|
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: 541.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVE-TAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNI 79
Cdd:COG1117 1 MTAPAsTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 LTNSQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQ 159
Cdd:COG1117 81 YDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....*...
gi 16131593 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 |
3.89e-166 |
|
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: 459.07 E-value: 3.89e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALL 89
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTE 249
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 16131593 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 |
2.55e-145 |
|
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: 405.80 E-value: 2.55e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHqsGYSLSGGQQQRLCIARGIAI 170
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-257 |
3.35e-129 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 366.41 E-value: 3.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALL 89
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFPMSIYDNIAFGVRLfeKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGARI--NGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFM---------YLGELIEFSNTDDLF 240
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIF 247
|
250
....*....|....*..
gi 16131593 241 TKPAKKQTEDYITGRYG 257
Cdd:PRK14243 248 NSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-257 |
3.11e-118 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 338.29 E-value: 3.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTED 250
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 16131593 251 YITGRYG 257
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-257 |
5.23e-105 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 304.84 E-value: 5.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKL--SRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKL-NGLvkSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
250
....*....|
gi 16131593 248 TEDYITGRYG 257
Cdd:PRK14267 244 TEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-255 |
8.74e-100 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 291.43 E-value: 8.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILtnSQDIAL 88
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKL-SRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*....
gi 16131593 247 QTEDYITGR 255
Cdd:PRK14247 240 LTEKYVTGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-257 |
2.88e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 272.68 E-value: 2.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELI--TELKQDYTVVIVTHNMQQAARCSDHTAFMY-----LGELIEFSNTDDLFTKP 243
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 16131593 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 |
1.24e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 231.81 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQT 248
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
....
gi 16131593 249 EDYI 252
Cdd:COG1126 233 RAFL 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-257 |
1.77e-71 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 220.35 E-value: 1.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 4 VETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILtNS 83
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIF-NY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
250
....*....|....
gi 16131593 244 AKKQTEDYITGRYG 257
Cdd:PRK14271 254 KHAETARYVAGLSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-255 |
3.14e-71 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 219.15 E-value: 3.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQ-RAEGEILLDGDNI 79
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKiKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 LtnSQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQ 158
Cdd:PRK14246 81 F--QIDAIKLRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNE 238
|
250
....*....|....*..
gi 16131593 239 LFTKPAKKQTEDYITGR 255
Cdd:PRK14246 239 IFTSPKNELTEKYVIGR 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-225 |
5.19e-71 |
|
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: 216.63 E-value: 5.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFM 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-243 |
2.97e-68 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 219.00 E-value: 2.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNS-Q 84
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL-----LRPTSGSILFDGKDLTKLSrR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKL-HQsgysLSGGQQ 159
Cdd:COG1123 336 SLRELRRRVQMVFQDPYsslnPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHE----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTD 237
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
....*.
gi 16131593 238 DLFTKP 243
Cdd:COG1123 491 EVFANP 496
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-243 |
1.83e-67 |
|
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: 208.34 E-value: 1.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltNSQDIALL 89
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDI--TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:COG1122 74 RRKVGLVFQNPDDqlFAPTVEEDVAFGPENL-GLPREEIRERVEEALELVGLE----HLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 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 |
2.30e-67 |
|
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: 208.12 E-value: 2.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNI--LTNSQDIAL 88
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPDS--GEVLIDGEDIsgLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 lRAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03261 76 -RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 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 |
2.25e-65 |
|
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: 203.29 E-value: 2.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLDGDNILTNSQD-IALL 89
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI--IGLLRPD---SGEILVDGQDITGLSEKeLYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQRLCIARG 167
Cdd:COG1127 81 RRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMpSE----LSGGMRKRVALARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
7.45e-64 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 203.02 E-value: 7.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMvetapSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGd 77
Cdd:COG3842 1 MAM-----PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagF--------ETPDSGRILLDG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 78 niltnsQDIALLRA---KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALtkaalwnetkDKLHQSGYS 153
Cdd:COG3842 67 ------RDVTGLPPekrNVGMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIRARVAELL----------ELVGLEGLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 154 ------LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHT 222
Cdd:COG3842 130 dryphqLSGGQQQRVALARALAPEPRVLLLDEPLSALDA---KLREEMREELRRlqrelGITFIYVTHDQEEALALADRI 206
|
250 260
....*....|....*....|..
gi 16131593 223 AFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-229 |
2.09e-63 |
|
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: 196.25 E-value: 2.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILTNSQDIALLR 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIA 169
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
6.94e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 192.61 E-value: 6.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMvetAPSKIQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEIL 73
Cdd:COG1116 1 MSA---AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagL--------EKPTSGEVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 74 LDGdniltnsQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwNETKDKL-HQsg 151
Cdd:COG1116 70 VDG-------KPVTGPGPDRGVVFQEPALLPwLTVLDNVALGLEL-RGVPKAERRERARELLELVGL-AGFEDAYpHQ-- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 152 ysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFM 225
Cdd:COG1116 139 --LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLADRVVVL 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-245 |
1.89e-60 |
|
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: 198.59 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRAEGEILLDGDNILTnsQDIAL 88
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL--MGLLPHGGRISGEVLLDGRDLLE--LSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:COG1123 81 RGRRIGMVFQDPMTqlNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 16131593 245 K 245
Cdd:COG1123 236 A 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-239 |
2.11e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNSQDIallR 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL--LRPT---SGEVRVLGEDVARDPAEV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLY-GLPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-233 |
2.44e-60 |
|
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: 189.65 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnsQDIALLR 90
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-225 |
2.35e-59 |
|
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: 186.90 E-value: 2.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFH--ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNSQDIALL 89
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDL--TKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKP-TPFPM-SIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03225 74 RRKVGLVFQNPdDQFFGpTVEEEVAFGLENL-GLPEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-252 |
3.46e-59 |
|
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: 187.51 E-value: 3.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltNSQDIALL 89
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE--PT---SGEIFIDGEDI--REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSRADMDERVQWALTKAALwnETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIAL-VPKLLKWPKEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*.
gi 16131593 247 QTEDYI 252
Cdd:cd03295 231 FVAEFV 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-230 |
6.35e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.79 E-value: 6.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNSQDIALLR 90
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-----DPPTSGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKlsRADMdERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRER--KFDR-ERALELLERLGL---PPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-243 |
1.17e-58 |
|
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: 187.27 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILT-NSQ 84
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITAkKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRL 162
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGL---DEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 16131593 241 TKP 243
Cdd:TIGR04521 232 SDV 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
9-244 |
5.82e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 187.97 E-value: 5.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGdniltnsQD 85
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagL--------EDPTSGEILIGG-------RD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALtkaalwnetkDKLHQSGY------SLS 155
Cdd:COG3839 67 VTDLPPKdrnIAMVFQSYALYPhMTVYENIAFPLKL-RKVPKAEIDRRVREAA----------ELLGLEDLldrkpkQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPIStgRiEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKL--R-VEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
250
....*....|....
gi 16131593 231 IEFSNTDDLFTKPA 244
Cdd:COG3839 213 QQVGTPEELYDRPA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-241 |
6.21e-58 |
|
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: 184.86 E-value: 6.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDNILT-NSQDIAll 89
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKP---SSGEVLLDGRDLASlSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 rAKVGMVFQKPT-PFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCI 164
Cdd:COG1120 75 -RRIAYVPQEPPaPFGLTVRELVALGryphLGLFGRPSAED-REAVEEALERTGLE----HLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-244 |
1.06e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 187.28 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfelypeqrA------EGEILLDGDNILTN-- 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII-----------AgletpdSGRIVLNGRDLFTNlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 SQDiallRaKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERV-QWaLTKAALwnetkDKL-----HQsgysLS 155
Cdd:COG1118 72 PRE----R-RVGFVFQHYALFPhMTVAENIAFGLRV-RPPSKAEIRARVeEL-LELVQL-----EGLadrypSQ----LS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250
....*....|.
gi 16131593 234 SNTDDLFTKPA 244
Cdd:COG1118 216 GTPDEVYDRPA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-233 |
4.37e-57 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 181.94 E-value: 4.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDI 86
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL-----LKPTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAK-VGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAAlwNETKDKLHQSGYSLSGGQQQR 161
Cdd:cd03257 77 RKIRRKeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-232 |
1.65e-55 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 177.54 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLR--------TfnkmfelypeqraEGEILLDGDN 78
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilggldrpT-------------SGEVLIDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 79 ILT-NSQDIALLRA-KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLS 155
Cdd:COG1136 72 ISSlSERELARLRRrHIGFVFQFFNLLPeLTALENVALPLLL-AGVSRKERRERARELLERVGL----GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-221 |
1.88e-55 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 177.28 E-value: 1.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLR---TFnkmfelypEQRAEGEILLDGdniltns 83
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiaGL--------ERPTSGEVLVDG------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQR 161
Cdd:cd03293 66 EPVTGPGPDRGYVFQQDALLPwLTVLDNVALGLEL-QGVPKAEARERAEELLELVGL-SGFENAYpHQ----LSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 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 |
8.96e-55 |
|
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: 175.37 E-value: 8.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNSQ 84
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-----DRPTSGEVRVDGTDIskLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPL-LLAGVPKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARC 218
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYA 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-244 |
1.27e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 178.32 E-value: 1.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQRAEGEILLDGDNILTNSQ-D 85
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDLLKLSEkE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAK-VGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL----HQsgysLSG 156
Cdd:COG0444 80 LRKIRGReIQMIFQDPMtslnPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLdrypHE----LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|
gi 16131593 235 NTDDLFTKPA 244
Cdd:COG0444 234 PVEELFENPR 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-252 |
1.28e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 179.12 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NSQD 85
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ERPTSGSVLVDGVDLTAlSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKptpFP-MS---IYDNIAFGVRLfEKLSRADMDERVqwaltkaalwNET------KDKLHQsgY--S 153
Cdd:COG1135 77 LRAARRKIGMIFQH---FNlLSsrtVAENVALPLEI-AGVPKAEIRKRV----------AELlelvglSDKADA--YpsQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|.
gi 16131593 232 EFSNTDDLFTKPAKKQTEDYI 252
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFL 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-243 |
1.58e-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: 175.76 E-value: 1.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEqrAEGEILLDGDNIlTNSQDI 86
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRA---LAGLERP--WSGEVTFDGRPV-TRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALlRAKVGMVFQKPT----PFpMSIYDNIAFGVRLfekLSRADMDERVQWALTKAALWNETKDKL-HQsgysLSGGQQQR 161
Cdd:COG1124 76 AF-RRRVQMVFQDPYaslhPR-HTVDRILAEPLRI---HGLPDREERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
....
gi 16131593 240 FTKP 243
Cdd:COG1124 227 LAGP 230
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-244 |
1.39e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 175.28 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLN-FYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTnsQDIALL 89
Cdd:COG1125 2 IEFENVTkRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEP-----TSGRILIDGEDIRD--LDPVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNET-KDKL-HQsgysLSGGQQQRLCIAR 166
Cdd:COG1125 75 RRRIGYVIQQIGLFPhMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEEyRDRYpHE----LSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-244 |
2.24e-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: 172.42 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGDNILtnsqDIA 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLiagF--------ETPTSGEILLDGKDIT----NLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03300 69 PHKRPVNTVFQNYALFPhLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPistgRI-EELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDL----KLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
....
gi 16131593 241 TKPA 244
Cdd:cd03300 220 EEPA 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-182 |
1.02e-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: 167.82 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNSQDIALLRAKVGMVFQKPTPFP- 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL-----LSPTEGTILLDGQDL--TDDERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 105 MSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:pfam00005 74 LTVRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-225 |
1.16e-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: 168.33 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG--KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNSQDIAL 88
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 168
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFM 225
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DRIIVL 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
11-252 |
2.82e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 169.89 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDIALLR 90
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:PRK09493 77 QEAGMVFQQFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPistgrieELITE-LK--QD-----YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK09493 153 VKPKLMLFDEPTSALDP-------ELRHEvLKvmQDlaeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
250
....*....|.
gi 16131593 242 KPAKKQTEDYI 252
Cdd:PRK09493 226 NPPSQRLQEFL 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-239 |
1.92e-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: 178.10 E-value: 1.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH--ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltNSQDIAL 88
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKL---LLGLYEPT--SGRILIDGIDL--RQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQQR 161
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLG------DPDAT-DEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDL 239
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEEL 696
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-252 |
6.11e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 166.73 E-value: 6.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI----LTNSQDI 86
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQFdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCI 164
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENlIEAPCKVL-GLSKEQAREKAMKLLARLRL----TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSnTDDLFTKP 243
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQP 231
|
....*....
gi 16131593 244 AKKQTEDYI 252
Cdd:COG4161 232 QTEAFAHYL 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-243 |
1.00e-50 |
|
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: 165.83 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDG-DNILTNSQD 85
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGtDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKptpFPM----SIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 161
Cdd:cd03258 77 LRKARRRIGMIFQH---FNLlssrTVFENVALPLEI-AGVPKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....
gi 16131593 240 FTKP 243
Cdd:cd03258 229 FANP 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-241 |
1.66e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.65 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGdniltnsQDIALLR 90
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVRLFG-------KPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPT---PFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLC 163
Cdd:COG1121 75 RRIGYVPQRAEvdwDFPITVRDVVLMGrygrRGLFRRPSRAD-REAVDEALERVGLE----DLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMyLGELIEFSNTDDLFT 241
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-253 |
1.67e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI----LTNSQDI 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNHFdfskTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRADMDERVQWALTKAALwNETKDK--LHqsgysLSGGQQQRL 162
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNlIEAPCRVL-GLSKDQALARAEKLLERLRL-KPYADRfpLH-----LSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEfSNTDDLFT 241
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVE-QGDASCFT 229
|
250
....*....|..
