKLSRTDmdERVQWALTKAALWN---ETKDKLH----QSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:cd03249 88 LFDGTIAENIRYG-----KPDATD--EEVEEAAKKANIHDfimSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 175 LLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-252 |
8.23e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.59 E-value: 8.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHalKNINLDITKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGDNILtnTQDIA 87
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLiagF--------LPPDSGRILWNGQDLT--ALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:COG3840 70 --ERPVSMLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGL----AGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 giAI---RPeVLLLDEPCSALDPIStgRIE--ELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG3840 143 --CLvrkRP-ILLLDEPFSALDPAL--RQEmlDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|...
gi 490994015 240 FTKPAKKQTEDYI 252
Cdd:COG3840 218 LDGEPPPALAAYL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-232 |
9.73e-42 |
|
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: 149.92 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 2 SMVNATPGKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNI 79
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQS---GSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 ltNTQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVrlfEKLSrtdmDERVQWALTKAAL--WNETKDK-----LHQSGY 152
Cdd:COG4987 400 --RDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLAR---PDAT----DEELWAALERVGLgdWLAALPDgldtwLGEGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-247 |
1.01e-41 |
|
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: 142.43 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIlTN--TQDIAl 88
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKA---ISGLLP--PRSGSIRFDGEDI-TGlpPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lRAKVGMVfqkptP-----FP-MSIYDNIAFGVRLfeKLSRTDMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRL 162
Cdd:COG0410 77 -RLGIGYV-----PegrriFPsLTVEENLLLGAYA--RRDRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
....*.
gi 490994015 242 KPAKKQ 247
Cdd:COG0410 226 DPEVRE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-232 |
1.44e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.62 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGdnILTNTQDIA 87
Cdd:PRK13635 5 IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPEA---GTITVGG--MVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKP-TPF-PMSIYDNIAFGVrlfEK--LSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFvGATVQDDVAFGL---ENigVPREEMVERVDQALRQVGM----EDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPIstGRIE--ELITELK--QDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-244 |
3.10e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-----------GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNI 79
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--P---TSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 LT-NTQDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKL-HQsgy 152
Cdd:COG4608 83 TGlSGRELRPLRRRMQMVFQDP--YaslnPrMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYpHE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 153 sLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpIStgrIE----ELITELKQDY--TVVIVTHNMQQAARCSDHTAFMY 226
Cdd:COG4608 158 -FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMY 232
|
250
....*....|....*...
gi 490994015 227 LGELIEFSNTDDLFTKPA 244
Cdd:COG4608 233 LGKIVEIAPRDELYARPL 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
3.49e-41 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 140.72 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK--FHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMfeLYPEQRA-EGEILLDGDNILTNTQDIa 87
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTL----KM--LTGELRPtSGTAYINGYSIRTDRKAA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfeK-LSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIA 165
Cdd:cd03263 74 --RQSLGYCPQFDALFDeLTVREHLRFYARL--KgLPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-225 |
4.53e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 144.70 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVNATPGK--LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdn 78
Cdd:PRK09452 3 KLNKQPSSLSplVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 79 iltntQDIALLRAK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysL 154
Cdd:PRK09452 76 -----QDITHVPAEnrhVNTVFQSYALFPhMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQ----L 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDpiSTGRiEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFM 225
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALD--YKLR-KQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-231 |
1.16e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.34 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGK---FH--ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNTQDIA 87
Cdd:PRK13637 5 IENLTHIYMEgtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKP---TSGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAAL-WNETKDKlhqSGYSLSGGQQQRLCI 164
Cdd:PRK13637 80 DIRKKVGLVFQYPEYqlFEETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-231 |
1.58e-40 |
|
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: 140.17 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLlrtFNKMFELYPEQraEGEILLDGdniltntQDIALL- 89
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTL---FNLITGFYRPT--SGRILFDG-------RDITGLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 ---RAKVGMV--FQKPTPFP-MSIYDNIAFGV------RLFEKLSRT--------DMDERVQWALTKAALwnetKDKLHQ 149
Cdd:COG0411 73 phrIARLGIArtFQNPRLFPeLTVLENVLVAAharlgrGLLAALLRLprarreerEARERAEELLERVGL----ADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 150 SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYL 227
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDF 228
|
....
gi 490994015 228 GELI 231
Cdd:COG0411 229 GRVI 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-244 |
3.47e-40 |
|
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: 141.09 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 42 IGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnTQDIALLRAkVGMVFQKPTPFP-MSIYDNIAFGVRLfEK 120
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGF-----EQPDSGSIMLDGEDV---TNVPPHLRH-INMVFQSYALFPhMTVEENVAFGLKM-RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 121 LSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIE-ELITEL 199
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490994015 200 KQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:TIGR01187 148 EQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-217 |
4.56e-40 |
|
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: 137.76 E-value: 4.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNT-QDIALLRAKVGMVF 97
Cdd:TIGR02673 11 YPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA-----LTPSRGQVRIAGEDVNRLRgRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 98 QKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:TIGR02673 86 QDFRLLPdRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490994015 177 LDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAAR 217
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDR 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-242 |
6.48e-40 |
|
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: 137.74 E-value: 6.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQraEGEILLDGDNIltNTQDIA 87
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR---FYDPQ--KGQILIDGIDI--RDISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklSRTDMDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQQ 160
Cdd:cd03254 74 SLRSMIGVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKlpngydtVLGENGGNLSQGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELL 225
|
..
gi 490994015 241 TK 242
Cdd:cd03254 226 AK 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
8.34e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 139.21 E-value: 8.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK-FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNTQDIALL 89
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTP--FPMSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRLCIARG 167
Cdd:PRK13636 81 RESVGMVFQDPDNqlFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-221 |
4.03e-39 |
|
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: 136.16 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG-KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlTNTQDIAL- 88
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGSVLIDGTDI-NKLKGKALr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 -LRAKVGMVFQKPTPFP-MSIYDNIAFG-----------VRLFEKLSRtdmdERVQWALTKAALwnetKDKLHQSGYSLS 155
Cdd:cd03256 75 qLRRQIGMIFQQFNLIErLSVLENVLSGrlgrrstwrslFGLFPKEEK----QRALAALERVGL----LDKAYQRADQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDH 221
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-257 |
8.85e-39 |
|
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: 135.12 E-value: 8.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlTNTQ--DIA 87
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-----SSGSILLEGTDI-TKLRgkKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFGvRL---------FEKLSRTDMdERVQWALTKAALwnetKDKLHQSGYSLSGG 157
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIErLTVLENVLHG-RLgykptwrslLGRFSEEDK-ERALSALERVGL----ADKAYQRADQLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIefsn 235
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIV---- 225
|
250 260
....*....|....*....|..
gi 490994015 236 tddlFTKPAKKQTEDYITGRYG 257
Cdd:TIGR02315 226 ----FDGAPSELDDEVLRHIYG 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-244 |
1.68e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 137.54 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNT---QDIA 87
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDVTHRSiqqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 llrakvgMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetkdklhqSGYS------LSGGQQQ 160
Cdd:PRK11432 82 -------MVFQSYALFPhMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDL----------AGFEdryvdqISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....*.
gi 490994015 239 LFTKPA 244
Cdd:PRK11432 224 LYRQPA 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-243 |
2.19e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.21 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK-FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNTQDIALL 89
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK--PT---SGEVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTP--FPMSIYDNIAFGvRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARG 167
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-245 |
3.60e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 135.15 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLdGDNILTNT---QDIALLRAKVGMVFQKPT 101
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-----QPTSGTVTI-GERVITAGkknKKLKPLRKKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 P--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13634 96 HqlFEETVEKDICFGPMNF-GVSEEDAKQKAREMIELVGL---PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 180 PCSALDPisTGRIE--ELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAK 245
Cdd:PRK13634 172 PTAGLDP--KGRKEmmEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
8.05e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.45 E-value: 8.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMvnatpgkLSVRNLNFYYGKF----HALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKM--FeLYPEqraEGEILL 74
Cdd:COG4525 1 MSM-------LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIagF-LAPS---SGEITL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 75 DGDNILTNTQDiallRakvGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYS 153
Cdd:COG4525 67 DGVPVTGPGAD----R---GVVFQKDALLPwLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGL----ADFARRRIWQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQA 215
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-243 |
5.14e-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: 5.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-----------GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypeQRAEGEILLDGDNI 79
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 LT-NTQDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFE-KLSRTDMDERVQWALTKAALWNETKDKL-HQsg 151
Cdd:COG4172 350 DGlSRRALRPLRRRMQVVFQDP--FgslsPrMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRYpHE-- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 152 ysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:COG4172 426 --FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250
....*....|....
gi 490994015 230 LIEFSNTDDLFTKP 243
Cdd:COG4172 504 VVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-220 |
1.15e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 130.63 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGK-FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRaeGEILLDGDNIltNTQDIALLRA 91
Cdd:PRK13647 7 VEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG---IYLPQR--GRVKVMGREV--NAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQKPTP--FPMSIYDNIAFGVRLFEkLSRTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:PRK13647 80 KVGLVFQDPDDqvFSSTVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSD 220
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWAD 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-210 |
3.50e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 128.12 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK--FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltntQDIAL 88
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDV----RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 --LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsrTDMDERVQWALtKAALWNETKDKLHQsGY---------SLSGG 157
Cdd:cd03251 72 asLRRQIGLVSQDVFLFNDTVAENIAYGRP-------GATREEVEEAA-RAANAHEFIMELPE-GYdtvigergvKLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-215 |
5.27e-36 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.38 E-value: 5.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNTQDIALLRAKVGMVFQ 98
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQS---GAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHC----LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490994015 177 LDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQA 215
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-244 |
1.25e-35 |
|
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: 132.89 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK----FHALKNINLDITKNQVTAFIGPSGCGKS----TLLRtfnkmfeLYPEQ--RAEGEILLDGDNIL 80
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-------LLPDPaaHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 81 TntQDIALLRA----KVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwNETKDKL----H 148
Cdd:COG4172 80 G--LSERELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRLdaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 149 QsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMY 226
Cdd:COG4172 156 Q----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*...
gi 490994015 227 LGELIEFSNTDDLFTKPA 244
Cdd:COG4172 232 QGEIVEQGPTAELFAAPQ 249
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-252 |
1.49e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 130.22 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNILTNTQD--IALLRAKVGMVFQKPTP 102
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE--P---TAGEVLIDGEDITKLSKKelRELRRKKMSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 FP-MSIYDNIAFG--VRlfeKLSRTDMDERVQWALTKAAL--WnetKDKL-HQsgysLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:COG4175 117 LPhRTVLENVAFGleIQ---GVPKAERRERAREALELVGLagW---EDSYpDE----LSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 177 LDEPCSALDPIstgrI-----EELIT---ELKQdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAkkqt 248
Cdd:COG4175 187 MDEAFSALDPL----IrremqDELLElqaKLKK--TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPA---- 256
|
....
gi 490994015 249 EDYI 252
Cdd:COG4175 257 NDYV 260
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-212 |
1.54e-35 |
|
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: 126.16 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltnTQ-D 85
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKL---LAGLYKPT--SGSVLLDGTDI---RQlD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEklsrtdmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQ 158
Cdd:cd03245 73 PADLRRNIGYVPQDVTLFYGTLRDNITLGAPLAD-------DERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
15-244 |
1.56e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.43 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 15 NLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltntQDIALLRAK-- 92
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQTSGHIRFHG-------TDVSRLHARdr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 -VGMVFQKPTPFP-MSIYDNIAFGVRLF---EKLSRTDMDERVQWALTKAALwnetkDKLHQSGYS-LSGGQQQRLCIAR 166
Cdd:PRK10851 75 kVGFVFQHYALFRhMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEMVQL-----AHLADRYPAqLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 GIAIRPEVLLLDEPCSALDpiSTGRIE------ELITELKqdYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
....
gi 490994015 241 TKPA 244
Cdd:PRK10851 226 REPA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-231 |
1.89e-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: 125.87 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDI---TKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNTQDIAL--LRAKVGMVFQKP 100
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPD-----GGTIVLNGTVLFDSRKKINLppQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 TPFP-MSIYDNIAFGVRlfeKLSRTDMDERVQWALTKAALwnetkDKLHQSG-YSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:cd03297 85 ALFPhLNVRENLAFGLK---RKRNREDRISVDELLDLLGL-----DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 179 EPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-241 |
1.94e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.05 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNT-----Q 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQS---GTVFLGDKPISMLSsrqlaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAkvgmvfQKPTPFPMSIYDNIAFG----VRLFEKLSRTDmDERVQWALTKAALwNETKDKLHQsgySLSGGQQQ 160
Cdd:PRK11231 77 RLALLPQ------HHLTPEGITVRELVAYGrspwLSLWGRLSAED-NARVNQAMEQTRI-NHLADRRLT---DLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
..