gi 16131593 242 KPAKKQTEDYIT 253
Cdd:PRK11124 230 QPQTEAFKNYLS 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-210 |
1.21e-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: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 4 VETAPSKIQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltn 82
Cdd:COG1132 333 LPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD--PT---SGRILIDGVDI--- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 sQDIAL--LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALW---NETKDKLH----QSGY 152
Cdd:COG1132 405 -RDLTLesLRRQIGVVPQDTFLFSGTIRENIRYG--------RPDAtDEEVEEAAKAAQAHefiEALPDGYDtvvgERGV 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-239 |
2.77e-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: 162.98 E-value: 2.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNSQ--DI 86
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEENlwEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 allRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfE--KLSRADMDERVQWALTKAALWnetkDKLHQSGYSL 154
Cdd:TIGR04520 76 ---RKKVGMVFQNP--------DNqfvgatveddVAFGL---EnlGVPREEMRKRVDEALKLVGME----DFRDREPHLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIstGRIE--ELITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLGEL 230
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK--GRKEvlETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKI 214
|
250
....*....|....*.
gi 16131593 231 IE-------FSNTDDL 239
Cdd:TIGR04520 215 VAegtpreiFSQVELL 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-220 |
4.36e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 161.76 E-value: 4.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNF-YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNS-QDIAL 88
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL--VEP---TSGEILVDGQDVTALRgRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKptpFP----MSIYDNIAFGvRL---------FEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLS 155
Cdd:COG3638 78 LRRRIGMIFQQ---FNlvprLSVLTNVLAG-RLgrtstwrslLGLFPPEDR-ERALEALERVGL----ADKAYQRADQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSD 220
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-213 |
1.63e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 159.83 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNILT-NSQDIA 87
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKL------LYGEERPtSGQVLVNGQDLSRlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKptpFP----MSIYDNIAFGVRLFEKlSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:COG2884 76 YLRRRIGVVFQD---FRllpdRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQ 213
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLE 198
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-239 |
1.74e-48 |
|
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: 168.01 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 6 TAPSKIQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNSQ 84
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsRADmDERVQWALTKAALWNETKD-------KLHQSGYSLSGG 157
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAGTIRENLRLGRP------DAS-DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTD 237
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHE 556
|
..
gi 16131593 238 DL 239
Cdd:COG4988 557 EL 558
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-252 |
3.99e-48 |
|
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: 159.25 E-value: 3.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNSQDialLR 90
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL--LKPD---SGSILIDGEDVRKEPRE---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPtPFP--MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGI 168
Cdd:COG4555 74 RQIGVLPDER-GLYdrLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
....*
gi 16131593 248 TEDYI 252
Cdd:COG4555 228 LEDAF 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-254 |
6.47e-48 |
|
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: 159.73 E-value: 6.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPSKIQVRNLNfyyGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNI- 79
Cdd:cd03294 18 FKLLAKGKSKEEILKKT---GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--P---TSGKVLIDGQDIa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 -LTNSQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGG 157
Cdd:cd03294 90 aMSRKELRELRRKKISMVFQSFALLPhRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL----EGWEHKYPDELSGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSN 235
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
250
....*....|....*....
gi 16131593 236 TDDLFTKPAKKQTEDYITG 254
Cdd:cd03294 245 PEEILTNPANDYVREFFRG 263
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
25-254 |
1.25e-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: 161.56 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILTNSQD--IALLRAKVGMVFQKPTP 102
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIE-----PTAGQIFIDGENIMKQSPVelREVRRKKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 FP-MSIYDNIAFGVrlfeKLSRADMDERVQWALTKAALWNeTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:TIGR01186 83 FPhMTILQNTSLGP----ELLGWPEQERKEKALELLKLVG-LEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 182 SALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITG 254
Cdd:TIGR01186 158 SALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-231 |
2.16e-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: 157.21 E-value: 2.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLlrtFNKMFELYPeqRAEGEILLDGDNILT-NSQDIAll 89
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTL---FNLISGFLR--PTSGSVLFDGEDITGlPPHEIA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLS---------RADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQ 159
Cdd:cd03219 74 RLGIGRTFQIPRLFPeLTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLA----DLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-229 |
2.18e-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: 156.83 E-value: 2.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIlTNSQDIALLR 90
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKT---IMGLLP--PRSGSIRFDGRDI-TGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfekLSRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03224 75 AGIGYVPEGRRIFPeLTVEENLLLGAYA---RRRAKRKARLERVY---ELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-230 |
3.27e-47 |
|
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: 154.48 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNSQDIallR 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKKEPEEV---K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgySLSGGQQQRLCIARGIA 169
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENL-----------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY-TVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-229 |
5.09e-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: 153.55 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGDNILTNsqDIALLRA 91
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI--AGLLKP---TSGEILIDGKDIAKL--PLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAIR 171
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 172 PEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-243 |
7.07e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 156.50 E-value: 7.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 3 MVETAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT- 81
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL-----ETPDSGEIRVGGEEIRLk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 ----------NSQDIALLRAKVGMVFQKptpFP----MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWnetkDKL 147
Cdd:COG4598 76 pdrdgelvpaDRRQLQRIRTRLGMVFQS---FNlwshMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA----DKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 148 HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistgrieELITE-LK--QDY-----TVVIVTHNMQQAARCS 219
Cdd:COG4598 149 DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmRDLaeegrTMLVVTHEMGFARDVS 221
|
250 260
....*....|....*....|....
gi 16131593 220 DHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-252 |
9.51e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.81 E-value: 9.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NSQD 85
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQDLTAlSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKptpFPM----SIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 161
Cdd:PRK11153 77 LRKARRQIGMIFQH---FNLlssrTVFDNVALPLEL-AGTPKAEIKARVTELLELVGL----SDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250
....*....|...
gi 16131593 240 FTKPAKKQTEDYI 252
Cdd:PRK11153 229 FSHPKHPLTREFI 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-244 |
1.12e-45 |
|
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: 152.88 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnsQDIALLR 90
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGEDA----TDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRL---FEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03296 74 RNVGFVFQHYALFRhMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ----LSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDpisTGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALD---AKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
...
gi 16131593 242 KPA 244
Cdd:cd03296 227 HPA 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-230 |
2.33e-45 |
|
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: 151.25 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltnsQDIALLR 90
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGG-------RDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03301 69 PKdrdIAMVFQNYALYPhMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 167 GIAIRPEVLLLDEPCSALDpiSTGRIeELITELK-----QDYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLD--AKLRV-QMRAELKrlqqrLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
11-252 |
3.64e-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: 154.81 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltnsQDIALL- 89
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGG-------RDITRLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 --RAKVGMVFQKPTPFP-MSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNeTKDKlhqsgY--SLSGGQQQRLCI 164
Cdd:TIGR03265 73 pqKRDYGIVFQSYALFPnLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPG-SERK-----YpgQLSGGQQQRVAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDpistGRI-EELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:TIGR03265 146 ARALATSPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
250
....*....|....
gi 16131593 239 LFTKPAKKQTEDYI 252
Cdd:TIGR03265 222 IYRHPATPFVADFV 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-252 |
6.82e-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: 150.95 E-value: 6.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHaLKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNILTNSQDiallR 90
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNGKDITNLPPE----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVqwaLTKAALWNETKdKLHQSGYSLSGGQQQRLCIARGIA 169
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKK-RKVDKKEIERKV---LEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQ 247
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*
gi 16131593 248 TEDYI 252
Cdd:cd03299 226 VAEFL 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-252 |
5.77e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 148.74 E-value: 5.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNfyyGKFHA---LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNILTNSQD 85
Cdd:PRK11264 2 SAIEVKNLV---KKFHGqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 -IALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklhQSGY--SLSGGQQQR 161
Cdd:PRK11264 79 lIRQLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK------ETSYprRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|..
gi 16131593 241 TKPAKKQTEDYI 252
Cdd:PRK11264 233 ADPQQPRTRQFL 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-223 |
8.69e-44 |
|
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: 147.29 E-value: 8.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGdniltnsQDIALLRA 91
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKA---ILGLLK--PTSGSIRVFG-------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVFQK---PTPFPMSIYDNIAFG----VRLFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCI 164
Cdd:cd03235 69 RIGYVPQRrsiDRDFPISVRDVVLMGlyghKGLFRRLSKADK-AKVDEALERVGL----SELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTA 223
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-252 |
4.64e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 149.99 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltnsQDIALL- 89
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDG-------VDLSHVp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 --RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:PRK11607 88 pyQRPINMMFQSYALFPhMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIE-ELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPT 242
|
....*...
gi 16131593 245 KKQTEDYI 252
Cdd:PRK11607 243 TRYSAEFI 250
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-225 |
5.74e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 149.71 E-value: 5.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPSkIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdnil 80
Cdd:PRK09452 6 KQPSSLSPL-VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 81 tnsQDIALLRAK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSG 156
Cdd:PRK09452 76 ---QDITHVPAEnrhVNTVFQSYALFPhMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQ----LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDpiSTGRiEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFM 225
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALD--YKLR-KQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-252 |
6.18e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.67 E-value: 6.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHalKNINLDIAKNQVTAFIGPSGCGKSTLLRT---FnkmfelypEQRAEGEILLDGDNILTNSQDia 87
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLiagF--------LPPDSGRILWNGQDLTALPPA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:COG3840 70 --ERPVSMLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGL----AGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 giAI---RPeVLLLDEPCSALDPIStgRIE--ELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG3840 143 --CLvrkRP-ILLLDEPFSALDPAL--RQEmlDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|...
gi 16131593 240 FTKPAKKQTEDYI 252
Cdd:COG3840 218 LDGEPPPALAAYL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-232 |
8.75e-43 |
|
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: 152.61 E-value: 8.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNILTNSQDIal 88
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQS---GSITLGGVDLRDLDEDD-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAAL--WNETKDK-----LHQSGYSLSGGQQQR 161
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLA------RPDAT-DEELWAALERVGLgdWLAALPDgldtwLGEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-244 |
3.78e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.42 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-----------GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNI 79
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--P---TSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 LT-NSQDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKL-HQsgy 152
Cdd:COG4608 83 TGlSGRELRPLRRRMQMVFQDP--YaslnPrMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYpHE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 153 sLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpIStgrIE----ELITELKQDY--TVVIVTHNMQQAARCSDHTAFMY 226
Cdd:COG4608 158 -FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMY 232
|
250
....*....|....*...
gi 16131593 227 LGELIEFSNTDDLFTKPA 244
Cdd:COG4608 233 LGKIVEIAPRDELYARPL 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-240 |
4.12e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.19 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK---FH--ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNSQD 85
Cdd:PRK13637 3 IKIENLTHIYMEgtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKP---TSGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKP--TPFPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAAL-WNETKDKlhqSGYSLSGGQQQRL 162
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-239 |
4.33e-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: 143.45 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY---GKFHALKNINLDIAKNQVTAFIGPSGCGKST----LLRTFNkmfelyPEqraEGEILLDGDNIltNS 83
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERFYD------PT---SGEILLDGVDI--RD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQwALTKAALWN---ETKDKLH----QSGYSLSG 156
Cdd:cd03249 70 LNLRWLRSQIGLVSQEPVLFDGTIAENIRYG------KPDATDEEVEE-AAKKANIHDfimSLPDGYDtlvgERGSQLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNT 236
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTH 221
|
...
gi 16131593 237 DDL 239
Cdd:cd03249 222 DEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-231 |
4.76e-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: 141.80 E-value: 4.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILT-NSQDIALLR 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-----SSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVfqkptpfpmsiydniafgvrlfekLSRADMDervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:cd03214 76 AYVPQA------------------------LELLGLA-----------------HLADRPFNELSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
1.04e-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: 142.26 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK--FHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMfeLYPEQRA-EGEILLDGDNILTNSQDIa 87
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTL----KM--LTGELRPtSGTAYINGYSIRTDRKAA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfeK-LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIA 165
Cdd:cd03263 74 --RQSLGYCPQFDALFDeLTVREHLRFYARL--KgLPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-254 |
1.48e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.80 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 7 APSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNkmfelYPEQRAEGEILLDGDNI------- 79
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-----FLEKPSEGSIVVNGQTInlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 ----LTNSQDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetkDKLHQSGY-- 152
Cdd:PRK10619 77 gqlkVADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI-----DERAQGKYpv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250 260
....*....|....*....|...
gi 16131593 232 EFSNTDDLFTKPAKKQTEDYITG 254
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-232 |
1.62e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.23 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGdnILTNSQDI 86
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPEA---GTITVGG--MVLSEETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKP-TPF-PMSIYDNIAFGVrlfEK--LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRL 162
Cdd:PRK13635 77 WDVRRQVGMVFQNPdNQFvGATVQDDVAFGL---ENigVPREEMVERVDQALRQVGM----EDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPIstGRIE--ELITELK--QDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-247 |
3.00e-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: 141.27 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIlTN--SQDIAll 89
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKA---ISGLLP--PRSGSIRFDGEDI-TGlpPHRIA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVfqkptP-----FP-MSIYDNIAFGVRLfeKLSRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLC 163
Cdd:COG0410 77 RLGIGYV-----PegrriFPsLTVEENLLLGAYA--RRDRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
....*
gi 16131593 243 PAKKQ 247
Cdd:COG0410 227 PEVRE 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-221 |
1.12e-40 |
|
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: 140.01 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG-KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlTNSQDIAL- 88
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGSVLIDGTDI-NKLKGKALr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 -LRAKVGMVFQKPTPFP-MSIYDNIAFG-------VR-LFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQ 158
Cdd:cd03256 75 qLRRQIGMIFQQFNLIErLSVLENVLSGrlgrrstWRsLFGLFPKEEK-QRALAALERVGL----LDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDH 221
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
1.45e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 141.14 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNSQDIALL 89
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTP--FPMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRLCIARG 167
Cdd:PRK13636 81 RESVGMVFQDPDNqlFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-242 |
1.52e-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: 139.28 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQraEGEILLDGDNIltNSQDIA 87
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR---FYDPQ--KGQILIDGIDI--RDISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGVrlfeklSRADMDERVQWALTKAA------LWNETKDKLHQSGYSLSGGQQQR 161
Cdd:cd03254 74 SLRSMIGVVLQDTFLFSGTIMENIRLGR------PNATDEEVIEAAKEAGAhdfimkLPNGYDTVLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELLA 226
|
.
gi 16131593 242 K 242
Cdd:cd03254 227 K 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-217 |
1.77e-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: 138.92 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNF-YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT-NSQDIAL 88
Cdd:TIGR02673 2 IEFHNVSKaYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA-----LTPSRGQVRIAGEDVNRlRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPdRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAAR 217
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDR 202
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-231 |
2.38e-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: 139.79 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLlrtFNKMFELYPEQraEGEILLDGdniltnsQDIALL-- 89
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTL---FNLITGFYRPT--SGRILFDG-------RDITGLpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 --RAKVGMV--FQKPTPFP-MSIYDNIAFGV------RLFEKLSR--------ADMDERVQWALTKAALwnetKDKLHQS 150
Cdd:COG0411 74 hrIARLGIArtFQNPRLFPeLTVLENVLVAAharlgrGLLAALLRlprarreeREARERAEELLERVGL----ADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLG 228
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDFG 229
|
...
gi 16131593 229 ELI 231
Cdd:COG0411 230 RVI 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-244 |
3.09e-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: 141.48 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 42 IGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnSQDIALLRAkVGMVFQKPTPFP-MSIYDNIAFGVRLfEK 120
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGF-----EQPDSGSIMLDGEDV---TNVPPHLRH-INMVFQSYALFPhMTVEENVAFGLKM-RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 121 LSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIE-ELITEL 199
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131593 200 KQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:TIGR01187 148 EQlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-215 |
1.16e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.07 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKF----HALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKM--FeLYPEqraEGEILLDGDNILTN 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIagF-LAPS---SGEITLDGVPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 SQDiallRakvGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 161
Cdd:COG4525 75 GAD----R---GVVFQKDALLPwLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQA 215
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-244 |
1.43e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 140.24 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNS---QDIA 87
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDVTHRSiqqRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 llrakvgMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetkdklhqSGYS------LSGGQQQ 160
Cdd:PRK11432 82 -------MVFQSYALFPhMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDL----------AGFEdryvdqISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....*.
gi 16131593 239 LFTKPA 244
Cdd:PRK11432 224 LYRQPA 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-257 |
1.47e-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: 137.43 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIL-TNSQDIAL 88
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-----SSGSILLEGTDITkLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFP-MSIYDNIAFGvRL---------FEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQ 158
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVLHG-RLgykptwrslLGRFSEEDK-ERALSALERVGL----ADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIefsnt 236
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIV----- 225
|
250 260
....*....|....*....|.
gi 16131593 237 ddlFTKPAKKQTEDYITGRYG 257
Cdd:TIGR02315 226 ---FDGAPSELDDEVLRHIYG 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-245 |
5.96e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.07 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLdGDNILTNS---QDIALLRAKVGMVFQKPT 101
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL-----QPTSGTVTI-GERVITAGkknKKLKPLRKKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 102 P--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13634 96 HqlFEETVEKDICFGPMNF-GVSEEDAKQKAREMIELVGL---PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 180 PCSALDPisTGRIE--ELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAK 245
Cdd:PRK13634 172 PTAGLDP--KGRKEmmEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-243 |
7.64e-39 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 141.75 E-value: 7.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 5 ETAPSKIQVRNLNFYY-----------GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypeQRAEGEIL 73
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 74 LDGDNILT-NSQDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFE-KLSRADMDERVQWALTKAALWNETKDK 146
Cdd:COG4172 344 FDGQDLDGlSRRALRPLRRRMQVVFQDP--FgslsPrMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 147 L-HQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTA 223
Cdd:COG4172 422 YpHE----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRALAHRVM 497
|
250 260
....*....|....*....|
gi 16131593 224 FMYLGELIEFSNTDDLFTKP 243
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-243 |
1.49e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.59 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNSQDIALL 89
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK--PT---SGEVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTP--FPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARG 167
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-220 |
2.46e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.86 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRaeGEILLDGDNIltNSQDIALL 89
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG---IYLPQR--GRVKVMGREV--NAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTP--FPMSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK13647 78 RSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSD 220
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWAD 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-244 |
8.44e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.60 E-value: 8.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGdniltnsQDIALLR 90
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQTSGHIRFHG-------TDVSRLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AK---VGMVFQKPTPFP-MSIYDNIAFGVRLF---EKLSRADMDERVQWALTKAALwnetkDKLHQSGYS-LSGGQQQRL 162
Cdd:PRK10851 71 ARdrkVGFVFQHYALFRhMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEMVQL-----AHLADRYPAqLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDpiSTGRIE------ELITELKqdYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
....*...
gi 16131593 237 DDLFTKPA 244
Cdd:PRK10851 222 DQVWREPA 229
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-244 |
1.33e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 135.62 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNILTNSQD--IALLRAKVGMVFQKPTP 102
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE--P---TAGEVLIDGEDITKLSKKelRELRRKKMSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 FP-MSIYDNIAFG--VRlfeKLSRADMDERVQWALTKAAL--WnetKDKL-HQsgysLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:COG4175 117 LPhRTVLENVAFGleIQ---GVPKAERRERAREALELVGLagW---EDSYpDE----LSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 177 LDEPCSALDPIstgrI-----EELIT---ELKQdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG4175 187 MDEAFSALDPL----IrremqDELLElqaKLKK--TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPA 256
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-239 |
1.39e-37 |
|
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: 131.34 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNSQDIallR 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTS---GRATVAGHDVVREPREV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIARGIA 169
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLY-GVPGAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELK--QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-210 |
2.81e-37 |
|
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: 131.20 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK--FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltnsQDIAL 88
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDV----RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 --LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsRADMDERVQWAltKAALWNETKDKLHQsGY---------SLSGG 157
Cdd:cd03251 72 asLRRQIGLVSQDVFLFNDTVAENIAYGRP------GATREEVEEAA--RAANAHEFIMELPE-GYdtvigergvKLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 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 |
7.16e-37 |
|
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: 128.69 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 19 YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNSQDIALLRAKVGMVFQ 98
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQS---GAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 99 KPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHC----LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131593 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 |
2.17e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.81 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK----FHALKNINLDIAKNQVTAFIGPSGCGKS----TLLRtfnkmfeLYPEQ--RAEGEILLDGDNIL 80
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-------LLPDPaaHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 81 TNSQdiALLRA----KVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL----H 148
Cdd:COG4172 80 GLSE--RELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRLdaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 149 QsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMY 226
Cdd:COG4172 156 Q----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*...
gi 16131593 227 LGELIEFSNTDDLFTKPA 244
Cdd:COG4172 232 QGEIVEQGPTAELFAAPQ 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-231 |
4.46e-36 |
|
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: 127.41 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKN---QVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNSQDIAL--LRAKVGMVFQKP 100
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGLEKPD-----GGTIVLNGTVLFDSRKKINLppQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 TPFP-MSIYDNIAFGVRlfeKLSRADMDERVQWALTKAALwnetkDKLHQSG-YSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:cd03297 85 ALFPhLNVRENLAFGLK---RKRNREDRISVDELLDLLGL-----DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 179 EPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-212 |
4.79e-36 |
|
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: 127.32 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltnSQ-DI 86
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKL---LAGLYKPT--SGSVLLDGTDI---RQlDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeklsrADmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQ 159
Cdd:cd03245 74 ADLRRNIGYVPQDVTLFYGTLRDNITLGAPL------AD-DERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-241 |
7.51e-36 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 127.82 E-value: 7.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNS----- 83
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQS---GTVFLGDKPISMLSsrqla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDIALLRAkvgmvfQKPTPFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALwNETKDKLHQsgySLSGGQQ 159
Cdd:PRK11231 76 RRLALLPQ------HHLTPEGITVRELVAYGrspwLSLWGRLSAED-NARVNQAMEQTRI-NHLADRRLT---DLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
...
gi 16131593 239 LFT 241
Cdd:PRK11231 225 VMT 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-222 |
3.09e-35 |
|
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: 131.64 E-value: 3.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 4 VETAPSKIQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGdnILTN 82
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNG--VPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 SQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWNETKD-------KLHQSGYSL 154
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIRLA--------RPDAsDAEIREALERAGLDEFVAAlpqgldtPIGEGGAGL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHT 222
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRI 526
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
10-213 |
3.13e-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: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNF-YYG-KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltnSQ-DI 86
Cdd:TIGR03375 463 EIEFRNVSFaYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKL---LLGLYQPT--EGSVLLDGVDI---RQiDP 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEklsradmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQ 159
Cdd:TIGR03375 535 ADLRRNIGYVPQDPRLFYGTLRDNIALGAPYAD-------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQR 607
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQ 213
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-218 |
7.60e-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: 7.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 13 VRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNSQDIALLR 90
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLL-----EKFDSGQVYLNGQETppLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKptpFPM----SIYDNIAFGVrLFEKLSRADMDERVQWALTKAALWNetkdKLHQSGYSLSGGQQQRLCIAR 166
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGL-KYKKLSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 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 ... |
11-211 |
9.55e-35 |
|
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: 124.06 E-value: 9.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNSQdIA 87
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVsdLRGRA-IP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKlSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPdRNVYENVAFALEVTGV-PPREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHN 211
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-215 |
1.05e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.84 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnsQDIAL 88
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLFIGEKRM----NDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWA---LTKAALWnETKDKlhqsgySLSGGQQQRLCI 164
Cdd:PRK11000 73 AERGVGMVFQSYALYPhLSVAENMSFGLKL-AGAKKEEINQRVNQVaevLQLAHLL-DRKPK------ALSGGQRQRVAI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPI--STGRIEelITELKQDY--TVVIVTHNMQQA 215
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAAlrVQMRIE--ISRLHKRLgrTMIYVTHDQVEA 197
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-247 |
1.18e-34 |
|
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: 124.31 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELYPeqRAEGEILLDGdniltnsQDIALL- 89
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDG-------QDITHLp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 ---RAKVGMVF--QKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:TIGR04406 70 mheRARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:TIGR04406 146 IARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
....*
gi 16131593 243 PAKKQ 247
Cdd:TIGR04406 226 EKVRR 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-242 |
1.41e-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: 124.14 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG--KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelYPEQraeGEILLDGDNILTnsQDIAL 88
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY--VPEN---GRVLVDGHDLAL--ADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIAfgvrlfekLSRADMD-ERVQWAlTKAALWNETKDKLH--------QSGYSLSGGQQ 159
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIA--------LADPGMSmERVIEA-AKLAGAHDFISELPegydtivgEQGAGLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
...