gi 490994015 240 FT 241
Cdd:PRK11231 226 MT 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-239 |
2.24e-35 |
|
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: 125.95 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNTQDIallRAK 92
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTS---GRATVAGHDVVREPREV---RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIARGIAIR 171
Cdd:cd03265 75 IGIVFQDLSVDDeLTGWENLYIHARLY-GVPGAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 172 PEVLLLDEPCSALDPISTGRIEELITELK--QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-225 |
2.55e-35 |
|
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: 125.06 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNF-YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTqdialLR 90
Cdd:cd03226 1 RIENISFsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL-----IKESSGSILLNGKPIKAKE-----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPtpfpmsiyDNIAFGVRLFEKLSRTDMD-----ERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIA 165
Cdd:cd03226 71 KSIGYVMQDV--------DYQLFTDSVREELLLGLKEldagnEQAETVLKDLDLY-ALKERHPLS---LSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-213 |
3.32e-35 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 132.68 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNF-YYG-KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltnTQ-D 85
Cdd:TIGR03375 462 GEIEFRNVSFaYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKL---LLGLYQPT--EGSVLLDGVDI---RQiD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEklsrtdmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQ 158
Cdd:TIGR03375 534 PADLRRNIGYVPQDPRLFYGTLRDNIALGAPYAD-------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQ 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQ 213
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-247 |
7.63e-35 |
|
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: 125.08 E-value: 7.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELYPeqRAEGEILLDGdniltntQDIALL- 89
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDG-------QDITHLp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 ---RAKVGMVF--QKPTPF-PMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:TIGR04406 70 mheRARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:TIGR04406 146 IARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
....*
gi 490994015 243 PAKKQ 247
Cdd:TIGR04406 226 EKVRR 230
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-218 |
8.45e-35 |
|
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: 123.88 E-value: 8.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNTQDIALLR 90
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLL-----EKFDSGQVYLNGQETppLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKptpFPM----SIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALWNetkdKLHQSGYSLSGGQQQRLCIAR 166
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGL-KYKKLSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARC 218
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELnDEGKTIIIVTHDPEVAKQA 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-211 |
1.21e-34 |
|
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: 123.67 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNTQdIALLRAKVGMV 96
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVsdLRGRA-IPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 97 FQKPTPFP-MSIYDNIAFGVRLFEKlSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVL 175
Cdd:cd03292 84 FQDFRLLPdRNVYENVAFALEVTGV-PPREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 490994015 176 LLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHN 211
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-239 |
3.08e-34 |
|
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: 125.20 E-value: 3.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltnTQDIALLRAKVGMVFQ 98
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDV---VREPRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KPTPFP-MSIYDNIAFGVRLFEkLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:TIGR01188 74 YASVDEdLTGRENLEMMGRLYG-LPKDEAEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 178 DEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-215 |
3.25e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 126.30 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltntQDIALLRA 91
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLFIGEKRM----NDVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWA---LTKAALWnETKDKlhqsgySLSGGQQQRLCIARG 167
Cdd:PRK11000 76 GVGMVFQSYALYPhLSVAENMSFGLKL-AGAKKEEINQRVNQVaevLQLAHLL-DRKPK------ALSGGQRQRVAIGRT 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490994015 168 IAIRPEVLLLDEPCSALDPI--STGRIEelITELKQDY--TVVIVTHNMQQA 215
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAAlrVQMRIE--ISRLHKRLgrTMIYVTHDQVEA 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-242 |
3.71e-34 |
|
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: 122.98 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNFYYG--KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelYPEQraeGEILLDGDNIltNTQDIALLRA 91
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY--VPEN---GRVLVDGHDL--ALADPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQKPTPFPMSIYDNIAfgvrlfekLSRTDMD-ERVQWAlTKAALWNETKDKLH--------QSGYSLSGGQQQRL 162
Cdd:cd03252 77 QVGVVLQENVLFNRSIRDNIA--------LADPGMSmERVIEA-AKLAGAHDFISELPegydtivgEQGAGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-232 |
3.94e-34 |
|
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: 122.96 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDIALlrakvgmVFQKPTPFP- 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGKQITEPGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 MSIYDNIAFGV-RLFEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 184 LDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFM------YLGELIE 232
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-222 |
7.16e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 127.79 E-value: 7.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNTQ 84
Cdd:TIGR02857 317 APASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DiaLLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTDM-DERVQWALTKAALWNETKD-------KLHQSGYSLSG 156
Cdd:TIGR02857 392 D--SWRDQIAWVPQHPFLFAGTIAENIRLA--------RPDAsDAEIREALERAGLDEFVAAlpqgldtPIGEGGAGLSG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHT 222
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRI 526
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-212 |
8.01e-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: 122.34 E-value: 8.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNF-YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNILTNTQDIalLRAK 92
Cdd:cd03253 4 ENVTFaYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL---LFRFYDVS--SGSILIDGQDIREVTLDS--LRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVFQKPTPFPMSIYDNIAFGvrlfeKLSRTDmdERVQWALTKAAL------WNETKD-KLHQSGYSLSGGQQQRLCIA 165
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYG-----RPDATD--EEVIEAAKAAQIhdkimrFPDGYDtIVGERGLKLSGGEKQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490994015 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-210 |
8.04e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.53 E-value: 8.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITkNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNTQDIallR 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTP--PS---SGTIRIDGQDVLKQPQKL---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGIA 169
Cdd:cd03264 72 RRIGYLPQEFGVYPnFTVREFLDYIAWL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-243 |
1.32e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 123.02 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNTQDIAL--LRAKVGMVFQKPTP- 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKP---SSGTITIAGYHITPETGNKNLkkLRKKVSLVFQFPEAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 -FPMSIYDNIAFGVRLFEKLSRTDMDERVQWaLTKAALWNETKDKlhqSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:PRK13641 98 lFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 182 SALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-240 |
1.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK---FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNTQDIA 87
Cdd:PRK13642 5 LEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELL--TAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTP--FPMSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALWN-ETKDKLHqsgysLSGGQQQRLCI 164
Cdd:PRK13642 78 NLRRKIGMVFQNPDNqfVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDfKTREPAR-----LSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
11-216 |
1.55e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 120.66 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMF-ELYPEQRAEGEILLDGdniltntQDIALL 89
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL---AAIAgTLSPAFSASGEVLLNG-------RRLTAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RA---KVGMVFQKPTPFP-MSIYDNIAFGVRlfEKLSRTDMDERVQWALTKAALwnetkdklhqSGY------SLSGGQQ 159
Cdd:COG4136 72 PAeqrRIGILFQDDLLFPhLSVGENLAFALP--PTIGRAQRRARVEQALEEAGL----------AGFadrdpaTLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI-TELKQ-DYTVVIVTHNMQQAA 216
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQrGIPALLVTHDEEDAP 198
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-239 |
2.31e-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: 120.71 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNIltnTQDIALLR 90
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKT---LMGLLPVKS--GSIRLDGEDI---TKLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGM--VFQKPTPFP-MSIYDNIAFGVRLFEKLSRtDMDERVqwaltkAALWNETKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:TIGR03410 73 ARAGIayVPQGREIFPrLTVEENLLTGLAALPRRSR-KIPDEI------YELFPVLKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-251 |
8.81e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 8.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 22 KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNTQD--IALLRAKVGMVFQK 99
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKP---TTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 PTP--FPMSIYDNIAFGVRLFeklsRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:PRK13646 94 PESqlFEDTVEREIIFGPKNF----KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 178 DEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKpaKKQTEDY 251
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-230 |
9.04e-33 |
|
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: 119.11 E-value: 9.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGK---FHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNIltNTQD 85
Cdd:cd03248 10 GIVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV---ALLENFYQPQ--GGQVLLDGKPI--SQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsrTDMDERVQWALTKA-----------ALWNETKDKlhqsGYSL 154
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQ-------SCSFECVKEAAQKAhahsfiselasGYDTEVGEK----GSQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGEL 230
Cdd:cd03248 152 SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-241 |
1.90e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFH--ALKNINLDITKNQVTAFIGPSGCGKSTllrtFNKMFE-LYPEQraEGEILLDGdnILTNTQDIAL 88
Cdd:PRK13632 9 KVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKST----ISKILTgLLKPQ--SGEIKIDG--ITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK13632 81 IRKKIGIIFQNPdNQFiGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILA-DKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-210 |
2.02e-32 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 124.36 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY-GKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltntQDI 86
Cdd:PRK11176 340 GDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDL----RDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 AL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRTDMDERvqwalTKAALWNETKDKLHQ--------SGYSLSG 156
Cdd:PRK11176 411 TLasLRNQVALVSQNVHLFNDTIANNIAYART--EQYSREQIEEA-----ARMAYAMDFINKMDNgldtvigeNGVLLSG 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:PRK11176 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-240 |
3.32e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.08 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDgDNILTNT---QDIALLRAKVGMVFQKPT 101
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVP---TQGSVRVD-DTLITSTsknKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 P--FPMSIYDNIAFGVRLFEklsrTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13649 96 SqlFEETVLKDVAFGPQNFG----VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 180 PCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-232 |
3.72e-32 |
|
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: 123.67 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYG--KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltntQDI 86
Cdd:TIGR02203 329 GDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDL----ADY 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 AL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsRTDMDERVQWALTKAALW---NETKDKLH----QSGYSLSGG 157
Cdd:TIGR02203 400 TLasLRRQVALVSQDVVLFNDTIANNIAYGRT------EQADRAEIERALAAAYAQdfvDKLPLGLDtpigENGVLLSGG 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
3.82e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.68 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNI--LTNTQDIALLRAKVGMVFQKPTP 102
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 FP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNetkdklHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK10070 118 MPhMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLEN------YAHSYpdELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 180 PCSALDP-ISTGRIEELIT-ELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITG 254
Cdd:PRK10070 191 AFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-248 |
4.52e-32 |
|
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: 117.64 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELypEQRAEGEILLDGdniltntQDIALL- 89
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGKILLDG-------QDITKLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 ---RAKVGMVF--QKPTPF-PMSIYDNIAfGVRLFEKLSRTDMDERVQwaltkaALWNETK-DKL-HQSGYSLSGGQQQR 161
Cdd:cd03218 69 mhkRARLGIGYlpQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLE------ELLEEFHiTHLrKSKASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
....*...
gi 490994015 241 TKPAKKQT 248
Cdd:cd03218 222 ANELVRKV 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-221 |
5.37e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 118.33 E-value: 5.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNILTNT-QDIALLRA 91
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG--QIAPDH---GEILFDGENIPAMSrSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKdkLHQSgySLSGGQQQRLCIARGIAI 170
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAK--LMPS--ELSGGMARRAALARAIAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDH 221
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADH 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
5.63e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.06 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltnTQDIallR 90
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI--LAPD---SGEVLWDGEPL---DPED---R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVG-M-----VFQKptpfpMSIYDNIAFGVRLfeK-LSRTDMDERVQWALTK---AALWNetkDKLHqsgySLSGGQQQ 160
Cdd:COG4152 71 RRIGyLpeergLYPK-----MKVGEQLVYLARL--KgLSKAEAKRRADEWLERlglGDRAN---KKVE----ELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-231 |
6.84e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.83 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNILTNTQDIALlR 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKI---LSGLY--KPDSGEILVDGKEVSFASPRDAR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQkptpfpmsiydniafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 170
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-232 |
1.81e-31 |
|
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: 115.39 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNILTNTQDiallR 90
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIKPD--SGEITFDGKSYQKNIEA----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLsrtdmDERVQWALTKAALWNETKDKLhqSGYSLsgGQQQRLCIARGIA 169
Cdd:cd03268 72 RRIGALIEAPGFYPnLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKV--KGFSL--GMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-211 |
1.85e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.90 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 8 PGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELypEQRAEGEILLDGdniltntQDIA 87
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGRIFLDG-------EDIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LL----RAKVGM--------VFQKptpfpMSIYDNIAfGVRLFEKLSRTDMDERVQwaltkaALWNETK-DKL-HQSGYS 153
Cdd:COG1137 69 HLpmhkRARLGIgylpqeasIFRK-----LTVEDNIL-AVLELRKLSKKEREERLE------ELLEEFGiTHLrKSKAYS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHN 211
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHN 195
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
8-185 |
3.97e-31 |
|
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: 121.22 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 8 PGKLS----VRNLNFYYGK--FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNILT 81
Cdd:TIGR03797 445 PGKLSgaieVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDLAG 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 ntQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeklsrtDMDErVQWALTKAALWNETKD---KLH----QSGYSL 154
Cdd:TIGR03797 520 --LDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPL-------TLDE-AWEAARMAGLAEDIRAmpmGMHtvisEGGGTL 589
|
170 180 190
....*....|....*....|....*....|.
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:TIGR03797 590 SGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-242 |
6.75e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.23 E-value: 6.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDgdNILTNTQDIALLRAKVGMVFQKP-TPF 103
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYN--NQAITDDNFEKLRKHIGIVFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 104 PMSI--YDnIAFGVRLFeKLSRTDMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:PRK13648 97 VGSIvkYD-VAFGLENH-AVPYDEMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 182 SALDPISTGRIEELITELKQDYTVVI--VTHNMQQAARcSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-218 |
7.71e-31 |
|
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: 112.69 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHA--LKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltNTQDIAL 88
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLRPT--SGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 168
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARC 218
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASA 162
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-232 |
1.19e-30 |
|
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: 113.68 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 3 MVNATPGKLSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLDGDN 78
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGL---LAGL--DRPTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 79 ILTNTQD-IALLRA-KVGMVFQK----PTpfpMSIYDNIAfgVRLfEKLSRTDMDERVQWALTKAALwnetKDKLHQSGY 152
Cdd:COG4181 76 LFALDEDaRARLRArHVGFVFQSfqllPT---LTALENVM--LPL-ELAGRRDARARARALLERVGL----GHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPiSTG-RIEELITELKQDY--TVVIVTHNMQQAARCsDHTAFMYLGE 229
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDA-ATGeQIIDLLFELNRERgtTLVLVTHDPALAARC-DRVLRLRAGR 223
|
...
gi 490994015 230 LIE 232
Cdd:COG4181 224 LVE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-210 |
1.37e-30 |
|
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: 112.96 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIltnTQDIALLR 90
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRI---LAGLLP--PSAGEVLWNGEPI---RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLF-EKLSRTDMDErvqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:COG4133 75 RRLAYLGHADGLKPeLTVRENLRFWAALYgLRADREAIDE----ALEAVGL----AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-242 |
1.52e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 115.22 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLdGDNILTNT---QDIALLRAKVGMVFQKPT 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-----QPTEGKVTV-GDIVVSSTskqKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 P--FPMSIYDNIAFGVRLFeKLSRtdmDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNF-GIPK---EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 180 PCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-243 |
1.70e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNIltNTQDIALL 89
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKP---TSGSVLIRGEPI--TKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTP--FPMSIYDNIAFG-VRLfeKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGpINL--GLDEETVAHRVSSALHMLGL----EELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-242 |
1.83e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.44 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGK---FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAE-GEILLDGDnILT--NTQDI 86
Cdd:PRK13650 7 VKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE------AEsGQIIIDGD-LLTeeNVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 allRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRLCI 164
Cdd:PRK13650 80 ---RHKIGMVFQNPdNQFvGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGM-QDFKER---EPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPisTGRIE--ELITELKQDY--TVVIVTHNMQQAArCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
..
gi 490994015 241 TK 242
Cdd:PRK13650 229 SR 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-244 |
4.33e-30 |
|
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: 115.20 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 28 NINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLDGDNILTNTQDIALLRAK--VGMVFQKPTPFP- 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRA---IAGL--ERPDSGRIRLGGEVLQDSARGIFLPPHRrrIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 MSIYDNIAFGV-RLFEKLSRTDMDERVQWaLTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:COG4148 92 LSVRGNLLYGRkRAPRAERRISFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 184 LDpisTGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG4148 164 LD---LARKAEILPYLERlrdelDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-247 |
4.40e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 113.36 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY---------GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNI-- 79
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDLyq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 80 LTNTQDIALLRaKVGMVFQK-PTPF--PMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSgysLSG 156
Cdd:TIGR02769 78 LDRKQRRAFRR-DVQLVFQDsPSAVnpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250
....*....|....*
gi 490994015 235 NTDDLFT--KPAKKQ 247
Cdd:TIGR02769 234 DVAQLLSfkHPAGRN 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-231 |
7.78e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 112.39 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILT-NTQ 84
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIQHyASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIAllrAKVGMVFQKP-TPFPMSIYDNIAFGVR----LFEKLSRTDMDervqwALTKAALWNETKDKLHQSGYSLSGGQQ 159
Cdd:PRK10253 78 EVA---RRIGLLAQNAtTPGDITVQELVARGRYphqpLFTRWRKEDEE-----AVTKAMQATGITHLADQSVDTLSGGQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-244 |
1.79e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.02 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG-----KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMF----------ELYPEQRAEGEILLD 75
Cdd:PRK13631 22 LRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 76 GDNiLTNTQDIALLRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLfeKLSRTDMDERVQWALTKAALwneTKDKLHQSGY 152
Cdd:PRK13631 102 NPY-SKKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGpVAL--GVKKSEAKKLAKFYLNKMGL---DDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|...