gi 16131593 240 FTK 242
Cdd:cd03252 224 LAE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-239 |
1.62e-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: 125.58 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 19 YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNSqdiALLRAKVGMVFQ 98
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDVVREP---RKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 99 KPTPFP-MSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:TIGR01188 74 YASVDEdLTGRENLEMMGRLYG-LPKDEAEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 178 DEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-225 |
1.73e-34 |
|
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: 123.14 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNF-YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltnsqDIALLR 90
Cdd:cd03226 1 RIENISFsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL-----IKESSGSILLNGKPI-----KAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTP--FPMSIYDNIAFGVRLFeklsrADMDERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIARGI 168
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKEL-----DAGNEQAETVLKDLDLY-ALKERHPLS---LSGGQKQRLAIAAAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-216 |
3.18e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.59 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMF-ELYPEQRAEGEILLDGdniltnsQDIALLR 90
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL---AAIAgTLSPAFSASGEVLLNG-------RRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 A---KVGMVFQKPTPFP-MSIYDNIAFGVRlfEKLSRADMDERVQWALTKAALwnetkdklhqSGY------SLSGGQQQ 160
Cdd:COG4136 73 AeqrRIGILFQDDLLFPhLSVGENLAFALP--PTIGRAQRRARVEQALEEAGL----------AGFadrdpaTLSGGQRA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI-TELKQ-DYTVVIVTHNMQQAA 216
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQrGIPALLVTHDEEDAP 198
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
12-239 |
5.16e-34 |
|
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: 122.63 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNILTNSQDiALLRA 91
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKT---LMGLLPVKS--GSIRLDGEDITKLPPH-ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVFQKPTPFP-MSIYDNIAFGvrlFEKLSRAD--MDERVqwaltkAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:TIGR03410 76 GIAYVPQGREIFPrLTVEENLLTG---LAALPRRSrkIPDEI------YELFPVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-232 |
6.94e-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: 122.19 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDIALlrakvgmVFQKPTPFP- 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGKQITEPGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 MSIYDNIAFGV-RLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 184 LDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFM------YLGELIE 232
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-212 |
1.41e-33 |
|
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: 121.57 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNF-YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNILTNSQDIalL 89
Cdd:cd03253 1 IEFENVTFaYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL---LFRFYDVS--SGSILIDGQDIREVTLDS--L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFPMSIYDNIAFG------VRLFEKLSRADMDERVQwaltkaALWNETKDKLHQSGYSLSGGQQQRLC 163
Cdd:cd03253 74 RRAIGVVPQDTVLFNDTIGYNIRYGrpdatdEEVIEAAKAAQIHDKIM------RFPDGYDTIVGERGLKLSGGEKQRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-210 |
1.45e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 127.44 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 4 VETAPSKIQVRNLNFYY-GKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIlt 81
Cdd:PRK11176 335 IERAKGDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 nsQDIAL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERvqwalTKAALWNETKDKLHQ--------SG 151
Cdd:PRK11176 408 --RDYTLasLRNQVALVSQNVHLFNDTIANNIAYART--EQYSREQIEEA-----ARMAYAMDFINKMDNgldtvigeNG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 152 YSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-221 |
1.46e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNILTNS-QDIALL 89
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG--QIAPDH---GEILFDGENIPAMSrSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETkdKLHQSgySLSGGQQQRLCIARGI 168
Cdd:PRK11831 83 RKRMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA--KLMPS--ELSGGMARRAALARAI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDH 221
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADH 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-210 |
1.61e-33 |
|
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: 120.76 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAkNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNSQDIallR 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTP--PS---SGTIRIDGQDVLKQPQKL---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGIA 169
Cdd:cd03264 72 RRIGYLPQEFGVYPnFTVREFLDYIAWL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-241 |
2.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH--ALKNINLDIAKNQVTAFIGPSGCGKSTllrtFNKMFE-LYPEQraEGEILLDGdnILTNSQDIA 87
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKST----ISKILTgLLKPQ--SGEIKIDG--ITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIA 165
Cdd:PRK13632 80 EIRKKIGIIFQNPdNQFiGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILA-DKVIVFSEGKLIAQGKPKEILN 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-243 |
2.48e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.25 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG-----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNSQD 85
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKP---SSGTITIAGYHITPETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IAL--LRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFEKLSRADMDERVQWaLTKAALWNETKDKlhqSGYSLSGGQQQR 161
Cdd:PRK13641 78 KNLkkLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
...
gi 16131593 241 TKP 243
Cdd:PRK13641 234 SDK 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-232 |
5.85e-33 |
|
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: 119.24 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEqrAEGEILLDGDNILTNSQDiallR 90
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIKP--DSGEITFDGKSYQKNIEA----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLsradmDERVQWALTKAALWNETKDKLhqSGYSLsgGQQQRLCIARGIA 169
Cdd:cd03268 72 RRIGALIEAPGFYPnLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKV--KGFSL--GMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-232 |
7.62e-33 |
|
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: 119.46 E-value: 7.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 3 MVETAPSKIQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLDGDN 78
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGL---LAGL--DRPTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 79 ILTNSQD-IALLRA-KVGMVFQK----PTpfpMSIYDNIAfgVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGY 152
Cdd:COG4181 76 LFALDEDaRARLRArHVGFVFQSfqllPT---LTALENVM--LPL-ELAGRRDARARARALLERVGL----GHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPiSTG-RIEELITELKQDY--TVVIVTHNMQQAARCsDHTAFMYLGE 229
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDA-ATGeQIIDLLFELNRERgtTLVLVTHDPALAARC-DRVLRLRAGR 223
|
...
gi 16131593 230 LIE 232
Cdd:COG4181 224 LVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-240 |
7.65e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.97 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK---FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNSQDIA 87
Cdd:PRK13642 5 LEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELL--TAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTP--FPMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWN-ETKDKLHqsgysLSGGQQQRLCI 164
Cdd:PRK13642 78 NLRRKIGMVFQNPDNqfVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDfKTREPAR-----LSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-230 |
8.48e-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: 8.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGK---FHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNIltNSQDI 86
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV---ALLENFYQPQ--GGQVLLDGKPI--SQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQWALTKAA----------LWNETKDKlhqsGYSLSG 156
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARSLQDNIAYG------LQSCSFECVKEAAQKAHAhsfiselasgYDTEVGEK----GSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGEL 230
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
10-251 |
9.99e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGK-----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNSQ 84
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKP---TTGTVTVDDITITHKTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 D--IALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeklsRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ 160
Cdd:PRK13646 77 DkyIRPVRKRIGMVFQFPESqlFEDTVEREIIFGPKNF----KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
250
....*....|...
gi 16131593 239 LFTKpaKKQTEDY 251
Cdd:PRK13646 233 LFKD--KKKLADW 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
1.10e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.60 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNIltnSQDIallR 90
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI--LAPD---SGEVLWDGEPL---DPED---R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVG-M-----VFQKptpfpMSIYDNIAFGVRLfeK-LSRADMDERVQWALTK---AALWNetkDKLHqsgySLSGGQQQ 160
Cdd:COG4152 71 RRIGyLpeergLYPK-----MKVGEQLVYLARL--KgLSKAEAKRRADEWLERlglGDRAN---KKVE----ELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-240 |
1.80e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 119.85 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTNS--QDIALLRAKVGMVFQKPTP 102
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVP---TQGSVRVDDTLITSTSknKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 --FPMSIYDNIAFGVRLFEklsrADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFG----VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 181 CSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-254 |
1.96e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 122.45 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNI--LTNSQDIALLRAKVGMVFQKPTP 102
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 FP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNetkdklHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK10070 118 MPhMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLEN------YAHSYpdELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 180 PCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITG 254
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-231 |
2.56e-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: 115.99 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNILTNSQDIAlLR 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKI---LSGLY--KPDSGEILVDGKEVSFASPRDA-RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 170
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-211 |
5.12e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELypEQRAEGEILLDGdniltnsQDIA 87
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGRIFLDG-------EDIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LL----RAKVGM--------VFQKptpfpMSIYDNIAfGVRLFEKLSRADMDERVQwaltkaALWNETK-DKL-HQSGYS 153
Cdd:COG1137 69 HLpmhkRARLGIgylpqeasIFRK-----LTVEDNIL-AVLELRKLSKKEREERLE------ELLEEFGiTHLrKSKAYS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHN 211
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHN 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-232 |
5.52e-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: 122.90 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 5 ETAPSKIQVRNLNFYYG--KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIltn 82
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDL--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 sQDIAL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERVQWALTKAaLWNETKDKLH----QSGYSLSG 156
Cdd:TIGR02203 397 -ADYTLasLRRQVALVSQDVVLFNDTIANNIAYGRT--EQADRAEIERALAAAYAQD-FVDKLPLGLDtpigENGVLLSG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVE 547
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-248 |
1.06e-31 |
|
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: 116.49 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELypEQRAEGEILLDGdniltnsQDIALL- 89
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGKILLDG-------QDITKLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 ---RAKVGMVF--QKPTPF-PMSIYDNIAfGVRLFEKLSRADMDERVQwaltkaALWNETK-DKL-HQSGYSLSGGQQQR 161
Cdd:cd03218 69 mhkRARLGIGYlpQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLE------ELLEEFHiTHLrKSKASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
....*...
gi 16131593 241 TKPAKKQT 248
Cdd:cd03218 222 ANELVRKV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
1.09e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.54 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDgdNILTNSQDIAL 88
Cdd:PRK13648 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYN--NQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKP-TPFPMSI--YDnIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIA 165
Cdd:PRK13648 81 LRKHIGIVFQNPdNQFVGSIvkYD-VAFGLENH-AVPYDEMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVI--VTHNMQQAARcSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
11-243 |
1.14e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.60 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNIltNSQDIALL 89
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKP---TSGSVLIRGEPI--TKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTP--FPMSIYDNIAFG-VRLfeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGpINL--GLDEETVAHRVSSALHMLGL----EELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-218 |
3.18e-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: 113.47 E-value: 3.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHA--LKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNIltNSQDIAL 88
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLRPT--SGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 168
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARC 218
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASA 162
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-242 |
3.74e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.37 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK---FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAE-GEILLDGDnILT--NSQ 84
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE------AEsGQIIIDGD-LLTeeNVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIallRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRL 162
Cdd:PRK13650 78 DI---RHKIGMVFQNPdNQFvGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGM-QDFKER---EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPisTGRIE--ELITELKQDY--TVVIVTHNMQQAArCSDHTAFMYLGELIEFSNTDD 238
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
....
gi 16131593 239 LFTK 242
Cdd:PRK13650 227 LFSR 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-210 |
4.57e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 114.11 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNIltnSQDIALLR 90
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRI---LAGLLP--PSAGEVLWNGEPI---RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLF-EKLSRADMDErvqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:COG4133 75 RRLAYLGHADGLKPeLTVRENLRFWAALYgLRADREAIDE----ALEAVGL----AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-231 |
1.51e-30 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 114.31 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 3 MVETaPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILT- 81
Cdd:PRK10253 1 MTES-VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIQHy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 NSQDIAllrAKVGMVFQKP-TPFPMSIYDNIAFGVR----LFEKLSRADMDervqwALTKAALWNETKDKLHQSGYSLSG 156
Cdd:PRK10253 75 ASKEVA---RRIGLLAQNAtTPGDITVQELVARGRYphqpLFTRWRKEDEE-----AVTKAMQATGITHLADQSVDTLSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-244 |
1.69e-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: 116.35 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 28 NINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLDGDNILTNSQDIALLRAK--VGMVFQKPTPFP- 104
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRA---IAGL--ERPDSGRIRLGGEVLQDSARGIFLPPHRrrIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 MSIYDNIAFGV-RLFEKLSRADMDERVQWaLTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:COG4148 92 LSVRGNLLYGRkRAPRAERRISFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 184 LDpisTGRIEELITELKQ-----DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:COG4148 164 LD---LARKAEILPYLERlrdelDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
10-185 |
2.01e-30 |
|
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: 119.29 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGK--FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNILtnSQDIA 87
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDLA--GLDVQ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeklsraDMDErVQWALTKAALWNETKD---KLH----QSGYSLSGGQQQ 160
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPL-------TLDE-AWEAARMAGLAEDIRAmpmGMHtvisEGGGTLSGGQRQ 595
|
170 180
....*....|....*....|....*
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALD 620
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-230 |
2.04e-30 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 112.89 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 22 KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNkMFElypeQRAEGEILLDGDNI--LTNSQDIALLRAKVGMVFQK 99
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFD----SLDSGSLTLAGKEVtnLSYSQKIILRRELIGYIFQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 PTPFP-MSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:NF038007 92 FNLIPhLSIFDNVALPLK-YRGVAKKERIERVNQVLNLFGIDNRRNHKPMQ----LSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 179 EPCSALDPISTGRIEELITEL-KQDYTVVIVTHNmQQAARCSDHTAFMYLGEL 230
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-247 |
3.18e-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: 113.75 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYY---------GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNI 79
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 --LTNSQDIALLRaKVGMVFQK-PTPF--PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSgysL 154
Cdd:TIGR02769 76 yqLDRKQRRAFRR-DVQLVFQDsPSAVnpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
250
....*....|....*..
gi 16131593 233 FSNTDDLFT--KPAKKQ 247
Cdd:TIGR02769 232 ECDVAQLLSfkHPAGRN 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-243 |
3.61e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 114.68 E-value: 3.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKF------HALKNINLDIAKNQVTAFIGPSGCGKSTLLRtfnkMFELYpEQRAEGEILLDGDNIL 80
Cdd:PRK11308 6 LQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLAR----LLTMI-ETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 81 TNS-QDIALLRAKVGMVFQKPTPfpmSIYDNIAFGVRLFE------KLSRADMDERVQWALTKAALWNEtkdklHQSGYS 153
Cdd:PRK11308 81 KADpEAQKLLRQKIQIVFQNPYG---SLNPRKKVGQILEEpllintSLSAAERREKALAMMAKVGLRPE-----HYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 154 --LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:PRK11308 153 hmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGR 232
|
250
....*....|....
gi 16131593 230 LIEFSNTDDLFTKP 243
Cdd:PRK11308 233 CVEKGTKEQIFNNP 246
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-231 |
3.69e-30 |
|
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: 112.08 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNILTNSQDI 86
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE--PDA---GFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 allRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIA 165
Cdd:cd03266 77 ---RRRLGFVSDSTGLYDrLTARENLEYFAGLY-GLKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-243 |
4.83e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQRAEGEILLDGDNIltNSQDIAL 88
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITL--TAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIAR 166
Cdd:PRK13640 82 IREKVGIVFQNPdNQFvGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPA----NLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-242 |
6.38e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.29 E-value: 6.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLdGDNILTNS---QDIALLRAKVGMVFQKPT 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL-----QPTEGKVTV-GDIVVSSTskqKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 102 P--FPMSIYDNIAFGVRLFeKLSRadmDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNF-GIPK---EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 180 PCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-210 |
1.62e-29 |
|
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: 110.28 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltnsQDIA 87
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDI----SKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 L--LRAKVGMVFQKPTPFPMSIYDNIAFgvrlFEKLSradmDERVQWALTKAALWNETK-------DKLHQSGYSLSGGQ 158
Cdd:cd03244 73 LhdLRSRISIIPQDPVLFSGTIRSNLDP----FGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI-TELKqDYTVVIVTH 210
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIrEAFK-DCTVLTIAH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-225 |
1.75e-29 |
|
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: 109.87 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELypeQRAEGEILLDGdniltnsqd 85
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEL---EKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 iallraKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsrADMD-ERVQWALTKAALwneTKD----------KLHQSGYSL 154
Cdd:cd03250 67 ------SIAYVSQEPWIQNGTIRENILFG---------KPFDeERYEKVIKACAL---EPDleilpdgdltEIGEKGINL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPiSTGR--IEELIT-ELKQDYTVVIVTHNMQQAARCsDHTAFM 225
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDA-HVGRhiFENCILgLLLNNKTRILVTHQLQLLPHA-DQIVVL 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-244 |
3.36e-29 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 112.63 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNL-NFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRtfnkMFE-LypEQRAEGEILLDG---DNILTN 82
Cdd:PRK11650 1 MAGLKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR----MVAgL--ERITSGEIWIGGrvvNELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 SQDIAllrakvgMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQwaltKAALWNETKDKLHQSGYSLSGGQQQR 161
Cdd:PRK11650 75 DRDIA-------MVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIEERVA----EAARILELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDP---ISTgRIE--ELITELKQdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAklrVQM-RLEiqRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
....*...
gi 16131593 237 DDLFTKPA 244
Cdd:PRK11650 220 VEVYEKPA 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-247 |
4.05e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.06 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGDNILTNSqdIALL 89
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--P---QSGRILIDGTDIRTVT--RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRAD-MDERVQWALTKAALWN--ETKDKLHQS-----GYSLSGGQQQR 161
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVG--------RPDaTDEEMRAAAERAQAHDfiERKPDGYDTvvgerGRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDL-- 239
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDELva 558
|
250
....*....|..
gi 16131593 240 ----FTKPAKKQ 247
Cdd:PRK13657 559 rggrFAALLRAQ 570
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-231 |
5.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.56 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-----GKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNIlTNSQ 84
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDT-SDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfEKLSRA--DMDERVQWALTKAALWNETKDKLHQsgy 152
Cdd:PRK13633 79 NLWDIRNKAGMVFQNP--------DNqivativeedVAFGP---ENLGIPpeEIRERVDESLKKVGMYEYRRHAPHL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 153 sLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIstGRIEEL--ITELKQDY--TVVIVTHNMQQAARcSDHTAFMYLG 228
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS--GRREVVntIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSG 220
|
...
gi 16131593 229 ELI 231
Cdd:PRK13633 221 KVV 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-244 |
5.16e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.48 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG-----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEI----LLDGDNILT 81
Cdd:PRK13631 22 LRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI-----KSKYGTIqvgdIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 NSQDIAL----------LRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLfeKLSRADMDERVQWALTKAALwneTKDKLH 148
Cdd:PRK13631 97 HELITNPyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGpVAL--GVKKSEAKKLAKFYLNKMGL---DDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 149 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYL 227
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDK 251
|
250
....*....|....*..
gi 16131593 228 GELIEFSNTDDLFTKPA 244
Cdd:PRK13631 252 GKILKTGTPYEIFTDQH 268
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-243 |
7.35e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 114.82 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY---GKFHALKNINLDIAKNQVTAFIGPSGCGKST---LLRTFnkmfelYpeQRAEGEILLDGDNIltnS 83
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNL------Y--QPTGGQVLLDGVPL---V 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 Q-DIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQWALTKAA------LWNETKDKLHQSGYSLSG 156
Cdd:TIGR00958 547 QyDHHYLHRQVALVGQEPVLFSGSVRENIAYG------LTDTPDEEIMAAAKAANAhdfimeFPNGYDTEVGEKGSQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDpistGRIEELITELK--QDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFS 234
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMG 695
|
....*....
gi 16131593 235 NTDDLFTKP 243
Cdd:TIGR00958 696 THKQLMEDQ 704
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-215 |
8.13e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNILTNSqdiallr 90
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVPYQ--HGSITLDGKPVEGPG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:PRK11248 70 AERGVVFQNEGLLPwRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQA 215
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-231 |
8.74e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNIL-TNSQDIALL 89
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSPDS---GEVRLNGRPLAdWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAkvgMVFQKPT-PFPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWnETKDKLHQsgySLSGGQQQRLCIARGI 168
Cdd:PRK13548 78 RA---VLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYP---QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 169 A------IRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-232 |
1.03e-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: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYG--KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDGDNILTNSqdiAL 88
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQQ---GEITLDGVPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsGYSLSGGQQQRLCIARGI 168
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIE 232
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-241 |
1.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDniLTNSQD 85
Cdd:PRK13645 7 IILDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN--LKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLFEklSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRL 162
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGE--NKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLF 240
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
.
gi 16131593 241 T 241
Cdd:PRK13645 240 S 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-211 |
1.10e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 113.61 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY-GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNILTNSQDiaLL 89
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT---LAGLLDPLQ--GEVTLDGVPVSSLDQD--EV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWN---ETKD----KLHQSGYSLSGGQQQR 161
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLRLA--------RPDAtDEELWAALERVGLADwlrALPDgldtVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHN 211
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-244 |
1.73e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.97 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 24 HALKnINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNILTNSQDIALL--RAKVGMVFQKPT 101
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGRTLFDSRKGIFLPpeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 102 PFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:TIGR02142 86 LFPhLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 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 ... |
1-239 |
2.52e-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: 113.30 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPSKIQVRNLNFYYG-KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNI 79
Cdd:TIGR01193 464 RTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF-----QARSGEILLNGFSL 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 ltNSQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERVQWALTKAALWNET---KDKLHQSGYSLSG 156
Cdd:TIGR01193 539 --KDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIENMPlgyQTELSEEGSSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELkQDYTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNT 236
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSH 692
|
...
gi 16131593 237 DDL 239
Cdd:TIGR01193 693 DEL 695
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-242 |
4.06e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.23 E-value: 4.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEQraeGEILLDGDNILTNSQdiAL 88
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQ---GEILLNGQPIADYSE--AA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAALWNETKDK------LHQSGYSLSGGQQQRL 162
Cdd:PRK11160 412 LRQAISVVSQRVHLFSATLRDNLLLA------APNAS-DEALIEVLQQVGLEKLLEDDkglnawLGEGGRQLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-225 |
4.17e-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: 106.42 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGkfHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmFELypeqRAEGEILLDGdniltnsQDIALL- 89
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAG-FET----PQSGRVLING-------VDVTAAp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 --RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLsRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:cd03298 67 paDRPVSMLFQENNLFAhLTVEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFM 225
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-220 |
4.73e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.46 E-value: 4.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 13 VRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEiLLDGDNILTNSQDiallraK 92
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-----ETPSAGE-LLAGTAPLAEARE------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 93 VGMVFQKPTPFP-MSIYDNIAFGVRlfeklsrADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIR 171
Cdd:PRK11247 83 TRLMFQDARLLPwKKVIDNVGLGLK-------GQWRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 172 PEVLLLDEPCSALDPIStgRIE--ELITELKQDY--TVVIVTHNMQQAARCSD 220
Cdd:PRK11247 152 PGLLLLDEPLGALDALT--RIEmqDLIESLWQQHgfTVLLVTHDVSEAVAMAD 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-243 |
1.15e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.10 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNL-----------NFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNI 79
Cdd:PRK10261 314 LQVRNLvtrfplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 80 --LTNSQdIALLRAKVGMVFQKP----TPfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklHQSGY- 152
Cdd:PRK10261 389 dtLSPGK-LQALRRDIQFIFQDPyaslDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPE-----HAWRYp 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 153 -SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:PRK10261 462 hEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQ 541
|
250
....*....|....
gi 16131593 230 LIEFSNTDDLFTKP 243
Cdd:PRK10261 542 IVEIGPRRAVFENP 555
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-231 |
1.97e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 104.67 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTNSQD-IALL 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGKPLDIAARNrIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMvFQKptpfpMSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 169
Cdd:cd03269 76 PEERGL-YPK-----MKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-221 |
2.78e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNI-LTNSQDiAlL 89
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKI---LSGVY--QPDSGEILLDGEPVrFRSPRD-A-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGvrlFEKLSRADMDERVQWALTKAALwnetkDKLHQS-------GySLSGGQQQR 161
Cdd:COG1129 78 AAGIAIIHQELNLVPnLSVAENIFLG---REPRRGGLIDWRAMRRRARELL-----ARLGLDidpdtpvG-DLSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDH 221
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADR 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-241 |
3.12e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 105.17 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRtfnkmfelypeqraegeiLLDGDNILTNSQDIAL-- 88
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS------------------LITGDLPPTYGNDVRLfg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 ----------LRAKVGMV---FQKPTPFPMSIYDNI---AFG-VRLFEKLSRADMDERVQWAltkaALWnETKDKLHQSG 151
Cdd:COG1119 66 errggedvweLRKRIGLVspaLQLRFPRDETVLDVVlsgFFDsIGLYREPTDEQRERARELL----ELL-GLAHLADRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 152 YSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250
....*....|..
gi 16131593 230 LIEFSNTDDLFT 241
Cdd:COG1119 221 VVAAGPKEEVLT 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-245 |
3.38e-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: 104.40 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNIltNSQDIAllr 90
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-----RPTSGEIIFDGHPW--TRKDLH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 aKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSradmDERVQWALTKAALWNETKDKLHQsgYSLsgGQQQRLCIARGIA 169
Cdd:TIGR03740 71 -KIGSLIESPPLYEnLTARENLKV-HTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQ--FSL--GMKQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 IRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI------EFSNTDDLFTK 242
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLGyqgkinKSENLEKLFVE 220
|
...
gi 16131593 243 PAK 245
Cdd:TIGR03740 221 VVK 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
8.60e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 8.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLN--FYYG---KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIlTNSQD 85
Cdd:COG1101 2 LELKNLSktFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP-----DSGSILIDGKDV-TKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IAllRAK-VGMVFQKP---TPFPMSIYDNIA--------FGVRLfeKLSRADMD---ERVqwaltkAALWNETKDKLHQS 150
Cdd:COG1101 76 YK--RAKyIGRVFQDPmmgTAPSMTIEENLAlayrrgkrRGLRR--GLTKKRRElfrELL------ATLGLGLENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLG 228
Cdd:COG1101 146 VGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
...
gi 16131593 229 ELI 231
Cdd:COG1101 226 RII 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
10-233 |
1.07e-26 |
|
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: 102.88 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGKF--HALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltNSQDIA 87
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDI--STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFPMSIYDNiafgVRLFEKLSradmDERVQWALtkaalwnetkdKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSN----LDPFDEYS----DEEIYGAL-----------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEF 233
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-242 |
1.33e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.32 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 15 NLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNSQDIALLRAKVG 94
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQK---GAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 95 MVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRP 172
Cdd:PRK13638 81 TVFQDPEQqiFYTDIDSDIAFSLRNL-GVPEAEITRRVDEALTLV----DAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 173 EVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-220 |
1.71e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNILTNSQDIalLR 90
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS--PT---SGTLLFEGEDISTLKPEI--YR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKlsRADMDeRVQWALTKAALWNETkdkLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQ--QPDPA-IFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVI--VTHNMQQAARCSD 220
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADK 206
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-220 |
1.79e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNIlTNSQDIALL 89
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT------LCGDPRAtSGRIVFDGKDI-TDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEklsRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAE---RDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSD 220
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLAD 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-243 |
2.51e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.85 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNIL-TNSQDIA-- 87
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL---SMISRLLPPD--SGEVLVDGLDVAtTPSRELAkr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 --LLRakvgmvfQKPTpFPM--SIYDNIAFGvRlF----EKLSRADmDERVQWALTKAALwNETKDK-LHQsgysLSGGQ 158
Cdd:COG4604 77 laILR-------QENH-INSrlTVRELVAFG-R-FpyskGRLTAED-REIIDEAIAYLDL-EDLADRyLDE----LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
....*..
gi 16131593 237 DDLFTKP 243
Cdd:COG4604 221 EEIITPE 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-238 |
3.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGK-----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQrAEGEILLDGDNILTNSQ 84
Cdd:PRK13651 2 QIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPDT-GTIEWIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIAL--------------------LRAKVGMVFQ--KPTPFPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwne 142
Cdd:PRK13651 79 EKEKvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 143 TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKR 234
|
250
....*....|....*..
gi 16131593 222 TAFMYLGELIEFSNTDD 238
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYD 251
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-243 |
7.12e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.73 E-value: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDNILT-NSQDIALL 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTP---SSGEVRLNGRPLAAwSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAkvgmVFQKPTP--FPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIAR- 166
Cdd:COG4559 77 RA----VLPQHSSlaFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLA----HLAGRSYQTLSGGEQQRVQLARv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 ------GIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:COG4559 148 laqlwePVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
....
gi 16131593 240 FTKP 243
Cdd:COG4559 228 LTDE 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-221 |
2.00e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.45 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLlrtFNKMFELYpeQRAEGEILLDGDNI--LTnSQDIAl 88
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLTGFY--KPTGGTILLRGQHIegLP-GHQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 lraKVGMV--FQKPTPF-PMSIYDNI------AFGVRLFEKL------SRADMDervqwALTKAALWNET---KDKLHQS 150
Cdd:PRK11300 79 ---RMGVVrtFQHVRLFrEMTVIENLlvaqhqQLKTGLFSGLlktpafRRAESE-----ALDRAATWLERvglLEHANRQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 151 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDH 221
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-231 |
2.04e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 6 TAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMfeLYPEQRA-EGEILLDGDNI-LTNS 83
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLM----KI--LYGLYQPdSGEILIDGKPVrIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDiALlRAKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsradMDERVQWALTKAALWNETKDKLHQSG---------YS 153
Cdd:COG3845 75 RD-AI-ALGIGMVHQHFMLVPnLTVAENIVLG-----------LEPTKGGRLDRKAARARIRELSERYGldvdpdakvED 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistGRIEELITELK----QDYTVVIVTHNMQQAARCSDHTAFMYLGE 229
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
..