gi 490994015 232 EFSNTDDLFTKPA 244
Cdd:PRK13631 256 KTGTPYEIFTDQH 268
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-243 |
1.83e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQRAEGEILLDGDNIltNTQDIAL 88
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITL--TAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIAR 166
Cdd:PRK13640 82 IREKVGIVFQNPdNQFvGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPA----NLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-230 |
1.95e-29 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 110.19 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 22 KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNkMFElypeQRAEGEILLDGDNI--LTNTQDIALLRAKVGMVFQK 99
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFD----SLDSGSLTLAGKEVtnLSYSQKIILRRELIGYIFQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 PTPFP-MSIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:NF038007 92 FNLIPhLSIFDNVALPLK-YRGVAKKERIERVNQVLNLFGIDNRRNHKPMQ----LSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 179 EPCSALDPISTGRIEELITEL-KQDYTVVIVTHNmQQAARCSDHTAFMYLGEL 230
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-247 |
2.72e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNILTNTqdIA 87
Cdd:PRK13657 333 GAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--P---QSGRILIDGTDIRTVT--RA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTD-MDERVQWALTKAALWN--ETKDKLHQS-----GYSLSGGQQ 159
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVG--------RPDaTDEEMRAAAERAQAHDfiERKPDGYDTvvgerGRQLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDEL 556
|
250
....*....|....
gi 490994015 240 ------FTKPAKKQ 247
Cdd:PRK13657 557 varggrFAALLRAQ 570
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-231 |
4.22e-29 |
|
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: 109.38 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 21 GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNILTNTQDIallRAKVGMVFQKP 100
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE--PDA---GFATVDGFDVVKEPAEA---RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 TPFP-MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:cd03266 88 GLYDrLTARENLEYFAGLY-GLKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 180 PCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-241 |
4.44e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.25 E-value: 4.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGK-----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDniLTNT 83
Cdd:PRK13645 5 KDIILDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN--LKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLFEklSRTDMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQ 160
Cdd:PRK13645 83 KEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGE--NKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
...
gi 490994015 239 LFT 241
Cdd:PRK13645 238 IFS 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-243 |
7.04e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 7.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKF------HALKNINLDITKNQVTAFIGPSGCGKSTLLRtfnkMFELYpEQRAEGEILLDGDNIL 80
Cdd:PRK11308 6 LQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLAR----LLTMI-ETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 81 TN-TQDIALLRAKVGMVFQKPTPfpmSIYDNIAFGVRLFE------KLSRTDMDERVQWALTKAALWNEtkdklHQSGYS 153
Cdd:PRK11308 81 KAdPEAQKLLRQKIQIVFQNPYG---SLNPRKKVGQILEEpllintSLSAAERREKALAMMAKVGLRPE-----HYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 --LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:PRK11308 153 hmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGR 232
|
250
....*....|....
gi 490994015 230 LIEFSNTDDLFTKP 243
Cdd:PRK11308 233 CVEKGTKEQIFNNP 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-231 |
7.72e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNFYY-----GKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNIlTNTQDIA 87
Cdd:PRK13633 8 KNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDT-SDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfEKLS--RTDMDERVQWALTKAALWNETKDKLHQsgysLS 155
Cdd:PRK13633 82 DIRNKAGMVFQNP--------DNqivativeedVAFGP---ENLGipPEEIRERVDESLKKVGMYEYRRHAPHL----LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPIstGRIEEL--ITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLGELI 231
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPS--GRREVVntIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-220 |
1.18e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.38 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 7 TPgkLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEiLLDGDNILTNTQDi 86
Cdd:PRK11247 11 TP--LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-----ETPSAGE-LLAGTAPLAEARE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 allraKVGMVFQKPTPFP-MSIYDNIAFGVRlfeklsrTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIA 165
Cdd:PRK11247 82 -----DTRLMFQDARLLPwKKVIDNVGLGLK-------GQWRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 166 RGIAIRPEVLLLDEPCSALDPIStgRIE--ELITELKQDY--TVVIVTHNMQQAARCSD 220
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALT--RIEmqDLIESLWQQHgfTVLLVTHDVSEAVAMAD 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-210 |
1.21e-28 |
|
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: 108.35 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltntQDI 86
Cdd:cd03244 1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDI----SKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 AL--LRAKVGMVFQKPTPFPMSIYDNIAFgvrlFEKLSrtdmDERVQWALTKAALWNETK-------DKLHQSGYSLSGG 157
Cdd:cd03244 72 GLhdLRSRISIIPQDPVLFSGTIRSNLDP----FGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI-TELKqDYTVVIVTH 210
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFK-DCTVLTIAH 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.26e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 107.01 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG--KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNILTNTqdiAL 88
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQ---GEITLDGVPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsGYSLSGGQQQRLCIARGI 168
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-225 |
1.43e-28 |
|
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: 107.56 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK-----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELypeQRAEGEILLDGdniltntqd 85
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEL---EKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 iallraKVGMVFQKPTPFPMSIYDNIAFGVRlFEKlsrtdmdERVQWALTKAALwneTKD----------KLHQSGYSLS 155
Cdd:cd03250 67 ------SIAYVSQEPWIQNGTIRENILFGKP-FDE-------ERYEKVIKACAL---EPDleilpdgdltEIGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPiSTGR--IEELIT-ELKQDYTVVIVTHNMQQAARCsDHTAFM 225
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDA-HVGRhiFENCILgLLLNNKTRILVTHQLQLLPHA-DQIVVL 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-243 |
3.01e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.89 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY---GKFHALKNINLDITKNQVTAFIGPSGCGKST---LLRTFnkmfelYpeQRAEGEILLDGDNIltn 82
Cdd:TIGR00958 477 GLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNL------Y--QPTGGQVLLDGVPL--- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 83 TQ-DIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRTDMDERVQWALTKAA------LWNETKDKLHQSGYSLS 155
Cdd:TIGR00958 546 VQyDHHYLHRQVALVGQEPVLFSGSVRENIAYG------LTDTPDEEIMAAAKAANAhdfimeFPNGYDTEVGEKGSQLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDpistGRIEELITELK--QDYTVVIVTHNMQQAARCsDHTAFMYLGELIEF 233
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVERA-DQILVLKKGSVVEM 694
|
250
....*....|
gi 490994015 234 SNTDDLFTKP 243
Cdd:TIGR00958 695 GTHKQLMEDQ 704
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-220 |
3.23e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.66 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNIlTNTQDIALL 89
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT------LCGDPRAtSGRIVFDGKDI-TDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEklsRTDMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAE---RDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSD 220
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLAD 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-231 |
3.32e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNIL-TNTQDIALL 89
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDS---GEVRLNGRPLAdWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAkvgMVFQKPT-PFPMSIYDNIAFGvRLFEKLSRTDMDERVQWALTKAALWnETKDKLHQsgySLSGGQQQRLCIARGI 168
Cdd:PRK13548 78 RA---VLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYP---QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 169 A------IRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-211 |
3.38e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 112.07 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNILTNTQDiaLL 89
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT---LAGLLDPLQ--GEVTLDGVPVSSLDQD--EV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTDM-DERVQWALTKAALWN---ETKD----KLHQSGYSLSGGQQQR 161
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLRLA--------RPDAtDEELWAALERVGLADwlrALPDgldtVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHN 211
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-244 |
3.48e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNL-NFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRtfnkMFE-LypEQRAEGEILLDGDNIltNT---- 83
Cdd:PRK11650 3 GLKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR----MVAgL--ERITSGEIWIGGRVV--NElepa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 -QDIAllrakvgMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQwaltKAALWNETKDKLHQSGYSLSGGQQQR 161
Cdd:PRK11650 75 dRDIA-------MVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIEERVA----EAARILELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDP---ISTgRIE--ELITELKQdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAklrVQM-RLEiqRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*...
gi 490994015 237 DDLFTKPA 244
Cdd:PRK11650 220 VEVYEKPA 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-244 |
4.50e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 109.82 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKnINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNTQDIALL--RAKVGMVFQKPT 101
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGRTLFDSRKGIFLPpeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 PFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 181 CSALDPISTGRI----EELITELkqDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:TIGR02142 159 LAALDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-239 |
4.83e-28 |
|
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: 112.14 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYG-KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNIltNTQDIA 87
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF-----QARSGEILLNGFSL--KDIDRH 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRTDMDERVQWALTKAALWNET---KDKLHQSGYSLSGGQQQRLCI 164
Cdd:TIGR01193 545 TLRQFINYLPQEPYIFSGSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIENMPlgyQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELkQDYTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDL 239
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-215 |
5.33e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 107.48 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGdniltntQDIALLR 90
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVPYQ--HGSITLDG-------KPVEGPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:PRK11248 70 AERGVVFQNEGLLPwRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQA 215
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-225 |
9.83e-28 |
|
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: 105.65 E-value: 9.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 18 FYYGkfHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmFELypeqRAEGEILLDGdniltntQDIALL---RAKVG 94
Cdd:cd03298 8 FSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAG-FET----PQSGRVLING-------VDVTAAppaDRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 95 MVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMdERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPE 173
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGLKLTAEDR-QAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 174 VLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-221 |
1.27e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNI-LTNTQDiAlL 89
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKI---LSGVY--QPDSGEILLDGEPVrFRSPRD-A-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGvrlFEKLSRTDMDERVQWALTKAALwnetkDKLHQS-------GySLSGGQQQR 161
Cdd:COG1129 78 AAGIAIIHQELNLVPnLSVAENIFLG---REPRRGGLIDWRAMRRRARELL-----ARLGLDidpdtpvG-DLSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDH 221
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADR 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-233 |
1.35e-27 |
|
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: 105.19 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGKF--HALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltNTQDI 86
Cdd:cd03369 5 GEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDI--STIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFPMSIYDNiafgVRLFEKLSrtdmDERVQWALtkaalwnetkdKLHQSGYSLSGGQQQRLCIAR 166
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSN----LDPFDEYS----DEEIYGAL-----------RVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEF 233
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-231 |
1.54e-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: 105.06 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNT-QDIALL 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGKPLDIAArNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMvFQKptpfpMSIYDNIAFGVRLfEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:cd03269 76 PEERGL-YPK-----MKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-243 |
1.85e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.33 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILT-NTQDIALLRAKVGMVFQKP-- 100
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPya 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 --TPfPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNEtkdklHQSGY--SLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:PRK10261 413 slDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPE-----HAWRYphEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 177 LDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-242 |
1.85e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNIltNT 83
Cdd:PRK11160 334 ADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQ---GEILLNGQPI--AD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklSRTDMDERVQWALTKAALWNETKDK------LHQSGYSLSGG 157
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDkglnawLGEGGRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTD 237
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQ 558
|
....*
gi 490994015 238 DLFTK 242
Cdd:PRK11160 559 ELLAQ 563
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-245 |
6.92e-27 |
|
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: 103.63 E-value: 6.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNIltNTQDIAllr 90
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-----RPTSGEIIFDGHPW--TRKDLH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 aKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSrtdmDERVQWALTKAALWNETKDKLHQsgYSLsgGQQQRLCIARGIA 169
Cdd:TIGR03740 71 -KIGSLIESPPLYEnLTARENLKV-HTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQ--FSL--GMKQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI------EFSNTDDLFTK 242
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLGyqgkinKSENLEKLFVE 220
|
...
gi 490994015 243 PAK 245
Cdd:TIGR03740 221 VVK 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-242 |
1.23e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.32 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNTQDIALLR 90
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQK---GAVLWQGKPLDYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK13638 77 QQVATVFQDPEQqiFYTDIDSDIAFSLRNL-GVPEAEITRRVDEALTLV----DAQHFRHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-249 |
1.95e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.63 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDN---ILTNT 83
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLR----AKVGMVFQKPTP-----FPMSiyDNIAFGVRLFEKLSRTDMDERVQWALTKAALwNETKDKLHQSGYSL 154
Cdd:PRK10261 93 QSAAQMRhvrgADMAMIFQEPMTslnpvFTVG--EQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250
....*....|....*..
gi 490994015 233 FSNTDDLFTKPAKKQTE 249
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTR 266
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-241 |
2.96e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.47 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQRAEGEILldgDNILTNTqDIALLR 90
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTYGNDVRLF---GERRGGE-DVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMV---FQKPTPFPMSIYDNI---AFG-VRLFEKLSRTDMDERVQWAltkaALWnETKDKLHQSGYSLSGGQQQRLC 163
Cdd:COG1119 78 KRIGLVspaLQLRFPRDETVLDVVlsgFFDsIGLYREPTDEQRERARELL----ELL-GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLT 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-220 |
3.21e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.10 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 3 MVNATPgKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTN 82
Cdd:PRK10247 1 MQENSP-LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PT---SGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 83 TQDIalLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKlsRTDMDeRVQWALTKAALWNETkdkLHQSGYSLSGGQQQRL 162
Cdd:PRK10247 75 KPEI--YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQ--QPDPA-IFLDDLERFALPDTI---LTKNIAELSGGEKQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVI--VTHNMQQAARCSD 220
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADK 206
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-221 |
7.26e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.61 E-value: 7.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLlrtFNKMFELYpeQRAEGEILLDGDNI--LTNtQDIAl 88
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLTGFY--KPTGGTILLRGQHIegLPG-HQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lraKVGMV--FQKPTPF-PMSIYDNI------AFGVRLFEKLSRTDMDERVQW-ALTKAALWNET---KDKLHQSGYSLS 155
Cdd:PRK11300 79 ---RMGVVrtFQHVRLFrEMTVIENLlvaqhqQLKTGLFSGLLKTPAFRRAESeALDRAATWLERvglLEHANRQAGNLA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDH 221
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
1.79e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLN--FYYG---KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlTNTQD 85
Cdd:COG1101 2 LELKNLSktFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP-----DSGSILIDGKDV-TKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IAllRAK-VGMVFQKP---TPFPMSIYDNIA------------FGVR-----LF-EKLSRTDMD-Ervqwaltkaalwne 142
Cdd:COG1101 76 YK--RAKyIGRVFQDPmmgTAPSMTIEENLAlayrrgkrrglrRGLTkkrreLFrELLATLGLGlE-------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 143 tkDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSD 220
Cdd:COG1101 140 --NRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGN 217
|
250
....*....|.
gi 490994015 221 HTAFMYLGELI 231
Cdd:COG1101 218 RLIMMHEGRII 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-238 |
2.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.32 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGK-----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQrAEGEILLDGDNILTNTQ 84
Cdd:PRK13651 2 QIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPDT-GTIEWIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIAL--------------------LRAKVGMVFQ--KPTPFPMSIYDNIAFGVRLFEklsrTDMDERVQWALTKAALWNE 142
Cdd:PRK13651 79 EKEKvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG----VSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 143 TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|....*..