gi 16131593 230 LI 231
Cdd:COG3845 219 VV 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-236 |
3.49e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 98.78 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 30 NLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNILTnsqdIALLRAKVGMVFQKPTPFP-MSIY 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSHTG----LAPYQRPVSMLFQENNLFAhLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 109 DNIAFGVRLFEKLSrADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIS 188
Cdd:TIGR01277 89 QNIGLGLHPGLKLN-AEQQEKVVDAAQQVGI----ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131593 189 TGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:TIGR01277 164 REEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-223 |
5.14e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 20 YGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPeqrAEGEILLDGDniltnsqdiallrAKVGMVF 97
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLL----KVLAgvLRP---TSGTVRRAGG-------------ARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 98 QK---PTPFPMSIYDNIAFGV----RLFEKLSRADmDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAI 170
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGRwarrGLWRRLTRDD-RAAVDDALERVGL----ADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARcSDHTA 223
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRR-ADPCV 189
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-249 |
6.22e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 13 VRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDN---ILTNSQD 85
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLR----AKVGMVFQKPTP-----FPMSiyDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKLHQSGYSLSG 156
Cdd:PRK10261 95 AAQMRhvrgADMAMIFQEPMTslnpvFTVG--EQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250
....*....|....*
gi 16131593 235 NTDDLFTKPAKKQTE 249
Cdd:PRK10261 252 SVEQIFHAPQHPYTR 266
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
26-247 |
1.10e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGDNILT-NSQDIALLRAKVGMVFQKP---- 100
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLL-----VGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDSisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 TPfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSgysLSGGQQQRLCIARGIAIRPEVLLLDEP 180
Cdd:PRK10419 103 NP-RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 181 CSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL--FTKPAKKQ 247
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSPAGRV 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-243 |
2.14e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.40 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTNSQ-DIALLRAKVGMVFQKP--- 100
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGEVAWLGKDLLGMKDdEWRAVRSDIQMIFQDPlas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 -TPfPMSIYDNIAFGVRLFE-KLSRADMDERVQWALTKAALW-NETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:PRK15079 111 lNP-RMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLpNLINRYPHE----FSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 178 DEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-210 |
2.16e-24 |
|
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: 101.44 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQraEGEILLDGDNILTNSQdiALLRAKVGMVFQKPTPFPM 105
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARL---LFRFYDVT--SGRILIDGQDIRDVTQ--ASLRAAIGIVPQDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGvrlfeklsRADMDERVQWALTKAAlwnetkdKLHQ------SGYS---------LSGGQQQRLCIARGIAI 170
Cdd:COG5265 447 TIAYNIAYG--------RPDASEEEVEAAARAA-------QIHDfieslpDGYDtrvgerglkLSGGEKQRVAIARTLLK 511
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131593 171 RPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-218 |
3.03e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 7 APSKIQVRNLNFYYG----KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILT- 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-----DDGSSGEVSLVGQPLHQm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 NSQDIALLRAK-VGMVFQK----PTpfpMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSG 156
Cdd:PRK10584 78 DEEARAKLRAKhVGFVFQSfmliPT---LNALENVELPA-LLRGESSRQSRNGAKALLEQLGL----GKRLDHLPAQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARC 218
Cdd:PRK10584 150 GEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARC 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-244 |
4.42e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPSKIQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTllRTFNKMFELYPEQRAEGEILLDG 76
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQ--TAFALMGLLAANGRIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 77 DNILT-NSQDIALLRA-KVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRAD-MDERVQwaLTKAALWNETKDKLHQ 149
Cdd:PRK09473 81 REILNlPEKELNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKAEaFEESVR--MLDAVKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 150 SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYL 227
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYA 237
|
250
....*....|....*..
gi 16131593 228 GELIEFSNTDDLFTKPA 244
Cdd:PRK09473 238 GRTMEYGNARDVFYQPS 254
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-210 |
4.93e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLDGDNILTNSQdiAL 88
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLA---SLLMGYYPLT--EGEIRLDGRPLSSLSH--SV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMVFQKPTPFPMSIYDNIAFGVRLFE-KLSRADmdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANVTLGRDISEeQVWQAL--ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-217 |
5.18e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.10 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 19 YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNSQdIALLRAKVGMV 96
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDItrLKNRE-VPFLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 97 FQKP-TPFPMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVL 175
Cdd:PRK10908 85 FQDHhLLMDRTVYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 176 LLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAAR 217
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-217 |
1.77e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.46 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQRAEGEILLDGDNILTN---SQDIA 87
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREgrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFP-MSIYDNIAFG-----------VRLFEKLSRadmdERVQWALTKAALWNETkdklHQSGYSLS 155
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNrLSVLENVLIGalgstpfwrtcFSWFTREQK----QRALQALTRVGMVHFA----HQRVSTLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAAR 217
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-238 |
2.93e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 19 YYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGdniltnsqDIA-LLRakVGMVF 97
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LEPT---SGRVEVNG--------RVSaLLE--LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 98 QkptpfP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:COG1134 100 H-----PeLTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL----GDFIDQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 177 LDEpcsALdpiSTG----------RIEELITELKqdyTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDD 238
Cdd:COG1134 170 VDE---VL---AVGdaafqkkclaRIRELRESGR---TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-237 |
3.05e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.56 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY---GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFEL--------YPEQRAE--------- 69
Cdd:PTZ00265 1165 KIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfKNEHTNDmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 70 --------------------------------GEILLDGDNILT-NSQDialLRAKVGMVFQKPTPFPMSIYDNIAFGVr 116
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDyNLKD---LRNLFSIVSQEPMLFNMSIYENIKFGK- 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 117 lfEKLSRADMDERVQWALTKA---ALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIE 193
Cdd:PTZ00265 1321 --EDATREDVKRACKFAAIDEfieSLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16131593 194 ELITELKQ--DYTVVIVTHNMQQAARcSDhtafmylgELIEFSNTD 237
Cdd:PTZ00265 1399 KTIVDIKDkaDKTIITIAHRIASIKR-SD--------KIVVFNNPD 1435
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-232 |
3.72e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.99 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraeGEILLDGdnILTNSQDIALLRAKVGMVFQKPTPFPM 105
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPYQ---GSLKING--IELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWNETKDKLH--------QSGySLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:PRK11174 438 TLRDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLPQgldtpigdQAA-GLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 177 LDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIE 232
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-248 |
7.75e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 93.61 E-value: 7.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNLNFYYGKfHALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELYPE--QRAEGEILLDGDNILTNSqd 85
Cdd:PRK10418 2 PQQIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSL---TCAAALGILPAgvRQTAGRVLLDGKPVAPCA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 ialLRAK-VGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWN-ETKDKLHQsgYSLSGGQQQRLC 163
Cdd:PRK10418 76 ---LRGRkIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENaARVLKLYP--FEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
....*..
gi 16131593 242 KPAKKQT 248
Cdd:PRK10418 231 APKHAVT 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-238 |
7.96e-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: 96.74 E-value: 7.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEQRaeGEILLDGDNIltnSQ-DI 86
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPPTA--GSVRLDGADL---SQwDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTPFPMSIYDNIAfgvRLFEklsrADmDERVQWALTKAALwNETKDKLHQ--------SGYSLSGGQ 158
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA---RFGD----AD-PEKVVAAAKLAGV-HEMILRLPDgydtrigeGGARLSGGQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTD 237
Cdd:COG4618 473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRD 551
|
.
gi 16131593 238 D 238
Cdd:COG4618 552 E 552
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-240 |
1.57e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 15 NLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELYPeqRAEGEILLDGDniltnsqDIALL----- 89
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDE-------DISLLplhar 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 -RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVqwaltkaalwNETKDKLHQS------GYSLSGGQQQR 161
Cdd:PRK10895 76 aRRGIGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRA----------NELMEEFHIEhlrdsmGQSLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKqDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDL 239
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
.
gi 16131593 240 F 240
Cdd:PRK10895 225 L 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-257 |
2.43e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLN--FYY--GKFH-----ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDgDNILT 81
Cdd:PRK15112 5 LEVRNLSktFRYrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE--P---TSGELLID-DHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 NSqDIALLRAKVGMVFQKPT----PfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklHQSGYS--LS 155
Cdd:PRK15112 79 FG-DYSYRSQRIRMIFQDPStslnP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD-----HASYYPhmLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|....
gi 16131593 234 SNTDDLFTKPAKKQTEDYITGRYG 257
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAGHFG 255
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-217 |
2.62e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 30 NLDIAKNQVTAFIGPSGCGKSTLLrtfNKM--FeLYPEQraeGEILLDGDNILTNSQDiallRAKVGMVFQKPTPFP-MS 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL---NLIagF-LTPAS---GSLTLNGQDHTTTPPS----RRPVSMLFQENNLFShLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 107 IYDNIAFGVRLFEKLSRADMDERVQWAlTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDP 186
Cdd:PRK10771 88 VAQNIGLGLNPGLKLNAAQREKLHAIA-RQMGI----EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190
....*....|....*....|....*....|...
gi 16131593 187 ISTGRIEELITEL--KQDYTVVIVTHNMQQAAR 217
Cdd:PRK10771 163 ALRQEMLTLVSQVcqERQLTLLMVSHSLEDAAR 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-248 |
3.21e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 5 ETAPSKIQVRNLNFYY-----------GKFHALKNINLDIAKNQVTAFIGPSGCGKST----LLRTFnkmfelypeqRAE 69
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI----------NSQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 70 GEILLDGDNI-LTNSQDIALLRAKVGMVFQKP----TPfPMSIYDNIAFGVRLFEK-LSRADMDERVQWALTKAALWNET 143
Cdd:PRK15134 340 GEIWFDGQPLhNLNRRQLLPVRHRIQVVFQDPnsslNP-RLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 144 KdklHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTV--VIVTHNMQQAARCSDH 221
Cdd:PRK15134 419 R---HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQ 495
|
250 260
....*....|....*....|....*..
gi 16131593 222 TAFMYLGELIEFSNTDDLFTKPAKKQT 248
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-213 |
1.23e-21 |
|
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: 89.70 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-FHALKNINLDIAKNQVTAFIGPSGCGKSTLL-RTFNKMfelypeQRAEGEILLDGDNILTNSQDIAL 88
Cdd:cd03290 1 VQVTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEM------QTLEGKVHWSNKNESEPSFEATR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAK--VGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDE-RVQWALTKAALWNETKdkLHQSGYSLSGGQQQRLCIA 165
Cdd:cd03290 75 SRNRysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131593 166 RGIAIRPEVLLLDEPCSALD-PISTGRIEELITELKQD--YTVVIVTHNMQ 213
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-225 |
2.22e-21 |
|
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: 89.03 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 22 KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRA-EGEILLDGDNILTN------SQDIALLRAKVG 94
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKC------IYGNYLPdSGSILVRHDGGWVDlaqaspREILALRRRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 95 MVFQkptpF----P-MSIYDNIAfgvrlfEKLSRADMDERVqwALTKAA-----------LWnetkdklHQSGYSLSGGQ 158
Cdd:COG4778 97 YVSQ----FlrviPrVSALDVVA------EPLLERGVDREE--ARARARellarlnlperLW-------DLPPATFSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVI-VTHNMQQAARCSDHTAFM 225
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVADRVVDV 225
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-243 |
4.01e-21 |
|
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: 89.12 E-value: 4.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQRAEGEILLDGDNI----LTNSQDI 86
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG--RLAPDHGTATYIMRSGAELelyqLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRADMD--ERVQWALTKaalwneTKDKLHQsgysLSG 156
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDglrMRVSAGANIgerlmAIGARHYGNIRATAQDwlEEVEIDPTR------IDDLPRA----FSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 157 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIEFS 234
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
....*....
gi 16131593 235 NTDDLFTKP 243
Cdd:TIGR02323 232 LTDQVLDDP 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-217 |
4.77e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.09 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNkmfelYPEQRAEGEILLDGDNILT-NSQDIALLRAK-VGMVFQKPTPF 103
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILG-----CLDKPTSGTYRVAGQDVATlDADALAQLRREhFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 104 P-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK10535 99 ShLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131593 183 ALDPISTgriEELITELKQ----DYTVVIVTHNMQQAAR 217
Cdd:PRK10535 174 ALDSHSG---EEVMAILHQlrdrGHTVIIVTHDPQVAAQ 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-246 |
5.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.28 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK-FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNSQdIALL 89
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQK---GKVLVSGIDTGDFSK-LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKP-TPF-PMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:PRK13644 76 RKLVGIVFQNPeTQFvGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGL----EKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQaARCSDHTAFMYLGELIEFSNTDDLFTKPAKK 246
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-243 |
5.70e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.80 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGK----FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElYPEQRAEGEILLDGDNILTNS--Q 84
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLEFNGQDLQRISekE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPTpfpMSIYDNIAFGVRLFEKL------SRADMDERVQWALTKAALwNETKDKLHQSGYSLSGGQ 158
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPM---TSLNPCYTVGFQIMEAIkvhqggNKKTRRQRAIDLLNQVGI-PDPASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*..