gi 490994015 222 TAFMYLGELIEFSNTDD 238
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYD 251
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-243 |
3.93e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.80 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDNILT-NTQDIALL 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTP---SSGEVRLNGRPLAAwSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAkvgmVFQKPTP--FPMSIYDNIAFGvRLFEKLSRTDMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIAR- 166
Cdd:COG4559 77 RA----VLPQHSSlaFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLA----HLAGRSYQTLSGGEQQRVQLARv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 ------GIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG4559 148 laqlwePVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
....
gi 490994015 240 FTKP 243
Cdd:COG4559 228 LTDE 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-210 |
7.44e-25 |
|
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: 102.98 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYYGKFHA-LKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNILTNTQ 84
Cdd:COG5265 353 VGGGEVRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARL---LFRFYDVT--SGRILIDGQDIRDVTQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 diALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTDMDERVQWALTKAAlwnetkdKLHQ------SGYS----- 153
Cdd:COG5265 428 --ASLRAAIGIVPQDTVLFNDTIAYNIAYG--------RPDASEEEVEAAARAA-------QIHDfieslpDGYDtrvge 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 154 ----LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG5265 491 rglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-236 |
2.12e-24 |
|
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: 96.85 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 30 NLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTntqdIALLRAKVGMVFQKPTPFP-MSIY 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSHTG----LAPYQRPVSMLFQENNLFAhLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 109 DNIAFGVRLFEKLSRTDMDERVQwaltkAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIS 188
Cdd:TIGR01277 89 QNIGLGLHPGLKLNAEQQEKVVD-----AAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490994015 189 TGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:TIGR01277 164 REEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-247 |
2.27e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.22 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY------GKFHA---LKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNILT 81
Cdd:PRK10419 4 LNVSGLSHHYahgglsGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLL-----VGLESPSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 -NTQDIALLRAKVGMVFQKP----TPfPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSgysLSG 156
Cdd:PRK10419 79 lNRAQRKAFRRDIQMVFQDSisavNP-RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
250
....*....|....*
gi 490994015 235 NTDDL--FTKPAKKQ 247
Cdd:PRK10419 235 PVGDKltFSSPAGRV 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
11-218 |
4.28e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYG----KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NTQD 85
Cdd:PRK10584 7 VEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-----DDGSSGEVSLVGQPLHQmDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAK-VGMVFQK----PTpfpMSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQ 160
Cdd:PRK10584 82 RAKLRAKhVGFVFQSfmliPT---LNALENVELPA-LLRGESSRQSRNGAKALLEQLGL----GKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARC 218
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARC 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-223 |
4.69e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 20 YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPeqrAEGEILLDGDniltntqdiallrAKVGMVF 97
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLL----KVLAgvLRP---TSGTVRRAGG-------------ARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 98 QK---PTPFPMSIYDNIAFGV----RLFEKLSRTDmDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGRwarrGLWRRLTRDD-RAAVDDALERVGL----ADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490994015 171 RPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARcSDHTA 223
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRR-ADPCV 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-243 |
5.34e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNIL-TNTQDIA--- 87
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL---SMISRLLPPD--SGEVLVDGLDVAtTPSRELAkrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 -LLRakvgmvfQKPTpFPM--SIYDNIAFGV------RLfeklsrTDMDER-VQWALTKAALwNETKDK-LHQsgysLSG 156
Cdd:COG4604 78 aILR-------QENH-INSrlTVRELVAFGRfpyskgRL------TAEDREiIDEAIAYLDL-EDLADRyLDE----LSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
....*....
gi 490994015 235 NTDDLFTKP 243
Cdd:COG4604 219 TPEEIITPE 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-237 |
5.40e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.87 E-value: 5.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 5 NATPGKLSVRNLNFYY---GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFEL--------YPEQRAE---- 69
Cdd:PTZ00265 1160 NDIKGKIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfKNEHTNDmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 70 -------------------------------------GEILLDGDNILT-NTQDialLRAKVGMVFQKPTPFPMSIYDNI 111
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDyNLKD---LRNLFSIVSQEPMLFNMSIYENI 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 112 AFGVrlfEKLSRTDMDERVQWALTKA---ALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIS 188
Cdd:PTZ00265 1317 KFGK---EDATREDVKRACKFAAIDEfieSLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490994015 189 TGRIEELITELKQ--DYTVVIVTHNMQQAARcSDhtafmylgELIEFSNTD 237
Cdd:PTZ00265 1394 EKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SD--------KIVVFNNPD 1435
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-243 |
9.27e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.47 E-value: 9.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIL-TNTQDIALLRAKVGMVFQKP--- 100
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGEVAWLGKDLLgMKDDEWRAVRSDIQMIFQDPlas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 -TPfPMSIYDNIAFGVRLFE-KLSRTDMDERVQWALTKAALW-NETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:PRK15079 111 lNP-RMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLpNLINRYPHE----FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 178 DEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-231 |
9.99e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 9.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMfeLYPEQRA-EGEILLDGDNI-LTNTQDiAl 88
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLM----KI--LYGLYQPdSGEILIDGKPVrIRSPRD-A- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsrtdMDERVQWALTKAALWNETKDKLHQSG---------YSLSGGQ 158
Cdd:COG3845 78 IALGIGMVHQHFMLVPnLTVAENIVLG-----------LEPTKGGRLDRKAARARIRELSERYGldvdpdakvEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPistGRIEELITELK----QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-217 |
1.18e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.33 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNtQDIALLRAKVGMV 96
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDItrLKN-REVPFLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 97 FQKP-TPFPMSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVL 175
Cdd:PRK10908 85 FQDHhLLMDRTVYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490994015 176 LLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAAR 217
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-238 |
2.88e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 98.28 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNILTNTQDi 86
Cdd:COG4618 329 GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPPTA--GSVRLDGADLSQWDRE- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 aLLRAKVGMVFQKPTPFPMSIYDNIAfgvRLfeklsrTDMD-ERVQWALTKAALwNETKDKLHQ--------SGYSLSGG 157
Cdd:COG4618 403 -ELGRHIGYLPQDVELFDGTIAENIA---RF------GDADpEKVVAAAKLAGV-HEMILRLPDgydtrigeGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNT 236
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPR 550
|
..
gi 490994015 237 DD 238
Cdd:COG4618 551 DE 552
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-210 |
2.90e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 98.25 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNILTNTQdiA 87
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLA---SLLMGYYPLT--EGEIRLDGRPLSSLSH--S 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsrTDMDERVQW-ALTK---AALWNETKDKLH----QSGYSLSGGQQ 159
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLADTFLANVTLG---------RDISEEQVWqALETvqlAELARSLPDGLYtplgEQGNNLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-240 |
3.44e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.19 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELYPeqRAEGEILLDGDniltntqDIALL- 89
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDE-------DISLLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 -----RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVqwaltkaalwNETKDKLHQS------GYSLSGG 157
Cdd:PRK10895 72 lharaRRGIGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRA----------NELMEEFHIEhlrdsmGQSLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKqDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSN 235
Cdd:PRK10895 142 ERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
....*
gi 490994015 236 TDDLF 240
Cdd:PRK10895 221 PTEIL 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-244 |
6.62e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.18 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTllRTFNKMFELYPEQRAEGEILLDGDNILT-NTQD 85
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQ--TAFALMGLLAANGRIGGSATFNGREILNlPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRA-KVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRTD-MDERVQwaLTKAALWNETKDKLHQSGYSLSGGQQ 159
Cdd:PRK09473 91 LNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKAEaFEESVR--MLDAVKMPEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTD 237
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
....*..
gi 490994015 238 DLFTKPA 244
Cdd:PRK09473 248 DVFYQPS 254
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-257 |
1.06e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.70 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLN--FYY--GKFH-----ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNIlt 81
Cdd:PRK15112 5 LEVRNLSktFRYrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE--P---TSGELLIDDHPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NTQDIALLRAKVGMVFQKPT----PfPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWNEtkdklHQSGYS--LS 155
Cdd:PRK15112 78 HFGDYSYRSQRIRMIFQDPStslnP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD-----HASYYPhmLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|....
gi 490994015 234 SNTDDLFTKPAKKQTEDYITGRYG 257
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAGHFG 255
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-232 |
1.56e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.07 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraeGEILLDGdnILTNTQDIALLRAKVGMVFQKPTPFPM 105
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPYQ---GSLKING--IELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNIAFGvrlfeklsRTDM-DERVQWALTKAALWNETKDKLH--------QSGySLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:PRK11174 438 TLRDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLPQgldtpigdQAA-GLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 177 LDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-248 |
1.63e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.84 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 7 TPGKLSVRNLNFYYGKfHALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELYPE--QRAEGEILLDGDNILTNTq 84
Cdd:PRK10418 1 MPQQIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSL---TCAAALGILPAgvRQTAGRVLLDGKPVAPCA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 dialLRAK-VGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAALWN-ETKDKLHQsgYSLSGGQQQRL 162
Cdd:PRK10418 76 ----LRGRkIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENaARVLKLYP--FEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
....*...
gi 490994015 241 TKPAKKQT 248
Cdd:PRK10418 230 NAPKHAVT 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-238 |
2.43e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGdniltntqDIA-LLRakVGMVF 97
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LEPT---SGRVEVNG--------RVSaLLE--LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 98 QkptpfP-MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:COG1134 100 H-----PeLTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL----GDFIDQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490994015 177 LDEpcsALdpiSTG----------RIEELITELKqdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:COG1134 170 VDE---VL---AVGdaafqkkclaRIRELRESGR---TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-217 |
3.16e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 92.38 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQRAEGEILLDGDNILTN---TQDIA 87
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREgrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFG-----------VRLFEKLSRtdmdERVQWALTKAALWNETkdklHQSGYSLS 155
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNrLSVLENVLIGalgstpfwrtcFSWFTREQK----QRALQALTRVGMVHFA----HQRVSTLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAAR 217
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-243 |
7.79e-22 |
|
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: 91.05 E-value: 7.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQRAEGEILLDGDNI----LTNTQDI 86
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG--RLAPDHGTATYIMRSGAELelyqLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRTDMD--ERVQWALTKaalwneTKDKLHQsgysLSG 156
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDglrMRVSAGANIgerlmAIGARHYGNIRATAQDwlEEVEIDPTR------IDDLPRA----FSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
....*....
gi 490994015 235 NTDDLFTKP 243
Cdd:TIGR02323 232 LTDQVLDDP 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-246 |
1.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGdnilTNTQDIALL---RAKVGMVFQKP- 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQK---GKVLVSG----IDTGDFSKLqgiRKLVGIVFQNPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 TPF-PMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13644 88 TQFvGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGL----EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 180 PCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQaARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-248 |
1.28e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKST----LLRTFnkmfelypeqRAEGEILLDGDNI-LTNTQDIALLRAKVGMVFQ 98
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI----------NSQGEIWFDGQPLhNLNRRQLLPVRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KP----TPfPMSIYDNIAFGVRLFEK-LSRTDMDERVQWALTKAALWNETKdklHQSGYSLSGGQQQRLCIARGIAIRPE 173
Cdd:PRK15134 370 DPnsslNP-RLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPETR---HRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 174 VLLLDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQT 248
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-237 |
1.41e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.37 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDG-DNILTNTQDIA-- 87
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDA---GEVHYRMrDGQLRDLYALSea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 ----LLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRTDMD--ERVQWALtkaalwnetkDKLHQSGYS 153
Cdd:PRK11701 82 errrLLRTEWGFVHQHPRDglrMQVSAGGNIgerlmAVGARHYGDIRATAGDwlERVEIDA----------ARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
....*.
gi 490994015 232 EFSNTD 237
Cdd:PRK11701 232 ESGLTD 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-217 |
1.69e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.64 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 30 NLDITKNQVTAFIGPSGCGKSTLLrtfNKM--FeLYPEQraeGEILLDGDNiLTNTqdiALLRAKVGMVFQKPTPFP-MS 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL---NLIagF-LTPAS---GSLTLNGQD-HTTT---PPSRRPVSMLFQENNLFShLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 107 IYDNIAFGVRLFEKLSRTDMDERVQWAlTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDP 186
Cdd:PRK10771 88 VAQNIGLGLNPGLKLNAAQREKLHAIA-RQMGI----EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190
....*....|....*....|....*....|...
gi 490994015 187 ISTGRIEELITEL--KQDYTVVIVTHNMQQAAR 217
Cdd:PRK10771 163 ALRQEMLTLVSQVcqERQLTLLMVSHSLEDAAR 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-211 |
2.99e-21 |
|
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: 87.97 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkM-FELYPEqrAEGEILLDGDNILT-NTQDIAl 88
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MgHPKYEV--TEGEILFKGEDITDlPPEERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lRAKVGMVFQKPTPFPmsiydniafGVRLfeklsrtdmdervqwaltkaalwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:cd03217 76 -RLGIFLAFQYPPEIP---------GVKN--------------------------ADFLRYVNEGFSGGEKKRNEILQLL 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHN 211
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-243 |
4.71e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.19 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGK----FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElYPEQRAEGEILLDGDNI--LTNTQ 84
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLqrISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPTpfpMSIYDNIAFGVRLFEKLsrtdmdeRVQWALTKAALWNETKDKLHQSG------------Y 152
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPM---TSLNPCYTVGFQIMEAI-------KVHQGGNKKTRRQRAIDLLNQVGipdpasrldvypH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
250
....*....|...
gi 490994015 231 IEFSNTDDLFTKP 243
Cdd:PRK11022 233 VETGKAHDIFRAP 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-210 |
5.74e-21 |
|
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: 87.22 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 8 PGKLSVRNLNFY------YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGDNIlt 81
Cdd:cd03213 1 GVTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVLINGRPL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 ntqDIALLRAKVGMVFQkptpfpmsiyDNIafgvrLFEKLSrtdmderVQWALTKAAlwnetkdKLHqsgySLSGGQQQR 161
Cdd:cd03213 76 ---DKRSFRKIIGYVPQ----------DDI-----LHPTLT-------VRETLMFAA-------KLR----GLSGGERKR 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTH 210
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-217 |
1.03e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNkmfelYPEQRAEGEILLDGDNILT-NTQDIALLRAK-VGMVFQKPTPF 103
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILG-----CLDKPTSGTYRVAGQDVATlDADALAQLRREhFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 104 P-MSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK10535 99 ShLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 490994015 183 ALDPISTgriEELITELKQ----DYTVVIVTHNMQQAAR 217
Cdd:PRK10535 174 ALDSHSG---EEVMAILHQlrdrGHTVIIVTHDPQVAAQ 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-212 |
5.95e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGK---FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNiltNTQDI 86
Cdd:PTZ00265 382 KIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINDSH---NLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 AL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKL-------------SRTDMDERVQWALTKAALWNE-----TKDK 146
Cdd:PTZ00265 454 NLkwWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLealsnyynedgndSQENKNKRNSCRAKCAGDLNDmsnttDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 147 LHQ---------------------------------------SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPI 187
Cdd:PTZ00265 534 LIEmrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260
....*....|....*....|....*..