gi 16131593 237 DDLFTKP 243
Cdd:PRK11022 239 HDIFRAP 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-211 |
1.34e-20 |
|
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: 86.43 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkM-FELYPEqrAEGEILLDGDNILTNSQDialL 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MgHPKYEV--TEGEILFKGEDITDLPPE---E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVG--MVFQKPTPFPmsiydniafGVRLfeklsradmdervqwaltkaalwnetKDKLHQSGYSLSGGQQQRLCIARG 167
Cdd:cd03217 74 RARLGifLAFQYPPEIP---------GVKN--------------------------ADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131593 168 IAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHN 211
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-210 |
1.80e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.07 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNLNFY------YGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGDNIlt 81
Cdd:cd03213 1 GVTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVLINGRPL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 nsqDIALLRAKVGMVFQkptpfpmsiyDNIafgvrLFEKLSradmderVQWALTKAAlwnetkdKLHqsgySLSGGQQQR 161
Cdd:cd03213 76 ---DKRSFRKIIGYVPQ----------DDI-----LHPTLT-------VRETLMFAA-------KLR----GLSGGERKR 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTH 210
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-249 |
2.39e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 28 NINLDIAKNQVTAFIGPSGCGKS----TLLRTFNKMFELYPEqraeGEILLDGDNILTNSQdiALLRA----KVGMVFQK 99
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPS----GDIRFHGESLLHASE--QTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 PTpfpMSIYDNIAFGVRLFEKLS----------RADMD---ERVqwALTKAAlwNETKDKLHQsgysLSGGQQQRLCIAR 166
Cdd:PRK15134 101 PM---VSLNPLHTLEKQLYEVLSlhrgmrreaaRGEILnclDRV--GIRQAA--KRLTDYPHQ----LSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
....*
gi 16131593 245 KKQTE 249
Cdd:PRK15134 250 HPYTQ 254
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-212 |
2.54e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.09 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGK---FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNiltNSQDI 86
Cdd:PTZ00265 382 KIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINDSH---NLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 AL--LRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKL-------------SRADMDERVQWALTKAALWNE-----TKDK 146
Cdd:PTZ00265 454 NLkwWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLealsnyynedgndSQENKNKRNSCRAKCAGDLNDmsnttDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 147 LHQ---------------------------------------SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPI 187
Cdd:PTZ00265 534 LIEmrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260
....*....|....*....|....*..
gi 16131593 188 STGRIEELITELK--QDYTVVIVTHNM 212
Cdd:PTZ00265 614 SEYLVQKTINNLKgnENRITIIIAHRL 640
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-233 |
6.87e-20 |
|
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: 84.89 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 20 YGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGdniltnsQDIALLRAKVGMVFQk 99
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPD---SGTVTVRG-------RVSSLLGLGGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 ptpfpMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:cd03220 99 -----LTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSEL----GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 180 PCSALDPI----STGRIEELItelKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEF 233
Cdd:cd03220 169 VLAVGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-237 |
1.36e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEQraeGEILLDG-DNILTNSQDIA--- 87
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDA---GEVHYRMrDGQLRDLYALSeae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 ---LLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRADMD--ERVQWALtkaalwnetkDKLHQSGYSL 154
Cdd:PRK11701 83 rrrLLRTEWGFVHQHPRDglrMQVSAGGNIgerlmAVGARHYGDIRATAGDwlERVEIDA----------ARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
....*
gi 16131593 233 FSNTD 237
Cdd:PRK11701 233 SGLTD 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-221 |
2.88e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 6 TAPskIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEQraeGEILLDGDNILTNSQd 85
Cdd:PRK13537 5 VAP--IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDA---GSISLCGEPVPSRAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 iaLLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCI 164
Cdd:PRK13537 77 --HARQRVGVVPQFDNLDPdFTVRENLLVFGRYF-GLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-239 |
4.06e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 86.33 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFE-LYPEqrAEGEILLDGDNIltNSQDIAlL 89
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTM----KMLTgLLPA--SEGEAWLFGQPV--DAGDIA-T 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKptpFpmSIY------DNIAFGVRLFEkLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:NF033858 338 RRRVGYMSQA---F--SLYgeltvrQNLELHARLFH-LPAAEIAARVAEMLERFDL----ADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCsDHTAFMYLG---------ELIE 232
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHAGrvlasdtpaALVA 486
|
....*..
gi 16131593 233 FSNTDDL 239
Cdd:NF033858 487 ARGAATL 493
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-211 |
4.36e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkM-FELYpeQRAEGEILLDGDNILTNSQDIallR 90
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MgHPKY--EVTSGSILLDGEDILELSPDE---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVG--MVFQKPTPFP-MSIYD--NIAFGVRLFEKLSRADMDERVQwalTKAALWNETKDKLHQS-GYSLSGGQQQRLCI 164
Cdd:COG0396 75 ARAGifLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFLKLLK---EKMKELGLDEDFLDRYvNEGFSGGEKKRNEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131593 165 ARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHN 211
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHY 199
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-220 |
7.90e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPeqrAEGEILLDGDNIltNSQDIALLR 90
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTP---TAGTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQKPT-PFPMSIYDNIAFGVRlfEKLSRAD-MDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGRT--PHRSRFDtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSD 220
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCD 207
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-241 |
1.08e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPeqrAEGEILLDGDNILTNS-QDIALLRAKVGMvfQKPTPFP 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLP---GQGEILLNGRPLSDWSaAELARHRAYLSQ--QQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 MSIYDNIAFGVrlfEKLSRADMDERVQWALTkAALwnETKDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLL 177
Cdd:COG4138 84 MPVFQYLALHQ---PAGASSEAVEQLLAQLA-EAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 178 DEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-231 |
1.53e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNSQDIALLRA 91
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPL--ESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVFQK-PTPFPMSIYDNIAFGVRLFE----KLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK10575 86 KVAYLPQQlPAAEGMTVRELVAIGRYPWHgalgRFGAADR-EKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 167 GIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGELI 231
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-211 |
2.20e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTNS--QDIALLRAKVGMvfqKPTpf 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKLDGGDIDDPDvaEACHYLGHRNAM---KPA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 104 pMSIYDNIAFGVRLfeklsRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:PRK13539 88 -LTVAENLEFWAAF-----LGGEELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*....
gi 16131593 184 LDPISTGRIEELITE-LKQDYTVVIVTHN 211
Cdd:PRK13539 158 LDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-219 |
2.22e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.40 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--GKFHA--LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGD--NILTNSQ 84
Cdd:PRK11629 6 LQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQpmSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 163
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPdFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL----EHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 164 IARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL--KQDYTVVIVTHNMQQAARCS 219
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-230 |
2.53e-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: 79.78 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYygkfHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNILTNSQDIALlRA 91
Cdd:cd03215 6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEA---LFGLRP--PASGEITLDGKPVTRRSPRDAI-RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVfqkptP--------FP-MSIYDNIAFGVRLfeklsradmdervqwaltkaalwnetkdklhqsgyslSGGQQQRL 162
Cdd:cd03215 76 GIAYV-----PedrkreglVLdLSVAENIALSSLL-------------------------------------SGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-242 |
2.66e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 83.94 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 21 GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPEqrAEGEILLDGDNIltNSQDIALLRAKVGMVFQKP 100
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL---IVGIWPP--TSGSVRLDGADL--KQWDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 TPFPMSIYDNIAfgvRLFEKlsrADMDERVQWAltKAALWNETKDKLHQsGY---------SLSGGQQQRLCIARGIAIR 171
Cdd:TIGR01842 402 ELFPGTVAENIA---RFGEN---ADPEKIIEAA--KLAGVHELILRLPD-GYdtvigpggaTLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131593 172 PEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMqQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-230 |
5.77e-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: 83.14 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTllrTFNKMFELYPEqrAEGEILLDGDNILTNsqdIALLRAKVGMVFQKPTPFP 104
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPP--TSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 -MSIYDNIAFgvrlFEKLSRADMDERvqwALTKAALWNET--KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:TIGR01257 1017 hLTVAEHILF----YAQLKGRSWEEA---QLEMEAMLEDTglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131593 182 SALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-231 |
1.61e-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: 78.91 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY--------------GKFH-------ALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPEQr 67
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkSLFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTL----KILSglLQPTS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 68 aeGEILLDGdnILTNSQDIALLRaKVGMVF-QKPTpfpmSIYD-NIAFGVRLFEKLSRADmDERVQWALTKAALWNETKD 145
Cdd:cd03267 76 --GEVRVAG--LVPWKRRKKFLR-RIGVVFgQKTQ----LWWDlPVIDSFYLLAAIYDLP-PARFKKRLDELSELLDLEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 146 KLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQQAARCSDHTA 223
Cdd:cd03267 146 LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVL 225
|
....*...
gi 16131593 224 FMYLGELI 231
Cdd:cd03267 226 VIDKGRLL 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-239 |
1.66e-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: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 5 ETAP-------SKIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLD 75
Cdd:TIGR00957 1272 ETAPpsgwpprGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIID 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 76 GDNIltnsQDIAL--LRAKVGMVFQKPTPFPMSIYDNIafgvRLFEKLSradmDERVQWALTKAALW---NETKDKL-HQ 149
Cdd:TIGR00957 1347 GLNI----AKIGLhdLRFKITIIPQDPVLFSGSLRMNL----DPFSQYS----DEEVWWALELAHLKtfvSALPDKLdHE 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 150 ---SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAArcsDHTAFMY 226
Cdd:TIGR00957 1415 caeGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM---DYTRVIV 1491
|
250
....*....|....*
gi 16131593 227 L--GELIEFSNTDDL 239
Cdd:TIGR00957 1492 LdkGEVAEFGAPSNL 1506
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-210 |
1.79e-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: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 5 ETAPSKIQVRNLNFYYGKFHAL-KNINLDIAKNQVTAFIGPSGCGKSTLLRTFNkmfELYPeqRAEGEILL-DGDNILtn 82
Cdd:COG4178 357 TSEDGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWP--YGSGRIARpAGARVL-- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 sqdiallrakvgmvF--QKPtpfpmsiYdnIAFGvRLFEKLSRADM-----DERVQWALTKAALwNETKDKLHQS---GY 152
Cdd:COG4178 430 --------------FlpQRP-------Y--LPLG-TLREALLYPATaeafsDAELREALEAVGL-GHLAERLDEEadwDQ 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTH 210
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-231 |
2.63e-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: 78.08 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPeqRAEGEILLDGDNIltnsqDIALLRAKVGMVFQKPTPFP- 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--TTSGQILFNGQPR-----KPDQFQKCVAYVRQDDILLPg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 MSIYDNIAFGV--RLFEKLSRADMDERV------QWALTKAAlwnetkdklHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:cd03234 96 LTVRETLTYTAilRLPRKSSDAIRKKRVedvllrDLALTRIG---------GNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 177 LDEPCSALDPISTGRIEELITELKQDYTVVIVT-HnmQQAA---RCSDHTAFMYLGELI 231
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiH--QPRSdlfRLFDRILLLSSGEIV 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
10-218 |
4.23e-17 |
|
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: 78.36 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGDNilTNSQDIA 87
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGDIQIDGVS--WNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRADMDERVQWalTKAALWNETKD----------------KLHQSG 151
Cdd:cd03289 74 KWRKAFGVIPQK---------------VFIFSGTFRKNLDPYGKW--SDEEIWKVAEEvglksvieqfpgqldfVLVDGG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 152 YSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARC 218
Cdd:cd03289 137 CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLEC 203
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-210 |
5.92e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.76 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltnsQDIAL--LRAKVGMVFQKPTP 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPL----TKLQLdsWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 FPMSIYDNIAFGvrlfeklsRAD-MDERVQWAltkAALWNETKDKLH----------QSGYSLSGGQQQRLCIARGIAIR 171
Cdd:PRK10789 401 FSDTVANNIALG--------RPDaTQQEIEHV---ARLASVHDDILRlpqgydtevgERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 172 PEVLLLDEPCSALDpistGRIE-ELITELKQ---DYTVVIVTH 210
Cdd:PRK10789 470 AEILILDDALSAVD----GRTEhQILHNLRQwgeGRTVIISAH 508
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-239 |
8.87e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.40 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnkmfELYPEQRA--EGEI-LLDGDniLTNSQDIA 87
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVeVLGGD--MADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQ---K---PTpfpMSIYDNIAFGVRLFeKLSRADMDERVQwALTKAalwnetkdklhqSGYS-------- 153
Cdd:NF033858 73 AVCPRIAYMPQglgKnlyPT---LSVFENLDFFGRLF-GQDAAERRRRID-ELLRA------------TGLApfadrpag 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 154 -LSGGQQQR--LCIArgiAIR-PEVLLLDEPCSALDPISTGRIEELITELKQD---YTVVIVTHNMQQAARCsDHTAFMY 226
Cdd:NF033858 136 kLSGGMKQKlgLCCA---LIHdPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAERF-DWLVAMD 211
|
250 260
....*....|....*....|..