gi 490994015 188 STGRIEELITELK--QDYTVVIVTHNM 212
Cdd:PTZ00265 614 SEYLVQKTINNLKgnENRITIIIAHRL 640
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-249 |
6.02e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 6.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 28 NINLDITKNQVTAFIGPSGCGKS----TLLRTFNKMFELYPEqraeGEILLDGDNIL-TNTQDIALLRA-KVGMVFQKPT 101
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPS----GDIRFHGESLLhASEQTLRGVRGnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 pfpMSIYDNIAFGVRLFEKLS----------RTDMD---ERVqwALTKAAlwNETKDKLHQsgysLSGGQQQRLCIARGI 168
Cdd:PRK15134 103 ---VSLNPLHTLEKQLYEVLSlhrgmrreaaRGEILnclDRV--GIRQAA--KRLTDYPHQ----LSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
...
gi 490994015 247 QTE 249
Cdd:PRK15134 252 YTQ 254
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-213 |
7.19e-20 |
|
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: 85.08 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLL-RTFNKMfelypeQRAEGEILLDGDNILTNTQDIALLRAK--VGMVFQKPTP 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEM------QTLEGKVHWSNKNESEPSFEATRSRNRysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 FPMSIYDNIAFGVRLFEKLSRTDMDE-RVQWALTKAALWNETKdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 490994015 182 SALD-PISTGRIEELITELKQD--YTVVIVTHNMQ 213
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-225 |
1.35e-19 |
|
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: 84.41 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 22 KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNILTN-----TQDIALLRAK-VG 94
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKC------IYGNYLPdSGSILVRHDGGWVDlaqasPREILALRRRtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 95 MVFQkptpF----P-MSIYDNIAfgvrlfEKLSRTDMDERVqwALTKAA-----------LWnetkdklHQSGYSLSGGQ 158
Cdd:COG4778 97 YVSQ----FlrviPrVSALDVVA------EPLLERGVDREE--ARARARellarlnlperLW-------DLPPATFSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVI-VTHNMQQAARCSDHTAFM 225
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVADRVVDV 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-233 |
3.09e-19 |
|
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: 83.35 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 20 YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGdniltntQDIALLRAKVGMVFQk 99
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPD---SGTVTVRG-------RVSSLLGLGGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 ptpfpMSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:cd03220 99 -----LTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSEL----GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 180 PCSALDPI----STGRIEELItelKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03220 169 VLAVGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
11-211 |
3.56e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.58 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkM-FELYpeQRAEGEILLDGDNILT-NTQDIAl 88
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MgHPKY--EVTSGSILLDGEDILElSPDERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lRAKVGMVFQKPTPFP-MSIYD--NIAFGVRLFEKLSRTDMDERVQwalTKAALWNETKDKLHQS-GYSLSGGQQQRLCI 164
Cdd:COG0396 76 -RAGIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFLKLLK---EKMKELGLDEDFLDRYvNEGFSGGEKKRNEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490994015 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHN 211
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHY 199
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
9-242 |
5.51e-19 |
|
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: 85.86 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEqrAEGEILLDGDNIltNTQDI 86
Cdd:TIGR01842 315 GHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL---IVGIWPP--TSGSVRLDGADL--KQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFPMSIYDNIAfgvRLFEKLsrtDMDERVQWAltKAALWNETKDKLHQsGY---------SLSGG 157
Cdd:TIGR01842 388 ETFGKHIGYLPQDVELFPGTVAENIA---RFGENA---DPEKIIEAA--KLAGVHELILRLPD-GYdtvigpggaTLSGG 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNT 236
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRP-SLLGCVDKILVLQDGRIARFGER 537
|
....*.
gi 490994015 237 DDLFTK 242
Cdd:TIGR01842 538 DEVLAK 543
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-220 |
5.57e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDniltntqDIALLR 90
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTP---TAGTVLVAGD-------DVEALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFPMSIYDNiaFGVRLFEKLSRT-------DMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK09536 72 ARAASRRVASVPQDTSLSFE--FDVRQVVEMGRTphrsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSD 220
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCD 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-241 |
1.68e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPeqrAEGEILLDGDNILT-NTQDIALLRAKVGMvfQKPTPFP 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLP---GQGEILLNGRPLSDwSAAELARHRAYLSQ--QQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 MSIYDNIAFGVrlfEKLSRTDMDERVQWALTkAALwnETKDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLL 177
Cdd:COG4138 84 MPVFQYLALHQ---PAGASSEAVEQLLAQLA-EAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 178 DEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-230 |
2.10e-18 |
|
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: 80.17 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYygkfHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNILTNTQDIALlR 90
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEA---LFGLRP--PASGEITLDGKPVTRRSPRDAI-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVfqkptP--------FP-MSIYDNIAFGVRLfeklsrtdmdervqwaltkaalwnetkdklhqsgyslSGGQQQR 161
Cdd:cd03215 75 AGIAYV-----PedrkreglVLdLSVAENIALSSLL-------------------------------------SGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-231 |
2.16e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdNILTNTQDIALLRA 91
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDA-QPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 92 KVGMVFQKPTPFPMSIYDNIAFGVRLFE----KLSRTDMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGRYPWHgalgRFGAADR-EKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAML 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
11-211 |
3.35e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTNT--QDIAL 88
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKLDGGDIDDPDvaEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMvfqKPTpfpMSIYDNIAFGVRLfeklsRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK13539 78 LGHRNAM---KPA---LTVAENLEFWAAF-----LGGEELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTHN 211
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-210 |
4.05e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.22 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 4 VNATPGKLSVRNLNFYYGKFH--ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlt 81
Cdd:PRK10789 307 VPEGRGELDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPL-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 ntQDIAL--LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRTD-MDERVQWAltkAALWNETKDKLH---------- 148
Cdd:PRK10789 380 --TKLQLdsWRSRLAVVSQTPFLFSDTVANNIALG--------RPDaTQQEIEHV---ARLASVHDDILRlpqgydtevg 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 149 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpistGRIE-ELITELKQ---DYTVVIVTH 210
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD----GRTEhQILHNLRQwgeGRTVIISAH 508
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-218 |
5.03e-18 |
|
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: 81.05 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGDNilTNTQDI 86
Cdd:cd03289 1 GQMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGDIQIDGVS--WNSVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRTDMDERVQWalTKAALWNETKD----------------KLHQS 150
Cdd:cd03289 73 QKWRKAFGVIPQK---------------VFIFSGTFRKNLDPYGKW--SDEEIWKVAEEvglksvieqfpgqldfVLVDG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARC 218
Cdd:cd03289 136 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLEC 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-230 |
5.05e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.52 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTllrTFNKMFELYPEqrAEGEILLDGDNILTNtqdIALLRAKVGMVFQKPTPFP 104
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPP--TSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 -MSIYDNIAFgvrlFEKLSRTDMDERvqwALTKAALWNET--KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:TIGR01257 1017 hLTVAEHILF----YAQLKGRSWEEA---QLEMEAMLEDTglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490994015 182 SALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-221 |
1.34e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNTQdiaLLR 90
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDA---GSISLCGEPVPSRAR---HAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:PRK13537 80 QRVGVVPQFDNLDPdFTVRENLLVFGRYF-GLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 170 IRPEVLLLDEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-239 |
1.53e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 81.92 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNIltntQDI 86
Cdd:TIGR00957 1283 GRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI----AKI 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 AL--LRAKVGMVFQKPTPFPMSIYDNIafgvRLFEKLSrtdmDERVQWALTKAALW---NETKDKL-HQ---SGYSLSGG 157
Cdd:TIGR00957 1354 GLhdLRFKITIIPQDPVLFSGSLRMNL----DPFSQYS----DEEVWWALELAHLKtfvSALPDKLdHEcaeGGENLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAArcsDHTAFMYL--GELIEFSN 235
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM---DYTRVIVLdkGEVAEFGA 1502
|
....
gi 490994015 236 TDDL 239
Cdd:TIGR00957 1503 PSNL 1506
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-210 |
1.66e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYYGKFHAL-KNINLDITKNQVTAFIGPSGCGKSTLLRTFNkmfELYPeqRAEGEILL-DGDNILtnt 83
Cdd:COG4178 358 SEDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWP--YGSGRIARpAGARVL--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 qdiallrakvgmvF--QKPtpfpmsiYdnIAFGvRLFEKLSRTDM-----DERVQWALTKAALwNETKDKLHQS---GYS 153
Cdd:COG4178 430 -------------FlpQRP-------Y--LPLG-TLREALLYPATaeafsDAELREALEAVGL-GHLAERLDEEadwDQV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-219 |
2.14e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY--GKFHA--LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGD--NILTNTQ 84
Cdd:PRK11629 6 LQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQpmSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVrLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPdFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL----EHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCS 219
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-239 |
2.35e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFE-LYPEqrAEGEILLDGDNIltNTQDIALlRAK 92
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTM----KMLTgLLPA--SEGEAWLFGQPV--DAGDIAT-RRR 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVFQKptpFpmSIY------DNIAFGVRLFEkLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:NF033858 341 VGYMSQA---F--SLYgeltvrQNLELHARLFH-LPAAEIAARVAEMLERFDL----ADVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCsDHTAFMYLG---------ELIEFSN 235
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHAGrvlasdtpaALVAARG 489
|
....
gi 490994015 236 TDDL 239
Cdd:NF033858 490 AATL 493
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-218 |
2.46e-17 |
|
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: 81.11 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYY--GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGdnILTNTQDI 86
Cdd:TIGR01271 1216 GQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS------TEGEIQIDG--VSWNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRTDMDERVQWalTKAALWNETK------------DKLH----QS 150
Cdd:TIGR01271 1288 QTWRKAFGVIPQK---------------VFIFSGTFRKNLDPYEQW--SDEEIWKVAEevglksvieqfpDKLDfvlvDG 1350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARC 218
Cdd:TIGR01271 1351 GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-231 |
3.70e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.76 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPEQraeGEILLDGdnILTNTQDIALLRaKVGMVF-QKPT 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTL----KILSglLQPTS---GEVRVAG--LVPWKRRKKFLR-RIGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 pfpmSIYD-NIAFGVRLFEKLSRTDmDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:cd03267 106 ----LWWDlPVIDSFYLLAAIYDLP-PARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 181 CSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-231 |
4.38e-17 |
|
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: 77.70 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPeqRAEGEILLDGDNIltntqDIALLRAKVGMVFQKPTPFP- 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--TTSGQILFNGQPR-----KPDQFQKCVAYVRQDDILLPg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 MSIYDNIAFGV--RLFEKLS---RTDMDERV---QWALTKAAlwnetkdklHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:cd03234 96 LTVRETLTYTAilRLPRKSSdaiRKKRVEDVllrDLALTRIG---------GNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 177 LDEPCSALDPISTGRIEELITELKQDYTVVIVT-HnmQQAA---RCSDHTAFMYLGELI 231
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiH--QPRSdlfRLFDRILLLSSGEIV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-210 |
3.43e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEqraEGEILLDGDniltntqdiallrAK 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--ELEPD---SGEVSIPKG-------------LR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVFQKPTPFP-MSIYDNIAFGV-----------RLFEKLSRTDMD----ERVQWALTKAALWN-ETK----------- 144
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGDaelraleaeleELEAKLAEPDEDlerlAELQEEFEALGGWEaEARaeeilsglgfp 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 145 -DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgrIEELITELKQ-DYTVVIVTH 210
Cdd:COG0488 143 eEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWLEEFLKNyPGTVLVVSH 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-210 |
5.52e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 22 KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRtfnKMFELYPEQRAEGEILLDGDNILTNTqdiallrakvgmvfqkpt 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR---LLAGALKGTPVAGCVDVPDNQFGREA------------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 pfpmSIYDNIAfgvrlfeklSRTDMDERVQwaltkaalwnetkdKLHQSGYS-----------LSGGQQQRLCIARGIAI 170
Cdd:COG2401 101 ----SLIDAIG---------RKGDFKDAVE--------------LLNAVGLSdavlwlrrfkeLSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490994015 171 RPEVLLLDEPCSALDPISTGR----IEELITELKQdyTVVIVTH 210
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRvarnLQKLARRAGI--TLVVATH 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-210 |
5.65e-16 |
|
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: 72.48 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGdniltntqdiallR 90
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD-----EGIVTWGS-------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQkptpfpmsiydniafgvrlfeklsrtdmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 170
Cdd:cd03221 63 VKIGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490994015 171 RPEVLLLDEPCSALDPIStgrIEELITELKQDY-TVVIVTH 210
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALKEYPgTVILVSH 125
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-239 |
6.68e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY-----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEI-LLDGDNILTNTQ 84
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE--P---TSGEVnVRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALLRAKV----GMVFQKPTPFP-MSIYDNI--AFGVRLFEKLSRTdmdeRVQWALtKAALWNETKDK--LHQSGYSLS 155
Cdd:TIGR03269 355 PGPDGRGRAkryiGILHQEYDLYPhRTVLDNLteAIGLELPDELARM----KAVITL-KMVGFDEEKAEeiLDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI----TELKQdyTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQ--TFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
....*...
gi 490994015 232 EFSNTDDL 239
Cdd:TIGR03269 508 KIGDPEEI 515
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-237 |
8.59e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 5 NATPGK--LSVRNLNfyygKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNI-LT 81
Cdd:COG1129 249 AAAPGEvvLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA---LFGADP--ADSGEIRLDGKPVrIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NTQD-----IALL---RAKVGMVFqkptpfPMSIYDNIAFGVrlFEKLSRTD-MDERVQWALTKAALwnetkDKL----- 147
Cdd:COG1129 320 SPRDairagIAYVpedRKGEGLVL------DLSIRENITLAS--LDRLSRGGlLDRRRERALAEEYI-----KRLriktp 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 148 --HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPcsaldpisTgR---------IEELITEL-KQDYTVVIVTHNMQQA 215
Cdd:COG1129 387 spEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP--------T-RgidvgakaeIYRLIRELaAEGKAVIVISSELPEL 457
|
250 260
....*....|....*....|...
gi 490994015 216 ARCSDHTAFMYLGELI-EFSNTD 237
Cdd:COG1129 458 LGLSDRILVMREGRIVgELDREE 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-252 |
1.34e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGDNIL-TNTQDIAll 89
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG---VYPHGTWDGEIYWSGSPLKaSNIRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWAltkAALWNETK---DKLHQSGYSLSGGQQQRLCIA 165
Cdd:TIGR02633 77 RAGIVIIHQELTLVPeLSVAENIFLGNEITLPGGRMAYNAMYLRA---KNLLRELQldaDNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfTKPA 244
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVA--------TKDM 225
|
....*...
gi 490994015 245 KKQTEDYI 252
Cdd:TIGR02633 226 STMSEDDI 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-239 |
1.78e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 12 SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnkmfELYPEQRA--EGEI-LLDGDniLTNTQDIAL 88
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVeVLGGD--MADARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQ---K---PTpfpMSIYDNIAFGVRLFeKLSRTDMDERVQwALTKAalwnetkdklhqSGYS--------- 153
Cdd:NF033858 74 VCPRIAYMPQglgKnlyPT---LSVFENLDFFGRLF-GQDAAERRRRID-ELLRA------------TGLApfadrpagk 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 154 LSGGQQQR--LCIArgiAIR-PEVLLLDEPCSALDPISTGRIEELITELKQD---YTVVIVTHNMQQAARCsDHTAFMYL 227
Cdd:NF033858 137 LSGGMKQKlgLCCA---LIHdPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAERF-DWLVAMDA 212
|
250 260
....*....|....*....|.
gi 490994015 228 G---------ELIEFSNTDDL 239
Cdd:NF033858 213 GrvlatgtpaELLARTGADTL 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-252 |
2.17e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.45 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY----GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNI-LTNTQD 85
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLrLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKPtpfpMSIYD-NIAFGVRLFEKLSRTDMD----ERVQWALTKAALW------NETKDKLHQSGYSL 154
Cdd:PRK15093 84 RKLVGHNVSMIFQEP----QSCLDpSERVGRQLMQNIPGWTYKgrwwQRFGWRKRRAIELlhrvgiKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260
....*....|....*....|
gi 490994015 233 FSNTDDLFTKPAKKQTEDYI 252
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALI 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-217 |
3.54e-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: 74.95 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGdniltntqdiallraKVGMVFQKPTPFPM 105
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEP---SEGKIKHSG---------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNIAFGVRlFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:TIGR01271 502 TIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 490994015 186 PISTGRI-EELITELKQDYTVVIVTHNMQQAAR 217
Cdd:TIGR01271 581 VVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-244 |
4.43e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 28 NINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLdGDNILTNT-QDIALL--RAKVGMVFQKPTPFP 104
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTRPQ--KGRIVL-NGRVLFDAeKGICLPpeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 -MSIYDNIAFGVRlfeKLSRTDMDERVQwALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:PRK11144 90 hYKVRGNLRYGMA---KSMVAQFDKIVA-LLGIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 184 LD-PistgRIEELIT---ELKQDYTVVI--VTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:PRK11144 159 LDlP----RKRELLPyleRLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-242 |
6.04e-15 |
|
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: 72.25 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKLSVRNLNFYYGKF--HALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNTQDI 86
Cdd:cd03288 18 GEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMVFQKPTPFPMSIYDNIafgvrlfeKLSRTDMDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQ 159
Cdd:cd03288 91 HTLRSRLSIILQDPILFSGSIRFNL--------DPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03288 163 QLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
...
gi 490994015 240 FTK 242
Cdd:cd03288 242 LAQ 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-241 |
7.52e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 5 NATPGKLSVRNLNFYYGKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEIlldgdNILTNT 83
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRL-----ASGKI-----SILGQP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 84 QDIALLRAKVGMVFQKPT---PFPMSIYDNIA---FGVRLFEKLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGG 157
Cdd:PRK15056 71 TRQALQKNLVAYVPQSEEvdwSFPVLVEDVVMmgrYGHMGWLRRAKKRDRQIVTAALARVDM----VEFRHRQIGELSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAfMYLGELIEFSNT 236
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPT 225
|
....*
gi 490994015 237 DDLFT 241
Cdd:PRK15056 226 ETTFT 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-220 |
8.54e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNI-LTNTQDIalLRAKVGMVFQKPTPF 103
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-----QPDAGSILIDGQEMrFASTTAA--LAAGVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 104 P-MSIYDNIAFGvRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGYsLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK11288 92 PeMTVAENLYLG-QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 490994015 183 ALDPISTGRIEELITELKQDYTVVI-VTHNMQQAARCSD 220
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCD 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-254 |
1.47e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 4 VNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LT 81
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-----VPPDSGTLEIGGNPCarLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NTQDIALlraKVGMVFQKPTPFP-MSIYDNIAFGvrlfekLSRTDMDERVQWALTKAAlwnETKDKLHQSGYSLSGGQQQ 160
Cdd:PRK15439 80 PAKAHQL---GIYLVPQEPLLFPnLSVKENILFG------LPKRQASMQKMKQLLAAL---GCQLDLDSSAGSLEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPIST----GRIEELiteLKQDYTVVIVTHNMQQAARCSDHTAFM-----YLGELI 231
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETerlfSRIREL---LAQGVGIVFISHKLPEIRQLADRISVMrdgtiALSGKT 224
|
250 260
....*....|....*....|...
gi 490994015 232 EFSNTDDLFTKPAKKQTEDYITG 254
Cdd:PRK15439 225 ADLSTDDIIQAITPAAREKSLSA 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-244 |
2.12e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelyPEQ------RAEGEILLDGDNILT-NTQDIALLRAkvgMVFQ 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGgaprgaRVTGDVTLNGEPLAAiDAPRLARLRA---VLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KPTP-FPMSIYDNIAFG----VRLFEKLSRTDMDerVQWaltkAALWNETKDKL-HQSGYSLSGGQQQRLCIARGIA--- 169
Cdd:PRK13547 91 AAQPaFAFSAREIVLLGryphARRAGALTHRDGE--IAW----QALALAGATALvGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 170 ------IRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
...
gi 490994015 242 kPA 244
Cdd:PRK13547 245 -PA 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-210 |
3.63e-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: 68.92 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTN----TQDI 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRPD---SGEVRWNGTPLAEQrdepHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 87 ALLRAKVGMvfqKPTpfpMSIYDNIAFGVRLFEKLSRTDMDervqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:TIGR01189 76 LYLGHLPGL---KPE---LSALENLHFWAAIHGGAQRTIED-----ALAAVGL----TGFEDLPAAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-210 |
6.37e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLdGDNILTN--TQDIAL 88
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPD---SGTVKL-GETVKIGyfDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKvgmvfqkptpfpMSIYDNIAfgvRLFEKLSRTDmdervqwALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:COG0488 390 LDPD------------KTVLDELR---DGAPGGTEQE-------VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490994015 169 AIRPEVLLLDEPCSALDPIStgrIEELiTELKQDY--TVVIVTH 210
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET---LEAL-EEALDDFpgTVLLVSH 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-210 |
7.67e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFELYPE-QRAEGEILLDGDNILTNTQDIall 89
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLS----KVIAGHPAyKILEGDILFKGESILDLEPEE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVG--MVFQKPTPFP--------MSIY------------DNIAFGVRLFEKLSRTDMDERVqwaLTKAAlwNEtkdkl 147
Cdd:CHL00131 81 RAHLGifLAFQYPIEIPgvsnadflRLAYnskrkfqglpelDPLEFLEIINEKLKLVGMDPSF---LSRNV--NE----- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 148 hqsGYslSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTH 210
Cdd:CHL00131 151 ---GF--SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITH 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-242 |
1.27e-13 |
|
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: 69.83 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEqraEGEIL----------------- 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT---SGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 74 --------------LDGDNILTNTQDIALLRAKVGMVFQKPtpfpMSIYDNIAFGVRLFEKLSrtDMDERVQWALTKAA- 138
Cdd:TIGR03269 78 vgepcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRT----FALYGDDTVLDNVLEALE--EIGYEGKEAVGRAVd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 139 LWNETK--DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQ 214
Cdd:TIGR03269 152 LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|....*...
gi 490994015 215 AARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-213 |
1.89e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPEqraEGEILLDGDNIltNTQDIALLRaKVGMVF-QK- 99
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTI----KMLTgiLVPT---SGEVRVLGYVP--FKRRKEFAR-RIGVVFgQRs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 ------PT--PFPM--SIYDniafgvrlfekLSRTDMDERVQWaLTKaALwnETKDKLHQSGYSLSGGQQQRLCIArgiA 169
Cdd:COG4586 106 qlwwdlPAidSFRLlkAIYR-----------IPDAEYKKRLDE-LVE-LL--DLGELLDTPVRQLSLGQRMRCELA---A 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490994015 170 I---RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQ 213
Cdd:COG4586 168 AllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-243 |
1.98e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 41 FIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGDNILTNTQ-DIALLRAKVGMvfQKPTPFPMSIYDNIAF----GV 115
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLP------GSGSIQFAGQPLEAWSAaELARHRAYLSQ--QQTPPFAMPVFQYLTLhqpdKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 116 RLFEKLSR-TDMDERVQwaLTkaalwnetkDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLLDEPCSALDPI 187
Cdd:PRK03695 99 RTEAVASAlNEVAEALG--LD---------DKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 188 STGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK03695 168 QQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-252 |
2.23e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGDNI-LTNTQDIAll 89
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYPHGTYEGEIIFEGEELqASNIRDTE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRTDMDERVQWAltkAALWNETKDKL--HQSGYSLSGGQQQRLCIAR 166
Cdd:PRK13549 81 RAGIAIIHQELALVKeLSVLENIFLGNEI-TPGGIMDYDAMYLRA---QKLLAQLKLDInpATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfTKPAK 245
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICVIRDGRHIG--------TRPAA 228
|
....*..
gi 490994015 246 KQTEDYI 252
Cdd:PRK13549 229 GMTEDDI 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-220 |
2.24e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 20 YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNTQdiaLLRAKVGMVFQK 99
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PD---AGKITVLGVPVPARAR---LARARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 PTPFP-MSIYDN-IAFGvRLFeKLSRTDMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:PRK13536 123 DNLDLeFTVRENlLVFG-RYF-GMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490994015 178 DEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSD 220
Cdd:PRK13536 197 DEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCD 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-237 |
3.00e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 5 NATPgKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNILTNTQ 84
Cdd:PRK09700 1 MATP-YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--P---TKGTITINNINYNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIAlLRAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRTD------MDERVQWALTKAALwnetKDKLHQSGYSLSGG 157
Cdd:PRK09700 75 KLA-AQLGIGIIYQELSVIdELTVLENLYIGRHLTKKVCGVNiidwreMRVRAAMMLLRVGL----KVDLDEKVANLSIS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT-VVIVTHNMQQAARCSDHTAFM------YLGEL 230
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVMkdgssvCSGMV 229
|
....*..
gi 490994015 231 IEFSNTD 237
Cdd:PRK09700 230 SDVSNDD 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-237 |
3.27e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 4 VNATPGK--LSVRNLNfyyGKfhALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNILT 81
Cdd:PRK10762 249 LDKAPGEvrLKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKV---LYGALP--RTSGYVTLDGHEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NT-QD-----IALL---RAKVGMVFQkptpfpMSIYDNIAF-GVRLFEKLS-RTDMDERVQWALTKAALWNETKDKLHQS 150
Cdd:PRK10762 319 RSpQDglangIVYIsedRKRDGLVLG------MSVKENMSLtALRYFSRAGgSLKHADEQQAVSDFIRLFNIKTPSMEQA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
....*....
gi 490994015 230 LI-EFSNTD 237
Cdd:PRK10762 473 ISgEFTREQ 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-210 |
3.59e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 1 MSMVNATPGKLSvrnlnfyYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNkmfelypeqraeGEILLDgDNIL 80
Cdd:PRK11147 1 MSLISIHGAWLS-------FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLD-DGRI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 81 TNTQDIALLRAKvgmvfQKPtpfPM----SIYDNIAFGVR-LFEKLSR---------TDMDE-------RVQWALTKAAL 139
Cdd:PRK11147 61 IYEQDLIVARLQ-----QDP---PRnvegTVYDFVAEGIEeQAEYLKRyhdishlveTDPSEknlnelaKLQEQLDHHNL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 140 W---NETKDKLHQSGY-------SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgrIEELITELKqDY--TVVI 207
Cdd:PRK11147 133 WqleNRINEVLAQLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLK-TFqgSIIF 208
|
...
gi 490994015 208 VTH 210
Cdd:PRK11147 209 ISH 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-217 |
1.37e-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: 66.03 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGdniltntqdiallraKVGMVFQKPTPFPM 105
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEP---SEGKIKHSG---------------RISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNIAFGVrlfeklsrtDMDERVQWALTKAALWNE------TKDK--LHQSGYSLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:cd03291 113 TIKENIIFGV---------SYDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490994015 178 DEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAAR 217
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-242 |
2.14e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNI----LTNtqdialLRAKVGMVFQKPT 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL-----EKGRIMIDDCDVakfgLTD------LRRVLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 102 PFPMSIydniAFGVRLFEKLSRTDMDERVQWALTKAALWNET---KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:PLN03232 1321 LFSGTV----RFNIDPFSEHNDADLWEALERAHIKDVIDRNPfglDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 179 EPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-239 |
2.81e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 13 VRNLNFYygKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFELYPeqRAEGEILLDGDNILTNTQDIALlraK 92
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDK--RAGGEIRLNGKDISPRSPLDAV---K 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 93 VGMVF----QKPTPF--PMSIYDNIAFGVRLfeKLSR--------TDMDERvQWALTKAALWNETKDKLHQSGYSLSGGQ 158
Cdd:PRK09700 338 KGMAYitesRRDNGFfpNFSIAQNMAISRSL--KDGGykgamglfHEVDEQ-RTAENQRELLALKCHSVNQNITELSGGN 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIE-FSNT 236
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNR 494
|
...
gi 490994015 237 DDL 239
Cdd:PRK09700 495 DDM 497
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-210 |
4.64e-12 |
|
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: 62.56 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEI-LLDGDNILtntqdiallrakvgMVFQKPtpfp 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIgMPEGEDLL--------------FLPQRP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 105 msiYdnIAFGvRLFEKLSRTdmdervqwaltkaalWNETkdklhqsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSAL 184
Cdd:cd03223 74 ---Y--LPLG-TLREQLIYP---------------WDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*.
gi 490994015 185 DPISTGRIEELITELKqdYTVVIVTH 210
Cdd:cd03223 123 DEESEDRLYQLLKELG--ITVISVGH 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-212 |
5.45e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFH--ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGdniltntqdial 88
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKG------------ 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lraKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRTDMdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:TIGR00957 700 ---SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVL-EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELIT---ELKQDYTVVIVTHNM 212
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGI 822
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-234 |
6.86e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDgdniltntQDIAllrakvgMVFQKPTPFPM 105
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----SEGRVWAE--------RSIA-------YVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNIAFgvrlFEKLSRTDMDERVQ-------WALTKAALWNETKDKlhqsGYSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:PTZ00243 736 TVRGNILF----FDEEDAARLADAVRvsqleadLAQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 179 EPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGElIEFS 234
Cdd:PTZ00243 808 DPLSALDAHVGERVvEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR-VEFS 862
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-221 |
4.51e-11 |
|
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: 60.73 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLL---------RTFNKMFELYPEQRAEGEILLDGDNILTNTQDIAL------ 88
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAIAIdqktts 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 --LRAKVGMVfqkptpfpMSIYDNIAFgvrLFeklSRTDMDERVQWaLTKAALWNETkdkLHQSGYSLSGGQQQRLCIAR 166
Cdd:cd03270 89 rnPRSTVGTV--------TEIYDYLRL---LF---ARVGIRERLGF-LVDVGLGYLT---LSRSAPTLSGGEAQRIRLAT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 167 GIAIR-PEVL-LLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNmQQAARCSDH 221
Cdd:cd03270 151 QIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHD-EDTIRAADH 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-209 |
6.02e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRAEGEILLDGDNIltntqDIALLRAKVGMVFQKPTPF 103
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 104 PM-SIYDNIAFG--VRLFEKLSRTDMDERVQWALTKAALWNETKDKLHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:TIGR00955 112 PTlTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|.
gi 490994015 179 EPCSALDPISTGRIEELITELKQDYTVVIVT 209
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-185 |
7.88e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY---GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqRAEGEILLdgdniltntqdia 87
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASVVI------------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 llRAKVGMVFQKPTPFPMSIYDNIAFGVRlFEKlsrtdmdERVQWALTKAALWNETK-------DKLHQSGYSLSGGQQQ 160
Cdd:PLN03130 678 --RGTVAYVPQVSWIFNATVRDNILFGSP-FDP-------ERYERAIDVTALQHDLDllpggdlTEIGERGVNISGGQKQ 747
|
170 180
....*....|....*....|....*
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-242 |
1.46e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.29 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTntQDIALLRAKVGMVFQKPTPFPM 105
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDISK--FGLMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIydniAFGVRLFEKLSRTDMDERVQWALTKAALWNETKD---KLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PLN03130 1328 TV----RFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGldaEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 183 ALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-210 |
1.47e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeQRAEGEILLDGDNILTNTQDialLR 90
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY---EVTGGTVEFKGKDLLELSPE---DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVG--MVFQKPTPFP-------MSIYDNIAFGVRLFEKLSRTDMDERVQwalTKAALWNETKDKLHQS-GYSLSGGQQQ 160
Cdd:PRK09580 76 AGEGifMAFQYPVEIPgvsnqffLQTALNAVRSYRGQEPLDRFDFQDLME---EKIALLKMPEDLLTRSvNVGFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490994015 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTH 210
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-240 |
1.64e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.95 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltNTQDIALLRAKVGMVFQKPTPFPM 105
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-----CGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNI-----AFGVRLFEKLSRTDMDERVqwaltkaALWNETKD-KLHQSGYSLSGGQQQRLCIARGIAIRPE-VLLLD 178
Cdd:PTZ00243 1399 TVRQNVdpfleASSAEVWAALELVGLRERV-------ASESEGIDsRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 179 EPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCS-----DHTAFMYLG---ELIEfsNTDDLF 240
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDkiivmDHGAVAEMGsprELVM--NRQSIF 1539
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-213 |
2.72e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 8 PG--KLSVRNLNFYYG---KFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRAEgeilldgdniltn 82
Cdd:PLN03232 610 PGapAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAETSS------------- 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 83 tqdiALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlFEKlsrtdmdERVQWALTKAALWNE-------TKDKLHQSGYSLS 155
Cdd:PLN03232 675 ----VVIRGSVAYVPQVSWIFNATVRENILFGSD-FES-------ERYWRAIDVTALQHDldllpgrDLTEIGERGVNIS 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDP-ISTGRIEELITELKQDYTVVIVTHNMQ 213
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLH 801
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
43-210 |
3.48e-10 |
|
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: 57.89 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 43 GPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNTQDIAllRAKVGMVFQKPTPFPMSIYDNIAFgvrlfekLS 122
Cdd:cd03231 33 GPNGSGKTTLLRILAGL-----SPPLAGRVLLNGGPLDFQRDSIA--RGLLYLGHAPGIKTTLSVLENLRF-------WH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 123 RTDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIT-ELKQ 201
Cdd:cd03231 99 ADHSDEQVEEALARVGL----NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAgHCAR 174
|
....*....
gi 490994015 202 DYTVVIVTH 210
Cdd:cd03231 175 GGMVVLTTH 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-254 |
4.86e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNILTNTQDIAlLRAKVGMVFQKPTPF- 103
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIY--QKDSGSILFQGKEIDFKSSKEA-LENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 104 PMSIYDNIAFGvRLFEKLSRTDMDErvqwaltkaaLWNETK---DKL------HQSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:PRK10982 87 QRSVMDNMWLG-RYPTKGMFVDQDK----------MYRDTKaifDELdididpRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 175 LLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfTKPAKKQTEDYIT 253
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDKII 227
|
.
gi 490994015 254 G 254
Cdd:PRK10982 228 A 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-224 |
9.40e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 9.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNILTN----TQDiallrAKVGMVFQKP 100
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSILYLGKEVTFNgpksSQE-----AGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 TPFP-MSIYDNIAFGVRLFEKLSRTDMDERVQWA---LTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:PRK10762 89 NLIPqLTIAENIFLGREFVNRFGRIDWKKMYAEAdklLARLNL----RFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490994015 177 LDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAAR-CSDHTAF 224
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEiCDDVTVF 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-185 |
1.10e-09 |
|
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: 56.48 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 8 PGKLSVRNLNFY----YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfelypEQRA-----EGEILLDGDN 78
Cdd:cd03232 1 GSVLTWKNLNYTvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--------AGRKtagviTGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 79 IltntqDIALLRaKVGMVFQKPTPFPMSiydniafgvrlfeklsrtdmdeRVQWALTKAALWNEtkdklhqsgysLSGGQ 158
Cdd:cd03232 73 L-----DKNFQR-STGYVEQQDVHSPNL----------------------TVREALRFSALLRG-----------LSVEQ 113
|
170 180
....*....|....*....|....*..
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-236 |
1.13e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 7 TPGK--LSVRNLNFYygKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILTNTQ 84
Cdd:PRK10982 245 KPGEviLEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKKINNHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 85 DIALL---------RAKVGMVFQKPTPFPmSIYDNIAFGVRLFEKLSRTDMDERVQWALTKAalwnETKDKLHQSGY-SL 154
Cdd:PRK10982 318 NEAINhgfalvteeRRSTGIYAYLDIGFN-SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSM----RVKTPGHRTQIgSL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
...
gi 490994015 234 SNT 236
Cdd:PRK10982 473 VDT 475
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-200 |
1.35e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGK--LSVRNLNFY-YGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEILLDGDNIlT 81
Cdd:COG3845 251 AEPGEvvLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEA------LAGLRPPAsGSIRLDGEDI-T 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NtQDIALLRA-----------KVGMVfqkPTpfpMSIYDNIAFGVRLFEKLSRT---DMDERVQWALTKAALWNETKDKL 147
Cdd:COG3845 324 G-LSPRERRRlgvayipedrlGRGLV---PD---MSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELIEEFDVRTPGP 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 148 HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK 200
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR 449
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-230 |
1.38e-09 |
|
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: 57.91 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYY---GKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeQRAEGEILLDGDNILTNTQDIA 87
Cdd:TIGR02633 258 LEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQA---LFGAYP-GKFEGNVFINGKPVDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LlRAKVGMV---FQKPTPFP-MSIYDNIAFGV-RLFEKLSRTDmDERVQWALTKAAlwnetkDKLHQSGYS-------LS 155
Cdd:TIGR02633 334 I-RAGIAMVpedRKRHGIVPiLGVGKNITLSVlKSFCFKMRID-AAAELQIIGSAI------QRLKVKTASpflpigrLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-212 |
1.42e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGdniltntqdiallR 90
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-----LGLVAPDEGVIKRNG-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQK----PT-PFPMSIYDNIAFGVRlfeklsRTDMD---ERVQwaltKAALWNETKDKLhqsgyslSGGQQQRL 162
Cdd:PRK09544 67 LRIGYVPQKlyldTTlPLTVNRFLRLRPGTK------KEDILpalKRVQ----AGHLIDAPMQKL-------SGGETQRV 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNM 212
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-222 |
1.58e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 25 ALKNINLDITKNQVTAFIGPSGCGKSTLlrtfnkMFEL---YPEQRAEGEILLDGD-------------NILTNTQDIAL 88
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTL------MKVLsgvYPHGSYEGEILFDGEvcrfkdirdsealGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LrakvgmvfqkptPFpMSIYDNIAFGvrlfeklsrtdmDERVQWALTKaalWNETKDK---------LHQSGYSLSG--- 156
Cdd:NF040905 90 I------------PY-LSIAENIFLG------------NERAKRGVID---WNETNRRarellakvgLDESPDTLVTdig 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 157 -GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHT 222
Cdd:NF040905 142 vGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-210 |
3.16e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 37 QVTafiGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNTQDIALLRA------KVGMvfqKP--TPFpmsiy 108
Cdd:PRK13538 31 QIE---GPNGAGKTSLLRILAGL-----ARPDAGEVLWQGEPI--RRQRDEYHQDllylghQPGI---KTelTAL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 109 DNIAFGVRLFEKLSrtdmDERVQWALTKAALwnetkdklhqSGY------SLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK13538 93 ENLRFYQRLHGPGD----DEALWEALAQVGL----------AGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 490994015 183 ALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:PRK13538 159 AIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-210 |
3.32e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.87 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 19 YYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLDGDniltntqdiallrAKVGMVFQ 98
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGV--DKDFNGEARPQPG-------------IKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 KPTPFP-MSIYDNIAFGVR-----------LFEKLSR--TDMDE------RVQWALTKAALWN-ETK-----DKLH---- 148
Cdd:TIGR03719 76 EPQLDPtKTVRENVEEGVAeikdaldrfneISAKYAEpdADFDKlaaeqaELQEIIDAADAWDlDSQleiamDALRcppw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 149 -QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELItelkQDY--TVVIVTH 210
Cdd:TIGR03719 156 dADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYpgTVVAVTH 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-242 |
1.15e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 2 SMVNATPGKLSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTllrtfnkmfELYPEQRAEGEILLDGDNILT 81
Cdd:NF000106 5 TISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R---------GALPAHV*GPDAGRRPWRF*T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 82 NTQDIALLRAKVGMvfQKPTPF----PMSIYDNIAFGVRLFEkLSRTDMDERVQWALTKAALwnetKDKLHQSGYSLSGG 157
Cdd:NF000106 76 WCANRRALRRTIG*--HRPVR*grreSFSGRENLYMIGR*LD-LSRKDARARADELLERFSL----TEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
....*.
gi 490994015 237 DDLFTK 242
Cdd:NF000106 229 DELKTK 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-221 |
2.28e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 14 RNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLL--------RTFNKMFELYPEQRAEGEILLDgdnIltnTQD 85
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLslitgdhpQGYSNDLTLFGRRRGSGETIWD---I---KKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 86 IALLRAKVGMVFQKPTpfpmSIYDNIAFG----VRLFEKLSRTDMDERVQWaLTKAALWNETKDKLHQSgysLSGGQQQR 161
Cdd:PRK10938 338 IGYVSSSLHLDYRVST----SVRNVILSGffdsIGIYQAVSDRQQKLAQQW-LDILGIDKRTADAPFHS---LSWGQQRL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 162 LCIARGIAIRPEVLLLDEPCSALDPIStgR------IEELITElkQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLN--RqlvrrfVDVLISE--GETQLLFVSHHAEDAPACITH 471
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-217 |
4.13e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 33 ITKNQVTAFIGPSGCGKSTLLRTFnkmfelypEQRAEGEILLDgdNILTNTQDIA--LLRaKVGMVFQKPTPFP-MSIYD 109
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNAL--------AGRIQGNNFTG--TILANNRKPTkqILK-RTGFVTQDDILYPhLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 110 NIAFG--VRLFEKLSRtdmDERVQWALTKAALWNETKDKLHQSGYS----LSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:PLN03211 160 TLVFCslLRLPKSLTK---QEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|....
gi 490994015 184 LDPISTGRIEELITELKQDYTvVIVTHNMQQAAR 217
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSR 269
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
55-235 |
4.53e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 55 TFNKMFELYPeQRAEGEILLDGDNILTNT------QDIALL---RAKVGMVFQkptpfpMSIYDNI--------AFGVRL 117
Cdd:PRK13549 304 LVQCLFGAYP-GRWEGEIFIDGKPVKIRNpqqaiaQGIAMVpedRKRDGIVPV------MGVGKNItlaaldrfTGGSRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 118 FEKLSRTDMDERVQWALTKAAlwnetkdKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIT 197
Cdd:PRK13549 377 DDAAELKTILESIQRLKVKTA-------SPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490994015 198 EL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI-EFSN 235
Cdd:PRK13549 450 QLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKgDLIN 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-210 |
5.34e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLdGDNiltntqdiallr 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKW-SEN------------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMvfqkptpFPMSIYDNIAFGVRLFEKLSR----TDMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK15064 382 ANIGY-------YAQDHAYDFENDLTLFDWMSQwrqeGDDEQAVRGTLGRLLF---SQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490994015 167 GIAIRPEVLLLDEPCSALDPIStgrIEELITELKQ-DYTVVIVTH 210
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSH 493
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-215 |
6.04e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 16 LNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMFElypeqrAEGEILLDGDniltntqdiallrakvgm 95
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLY------ASGKARLISF------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 96 vfqKPTPFPMSIydnIAFGvrlfeKLSRtdmdervqwaLTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPE-- 173
Cdd:cd03238 54 ---LPKFSRNKL---IFID-----QLQF----------LIDVGL---GYLTLGQKLSTLSGGELQRVKLASELFSEPPgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490994015 174 VLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHN---MQQA 215
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSA 155
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-242 |
1.36e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 23 FHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDniltntqdIALLRAKVGMVFQkptp 102
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG--SLSP---TVGKVDRNGE--------VSVIAISAGLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 103 fpMSIYDNIAFGVrLFEKLSRTDMDErvqwALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK13546 100 --LTGIENIEFKM-LCMGFKRKEIKA----MTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 183 ALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-210 |
1.55e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGK--FhALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNIltNTQDIA 87
Cdd:PRK10522 322 TLELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKPV--TAEQPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 88 LLRAKVGMVFQKptpfpmsiydniafgVRLFEKLsrtdMDERVQWALTKAA-LWNET---KDKLHQSGY-----SLSGGQ 158
Cdd:PRK10522 394 DYRKLFSAVFTD---------------FHLFDQL----LGPEGKPANPALVeKWLERlkmAHKLELEDGrisnlKLSKGQ 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTgRI--EELITELKQ-DYTVVIVTH 210
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFR-REfyQVLLPLLQEmGKTIFAISH 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
149-230 |
3.52e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 149 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYL 227
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
...
gi 490994015 228 GEL 230
Cdd:PRK15439 479 GEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-213 |
5.22e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 9 GKL--SVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLL--------------RTFNKM----F-----ELY 63
Cdd:PRK11147 316 GKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLklmlgqlqadsgriHCGTKLevayFdqhraELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 64 PEQR-----AEG--EILLDGD--NILTNTQDIaLLRAKVGMvfqkpTPfpmsiydniafgvrlfeklsrtdmdervqwal 134
Cdd:PRK11147 396 PEKTvmdnlAEGkqEVMVNGRprHVLGYLQDF-LFHPKRAM-----TP-------------------------------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 135 TKAalwnetkdklhqsgysLSGGQQQRLCIARgIAIRPEVLL-LDEPCSALDpistgrIE--ELITELKQDY--TVVIVT 209
Cdd:PRK11147 438 VKA----------------LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD------VEtlELLEELLDSYqgTVLLVS 494
|
....
gi 490994015 210 HNMQ 213
Cdd:PRK11147 495 HDRQ 498
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-221 |
5.91e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.15 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLLrtfNKMfeLYP--EQRAEGEILLDGdniltNTQDIALLRA--KVGMVFQK 99
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLI---NDT--LYPalARRLHLKKEQPG-----NHDRIEGLEHidKVIVIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 P---TP--------------------------------------------FPMSIYDNIAFgvrlFEKLSRtdMDERVQw 132
Cdd:cd03271 79 PigrTPrsnpatytgvfdeirelfcevckgkrynretlevrykgksiadvLDMTVEEALEF----FENIPK--IARKLQ- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 133 ALTKAALwnetkD--KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALdpiSTGRIEELITEL----KQDY 203
Cdd:cd03271 152 TLCDVGL-----GyiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL---HFHDVKKLLEVLqrlvDKGN 223
|
250
....*....|....*...
gi 490994015 204 TVVIVTHNMqQAARCSDH 221
Cdd:cd03271 224 TVVVIEHNL-DVIKCADW 240
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-210 |
1.85e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 6 ATPGKLSVRNLNFYY------GKFHaLKNINLDITKNQVTAFIGPSGCGKSTLLrtfnKMFE-LYPEQraEGEILLDGDN 78
Cdd:COG4615 323 ADFQTLELRGVTYRYpgedgdEGFT-LGPIDLTIRRGELVFIVGGNGSGKSTLA----KLLTgLYRPE--SGEILLDGQP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 79 IltNTQDIALLRAKVGMVFqkpTPFpmsiYdniafgvrLFEKL---SRTDMDERVQWALTKAALwnetKDKLH-QSGY-- 152
Cdd:COG4615 396 V--TADNREAYRQLFSAVF---SDF----H--------LFDRLlglDGEADPARARELLERLEL----DHKVSvEDGRfs 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 153 --SLSGGQQQRLciARGIAI---RPeVLLLDEPCSALDPISTgRI--EELITELK-QDYTVVIVTH 210
Cdd:COG4615 455 ttDLSQGQRKRL--ALLVALledRP-ILVFDEWAADQDPEFR-RVfyTELLPELKaRGKTVIAISH 516
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-210 |
2.04e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 18 FYYGKFHALKNINLditknqvtAF--------IGPSGCGKSTLLRTfnkMFELypEQRAEGE-ILLDGdniltntqdial 88
Cdd:PRK11819 15 VVPPKKQILKDISL--------SFfpgakigvLGLNGAGKSTLLRI---MAGV--DKEFEGEaRPAPG------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 lrAKVGMVFQKPTPFP-MSIYDNIAFGVR-LFEKLSR------------TDMDE------RVQWALTKAALWN-ETK--- 144
Cdd:PRK11819 70 --IKVGYLPQEPQLDPeKTVRENVEEGVAeVKAALDRfneiyaayaepdADFDAlaaeqgELQEIIDAADAWDlDSQlei 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490994015 145 --DKLH-----QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELItelkQDY--TVVIVTH 210
Cdd:PRK11819 148 amDALRcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-52 |
5.20e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 5.20e-06
10 20
....*....|....*....|....*....
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTL 52
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-210 |
5.77e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKFHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNIltnTQDIALLR 90
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLN--PEK---GEILFERQSI---KKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRlfekLSRTDMDervqwaLTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:PRK13540 74 KQLCFVGHRSGINPyLTLRENCLYDIH----FSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490994015 170 IRPEVLLLDEPCSALDPIStgrIEELITEL----KQDYTVVIVTH 210
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELS---LLTIITKIqehrAKGGAVLLTSH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-208 |
5.81e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 29 INLDITKNQVTAFIGPSGCGKSTLLRTfnkmfeLY-PEQRAEGEILLDGDNILTNT------QDIALL---RAKVGMVfq 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKL------LYgATRRTAGQVYLDGKPIDIRSprdairAGIMLCpedRKAEGII-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 99 kptpfPM-SIYDNIA---------FGVRLFEKLSRTDMDERVQwaltkaALWNETKDKlHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK11288 344 -----PVhSVADNINisarrhhlrAGCLINNRWEAENADRFIR------SLNIKTPSR-EQLIMNLSGGNQQKAILGRWL 411
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490994015 169 AIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIV 208
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFV 452
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
6.79e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 6.79e-06
10 20
....*....|....*....|....*....
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTL 52
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
10-211 |
1.11e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 10 KLSVRNLNFYYGKfhalknINLDITKNqVTAFIGPSGCGKSTLLRTFNkmFELYPEQRAEGEILLDGDNILTNtqdiall 89
Cdd:COG0419 4 RLRLENFRSYRDT------ETIDFDDG-LNLIVGPNGAGKSTILEAIR--YALYGKARSRSKLRSDLINVGSE------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 90 RAKVGMVFQ-KPTPF----------------PMSIYDNIA--FGVRLFEKLSR--TDMDERVQWALTKAALWNETKDKLH 148
Cdd:COG0419 68 EASVELEFEhGGKRYrierrqgefaefleakPSERKEALKrlLGLEIYEELKErlKELEEALESALEELAELQKLKQEIL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 149 Q--SGY----SLSGGQQQRLCIARGIAirpevLLLDEpcSALDPISTGRIEELITELKqdytvvIVTHN 211
Cdd:COG0419 148 AqlSGLdpieTLSGGERLRLALADLLS-----LILDF--GSLDEERLERLLDALEELA------IITHV 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-185 |
1.27e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 27 KNINLDITKNQVTAFIGPSGCGKSTLLRtfnkmfelypeqraegeiLLDGDniLTNTQDIALLRAKVGM-VFQKPTPFPM 105
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGE--LQPSSGTVFRSAKVRMaVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDN-IAFGVRLFEKLsrtdMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSAL 184
Cdd:PLN03073 586 DLSSNpLLYMMRCFPGV----PEQKLRAHLGSFGV---TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
.
gi 490994015 185 D 185
Cdd:PLN03073 659 D 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-71 |
1.28e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTLlrTFNKMFelypeqrAEGE 71
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL--AFDTIY-------AEGQ 48
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
42-210 |
1.32e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 42 IGPSGCGKSTLLRTFNkmfELYPeqraegeiLLDGdnILTNTQDIALLrakvgMVFQKP----------TPFPMSIYDNI 111
Cdd:TIGR00954 484 CGPNGCGKSSLFRILG---ELWP--------VYGG--RLTKPAKGKLF-----YVPQRPymtlgtlrdqIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 112 AFGVR---LFEKLSRTDMDErvqwALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPis 188
Cdd:TIGR00954 546 RRGLSdkdLEQILDNVQLTH----ILEREGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV-- 615
|
170 180
....*....|....*....|....
gi 490994015 189 tgRIEELITELKQDY--TVVIVTH 210
Cdd:TIGR00954 616 --DVEGYMYRLCREFgiTLFSVSH 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-212 |
3.28e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490994015 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-241 |
3.33e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 21 GKFH-ALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDniltntqdIALLRAKVGMVFQk 99
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV-----TMPNKGTVDIKGS--------AALIAISSGLNGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 100 ptpfpMSIYDNIAFGvRLFEKLSRtdmdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13545 100 -----LTGIENIELK-GLMMGLTK----EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490994015 180 PCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-210 |
3.78e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 38 VTAFIGPSGCGKSTLLRTFNkmFELYPEQRAeGEILLDGDNILTNTQDIallRAKVGMVFQKPTPFPM------SIYDNI 111
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK--YALTGELPP-NSKGGAHDPKLIREGEV---RAQVKLAFENANGKKYtitrslAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 112 AFgVRlfeklsrtdmDERVQWALTkaalwnETKDklhqsgySLSGGQQQ------RLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:cd03240 98 IF-CH----------QGESNWPLL------DMRG-------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*...
gi 490994015 186 PIS-TGRIEELITELKQDYT--VVIVTH 210
Cdd:cd03240 154 EENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-221 |
3.96e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 152 YSLSGGQQQRLCIARGI---AIRPEVLLLDEPCSALdpiSTGRIEELITELK----QDYTVVIVTHNMqQAARCSDH 221
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVADY 880
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-210 |
4.38e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 143 TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIteLKQDYTVVIVTH 210
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-235 |
5.68e-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: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 35 KNQVTAFIGPSGCGKSTLLRTFNKMFelypEQRAEGEILLDGDNILTNTQDIALLrakvgmvfqkptpfpmsiydniafg 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL----GPPGGGVIYIDGEDILEEVLDQLLL------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 115 vrlfeklsrtdmdervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEE 194
Cdd:smart00382 52 ------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490994015 195 LIT------ELKQDYTVVIVTHNMQQAARcsDHTAFMYLGELIEFSN 235
Cdd:smart00382 102 LEElrllllLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLL 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-185 |
7.83e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 26 LKNINLDITKNQVTAFIGPSGCGKSTLLRTFnkmfelypeqraEGEILLDGDNIlTNTQDIALlrakvGMVFQKPTPFPM 105
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL------------KNEISADGGSY-TFPGNWQL-----AWVNQETPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 106 SIYDNIAFGVRLFEKL--------SRTD----------MDERVQWALTK--AALWNE---TKDKLHQSGYSLSGGQQQRL 162
Cdd:PRK10636 79 PALEYVIDGDREYRQLeaqlhdanERNDghaiatihgkLDAIDAWTIRSraASLLHGlgfSNEQLERPVSDFSGGWRMRL 158
|
170 180
....*....|....*....|...
gi 490994015 163 CIARGIAIRPEVLLLDEPCSALD 185
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLD 181
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
146-212 |
9.35e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 9.35e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 146 KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALdpiSTGRIEELITEL----KQDYTVVIVTHNM 212
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL---HFDDIKKLLEVLqrlvDKGNTVVVIEHNL 892
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-226 |
1.23e-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: 41.58 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490994015 154 LSGGQQQR--LCIARGIA-IRPEVL-LLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTHNMQQAARcSDHTAFMY 226
Cdd:cd03227 78 LSGGEKELsaLALILALAsLKPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-225 |
1.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 147 LHQSGYSLSGGQQQRLCIARGIAIRPE--VLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAF 224
Cdd:PRK00635 1381 LGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIH 1460
|
.
gi 490994015 225 M 225
Cdd:PRK00635 1461 L 1461
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-226 |
1.89e-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: 41.58 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 37 QVTAFIGPSGCGKSTLLRTFNKmfELYPE-QRAEGEIllDGDNILTNTQDIAL------LRAKVGMVFQKPtpfpmSIYD 109
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAG--KLKPNlGKFDDPP--DWDEILDEFRGSELqnyftkLLEGDVKVIVKP-----QYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 110 NI--AFGVRLFEKLSRTDmdERVQWALTKAALwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD-- 185
Cdd:cd03236 98 LIpkAVKGKVGELLKKKD--ERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490994015 186 -PISTGR-IEELITELKqdyTVVIVTHNMQQAARCSDHTAFMY 226
Cdd:cd03236 174 qRLNAARlIRELAEDDN---YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
11-179 |
2.20e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 11 LSVRNLNFYYGKfHALKNINLDITKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIlTNTQD--IAL 88
Cdd:PRK13541 2 LSLHQLQFNIEQ-KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGI-----MQPSSGNIYYKNCNI-NNIAKpyCTY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 89 LRAKVGMVFQkptpfpMSIYDNIAFGVRLFeklsrtDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK13541 75 IGHNLGLKLE------MTVFENLKFWSEIY------NSAETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLI 138
|
170
....*....|.
gi 490994015 169 AIRPEVLLLDE 179
Cdd:PRK13541 139 ACQSDLWLLDE 149
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
10-60 |
2.38e-04 |
|
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: 41.82 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490994015 10 KLSVRNlnfyygkFHALKNINLDItKNQVTAFIGPSGCGKSTLLRTFNKMF 60
Cdd:pfam13175 5 SIIIKN-------FRCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
25-72 |
3.68e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.96 E-value: 3.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490994015 25 ALKNINLD----ITKNQVTAFIGPSGCGKSTLLrtfNKmfeLYPEQRAE-GEI 72
Cdd:PRK00098 149 AKEGEGLDelkpLLAGKVTVLAGQSGVGKSTLL---NA---LAPDLELKtGEI 195
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
5-53 |
6.42e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 490994015 5 NATPGKLSVRNLNFyygkfHALKNINLDITKNQVTAFIGPSGCGKSTLL 53
Cdd:TIGR00630 608 PGNGKFLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-212 |
7.99e-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: 40.54 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNM 212
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDL 272
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
153-228 |
8.01e-04 |
|
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: 40.77 E-value: 8.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTHNMQQAARCSDHTAFMYLG 228
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
10-56 |
1.06e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 1.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490994015 10 KLSVRNlnfyygkFHALKNINLDITknQVTAFIGPSGCGKSTLLRTF 56
Cdd:COG4637 4 RIRIKN-------FKSLRDLELPLG--PLTVLIGANGSGKSNLLDAL 41
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-72 |
2.04e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.15 E-value: 2.04e-03
10 20 30
....*....|....*....|....*....|....*....
gi 490994015 35 KNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEI 72
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNA------LLPELVLAtGEI 116
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
35-72 |
2.21e-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: 2.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 490994015 35 KNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEI 72
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNA------LLPELDLRtGEI 137
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-213 |
2.90e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490994015 153 SLSGGQQQRLCIAR--GIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQ 213
Cdd:PRK00635 476 TLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQ 539
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
153-180 |
3.15e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 3.15e-03
10 20
....*....|....*....|....*...
gi 490994015 153 SLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
73-211 |
5.13e-03 |
|
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: 37.75 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 73 LLDGDNILTNTQDIALLRAKVGMVFQKPTPFP---MSIYDNIAFGVRLFEKLSRTDMDERVQWaLTKAALWNETKDKLHQ 149
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKELLqrlVRGLKLADLNLSDLGEGIEKSLLVDDRL-RERGLILLENGGGGEL 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490994015 150 SGYSLSGGQQQRLCIA---RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT-VVIVTHN 211
Cdd:pfam13304 233 PAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-213 |
7.81e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 37.46 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 32 DITKNQVTAFIGPSGCGKSTllrtFNKMF--ELYPEqraEGEILLDGDnI------LTNTQDI---ALLRAKVGmvfqkp 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT----FAKILagVLKPD---EGEVDEDLK-IsykpqyISPDYDGtveEFLRSANT------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490994015 101 TPFPMSIYDN-IAFGVRLfEKLsrtdMDERVQwaltkaalwnetkdklhqsgySLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:COG1245 428 DDFGSSYYKTeIIKPLGL-EKL----LDKNVK---------------------DLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|....*..
gi 490994015 180 PCSALD---PISTGRIEELITElKQDYTVVIVTHNMQ 213
Cdd:COG1245 482 PSAHLDveqRLAVAKAIRRFAE-NRGKTAMVVDHDIY 517
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
8.83e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.83e-03
10 20
....*....|....*....|....*....
gi 490994015 24 HALKNINLDITKNQVTAFIGPSGCGKSTL 52
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| |