gi 16131593 227 LG---------ELIEFSNTDDL 239
Cdd:NF033858 212 AGrvlatgtpaELLARTGADTL 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-218 |
1.26e-16 |
|
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: 79.18 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYY--GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGdnILTNSQDIA 87
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS------TEGEIQIDG--VSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRADMDERVQWalTKAALWNETK------------DKLH----QSG 151
Cdd:TIGR01271 1289 TWRKAFGVIPQK---------------VFIFSGTFRKNLDPYEQW--SDEEIWKVAEevglksvieqfpDKLDfvlvDGG 1351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 152 YSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARC 218
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-210 |
1.85e-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: 74.02 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGdniltnsqdiallR 90
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPD-----EGIVTWGS-------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 170
Cdd:cd03221 63 VKIGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131593 171 RPEVLLLDEPCSALDPIStgrIEELITELKQDY-TVVIVTH 210
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALKEYPgTVILVSH 125
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-210 |
2.06e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 75.77 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 22 KFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRtfnKMFELYPEQRAEGEILLDGDNIltnSQDIALLRAkvgmvfqkpt 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR---LLAGALKGTPVAGCVDVPDNQF---GREASLIDA---------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 102 pfpMSIYDNIAFGVRLfekLSRAdmdervqwALTKAALWnetKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPC 181
Cdd:COG2401 106 ---IGRKGDFKDAVEL---LNAV--------GLSDAVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|...
gi 16131593 182 SALDPISTGR----IEELITELKQdyTVVIVTH 210
Cdd:COG2401 165 SHLDRQTAKRvarnLQKLARRAGI--TLVVATH 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-244 |
3.31e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 28 NINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPEQraEGEILLdGDNILTNS-QDIALL--RAKVGMVFQKPTPFP 104
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTRPQ--KGRIVL-NGRVLFDAeKGICLPpeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 -MSIYDNIAFGVRlfeKLSRADMDERVQwALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:PRK11144 90 hYKVRGNLRYGMA---KSMVAQFDKIVA-LLGIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 184 LD-PistgRIEELIT---ELKQDYTVVI--VTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPA 244
Cdd:PRK11144 159 LDlP----RKRELLPyleRLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-210 |
7.50e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 13 VRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPEqraEGEILLDGDniltnsqdiallrAK 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--ELEPD---SGEVSIPKG-------------LR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 93 VGMVFQKPTPFP-MSIYDNIAFGV-RLFEKLSR------------ADMDE--RVQWALTKAALWN-ETK----------- 144
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGDaELRALEAEleeleaklaepdEDLERlaELQEEFEALGGWEaEARaeeilsglgfp 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 145 -DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgrIEELITELKQ-DYTVVIVTH 210
Cdd:COG0488 143 eEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWLEEFLKNyPGTVLVVSH 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-239 |
8.29e-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: 76.38 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 4 VETAPSKIQVRNLNFYY-----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEI-LLDGD 77
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE--P---TSGEVnVRVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 78 NILTNSQDIALLRAKV----GMVFQKPTPFP-MSIYDNI--AFGVRLFEKLSRadmdERVQWALtKAALWNETKDK--LH 148
Cdd:TIGR03269 348 EWVDMTKPGPDGRGRAkryiGILHQEYDLYPhRTVLDNLteAIGLELPDELAR----MKAVITL-KMVGFDEEKAEeiLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 149 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELI----TELKQdyTVVIVTHNMQQAARCSDHTAF 224
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQ--TFIIVSHDMDFVLDVCDRAAL 500
|
250
....*....|....*
gi 16131593 225 MYLGELIEFSNTDDL 239
Cdd:TIGR03269 501 MRDGKIVKIGDPEEI 515
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-241 |
9.18e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEIlldgdNILTNSQDIA 87
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRL-----ASGKI-----SILGQPTRQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPT---PFPMSIYDNIA---FGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 161
Cdd:PRK15056 75 LQKNLVAYVPQSEEvdwSFPVLVEDVVMmgrYGHMGWLRRAKKRDRQIVTAALARVDM----VEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAfMYLGELIEFSNTDDLF 240
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
.
gi 16131593 241 T 241
Cdd:PRK15056 230 T 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-237 |
1.63e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNfyygKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNI-LTNSQD----- 85
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA---LFGADP--ADSGEIRLDGKPVrIRSPRDairag 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALL---RAKVGMVFqkptpfPMSIYDNIAFGVrlFEKLSRAD-MDERVQWALTKAALwnetkDKL-------HQSGYSL 154
Cdd:COG1129 329 IAYVpedRKGEGLVL------DLSIRENITLAS--LDRLSRGGlLDRRRERALAEEYI-----KRLriktpspEQPVGNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPcsaldpisTgR---------IEELITEL-KQDYTVVIVTHNMQQAARCSDHTAF 224
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEP--------T-RgidvgakaeIYRLIRELaAEGKAVIVISSELPELLGLSDRILV 466
|
250
....*....|....
gi 16131593 225 MYLGELI-EFSNTD 237
Cdd:COG1129 467 MREGRIVgELDREE 480
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-244 |
2.53e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelyPEQ------RAEGEILLDGDNILT-NSQDIALLRAkvgMVFQ 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL---TGGgaprgaRVTGDVTLNGEPLAAiDAPRLARLRA---VLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 99 KPTP-FPMSIYDNIAFG----VRLFEKLSRADMDerVQWaltkAALWNETKDKL-HQSGYSLSGGQQQRLCIARGIA--- 169
Cdd:PRK13547 91 AAQPaFAFSAREIVLLGryphARRAGALTHRDGE--IAW----QALALAGATALvGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 170 ------IRPEVLLLDEPCSALDPISTGRIEELITELKQDYT--VVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
...
gi 16131593 242 kPA 244
Cdd:PRK13547 245 -PA 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-252 |
8.29e-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: 73.32 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGDNILTNS-QDIAll 89
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG---VYPHGTWDGEIYWSGSPLKASNiRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWAltkAALWNETK---DKLHQSGYSLSGGQQQRLCIA 165
Cdd:TIGR02633 77 RAGIVIIHQELTLVPeLSVAENIFLGNEITLPGGRMAYNAMYLRA---KNLLRELQldaDNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 166 RGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfTKPA 244
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVA--------TKDM 225
|
....*...
gi 16131593 245 KKQTEDYI 252
Cdd:TIGR02633 226 STMSEDDI 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-242 |
8.94e-15 |
|
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: 73.30 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEqraEGEIL----------------L 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT---SGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 75 DGDNILT-----NSQDIAL----------LRAKVGMVFQKPtpfpMSIYDNIAFGVRLFEKLSRADM--DERVQWALTka 137
Cdd:TIGR03269 78 VGEPCPVcggtlEPEEVDFwnlsdklrrrIRKRIAIMLQRT----FALYGDDTVLDNVLEALEEIGYegKEAVGRAVD-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 138 aLWNETK--DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQ 213
Cdd:TIGR03269 152 -LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260
....*....|....*....|....*....
gi 16131593 214 QAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-254 |
1.01e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 6 TAPSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNI--LTNS 83
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-----VPPDSGTLEIGGNPCarLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 84 QDIALlraKVGMVFQKPTPFP-MSIYDNIAFGVRlfeklSRADMDERVQWALtkAALwnETKDKLHQSGYSLSGGQQQRL 162
Cdd:PRK15439 82 KAHQL---GIYLVPQEPLLFPnLSVKENILFGLP-----KRQASMQKMKQLL--AAL--GCQLDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPIST----GRIEELiteLKQDYTVVIVTHNMQQAARCSDHTAFM-----YLGELIEF 233
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETerlfSRIREL---LAQGVGIVFISHKLPEIRQLADRISVMrdgtiALSGKTAD 226
|
250 260
....*....|....*....|.
gi 16131593 234 SNTDDLFTKPAKKQTEDYITG 254
Cdd:PRK15439 227 LSTDDIIQAITPAAREKSLSA 247
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
10-242 |
1.07e-14 |
|
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: 71.48 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 10 KIQVRNLNFYYGKF--HALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEILLDGDNIltNSQDIA 87
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 LLRAKVGMVFQKPTPFPMSIYDNIafgvrlfeKLSRADMDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQQ 160
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNL--------DPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGELIEFSNTDDLF 240
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
..
gi 16131593 241 TK 242
Cdd:cd03288 243 AQ 244
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-213 |
1.58e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFE--LYPEqraEGEILLDGDNIltNSQDIALLRaKVGMVF-QK- 99
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTI----KMLTgiLVPT---SGEVRVLGYVP--FKRRKEFAR-RIGVVFgQRs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 ------PT--PFPM--SIYDniafgvrlfekLSRADMDERVQWaLTKaALwnETKDKLHQSGYSLSGGQQQRLCIArgiA 169
Cdd:COG4586 106 qlwwdlPAidSFRLlkAIYR-----------IPDAEYKKRLDE-LVE-LL--DLGELLDTPVRQLSLGQRMRCELA---A 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131593 170 I---RPEVLLLDEPCSALDPISTGRIEELITELKQDY--TVVIVTHNMQ 213
Cdd:COG4586 168 AllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-252 |
2.00e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 71.76 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY----GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYPEQRAEGEILLDGDNI-LTNSQD 85
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLrLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 86 IALLRAKVGMVFQKPtpfpMSIYD-NIAFGVRLFEKLS----RADMDERVQWALTKAALW------NETKDKLHQSGYSL 154
Cdd:PRK15093 84 RKLVGHNVSMIFQEP----QSCLDpSERVGRQLMQNIPgwtyKGRWWQRFGWRKRRAIELlhrvgiKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD--YTVVIVTHNMQQAARCSDHTAFMYLGELIE 232
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260
....*....|....*....|
gi 16131593 233 FSNTDDLFTKPAKKQTEDYI 252
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALI 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-217 |
2.12e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 72.64 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGdniltnsqdiallraKVGMVFQKPTPFPM 105
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEP---SEGKIKHSG---------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:TIGR01271 502 TIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 16131593 186 PISTGRI-EELITELKQDYTVVIVTHNMQQAAR 217
Cdd:TIGR01271 581 VVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-210 |
2.85e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLdGDNILTN--SQDIAL 88
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPD---SGTVKL-GETVKIGyfDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKvgmvfqkptpfpMSIYDNIafgvrlfeklSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:COG0488 390 LDPD------------KTVLDEL----------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131593 169 AIRPEVLLLDEPCSALDPIStgrIEELiTELKQDY--TVVIVTH 210
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET---LEAL-EEALDDFpgTVLLVSH 487
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-243 |
4.30e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 41 FIGPSGCGKSTLLRTFNKMFElypeqrAEGEILLDGDNILTNSQ-DIALLRAKVGMvfQKPTPFPMSIYDNIAfgvrlfe 119
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLP------GSGSIQFAGQPLEAWSAaELARHRAYLSQ--QQTPPFAMPVFQYLT------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 120 kLSRADM--DERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLLDEPCSALDPISTG 190
Cdd:PRK03695 92 -LHQPDKtrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131593 191 RIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKP 243
Cdd:PRK03695 171 ALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
5.01e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETApskIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPEqraEGEILLDGDNIL 80
Cdd:PRK13536 35 GSMSTVA---IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PD---AGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 81 TNSQdiaLLRAKVGMVFQKPTPFP-MSIYDN-IAFGvRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQ 158
Cdd:PRK13536 107 ARAR---LARARIGVVPQFDNLDLeFTVRENlLVFG-RYF-GMSTREIEAVIPSLLEFARLESKADARVSD----LSGGM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSD 220
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCD 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-220 |
6.30e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.71 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNI-LTNSQDIalLRAKVGMVFQKPTPF 103
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-----QPDAGSILIDGQEMrFASTTAA--LAAGVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 104 P-MSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYsLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PRK11288 92 PeMTVAENLYLG-QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131593 183 ALDPISTGRIEELITELKQDYTVVI-VTHNMQQAARCSD 220
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCD 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-237 |
1.26e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElyPeqrAEGEILLDGD--NILTNSQDIAL 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--P---TKGTITINNInyNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 lraKVGMVFQKPTPF-PMSIYDNIAFGVRLFEK------LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 161
Cdd:PRK09700 81 ---GIGIIYQELSVIdELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 162 LCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYT-VVIVTHNMQQAARCSDHTAFM------YLGELIEFS 234
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVMkdgssvCSGMVSDVS 233
|
...
gi 16131593 235 NTD 237
Cdd:PRK09700 234 NDD 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-242 |
5.06e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNI----LTNsqdialLRAKVGMVFQKPT 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL-----EKGRIMIDDCDVakfgLTD------LRRVLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 102 PFPMSIydniAFGVRLFEKLSRADMDERVQWALTKAALWNET---KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:PLN03232 1321 LFSGTV----RFNIDPFSEHNDADLWEALERAHIKDVIDRNPfglDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 179 EPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-210 |
5.65e-13 |
|
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: 65.84 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 13 VRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfeLYPEqraEGEILLDGDNILTN----SQDIAL 88
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRPD---SGEVRWNGTPLAEQrdepHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LRAKVGMvfqKPTpfpMSIYDNIAFGVRLFEKLSRADMDervqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:TIGR01189 78 LGHLPGL---KPE---LSALENLHFWAAIHGGAQRTIED-----ALAAVGL----TGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-237 |
7.31e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeqRAEGEILLDGDNILTNS-QD-----IALL---RAKVGMV 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKV---LYGALP--RTSGYVTLDGHEVVTRSpQDglangIVYIsedRKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 97 FQkptpfpMSIYDNIAF-GVRLFEKLS-RADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:PRK10762 343 LG------MSVKENMSLtALRYFSRAGgSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131593 175 LLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELI-EFSNTD 237
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGRISgEFTREQ 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-239 |
8.00e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFYygKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFELYPeqRAEGEILLDGDNILTNSQDIALlra 91
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDK--RAGGEIRLNGKDISPRSPLDAV--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 92 KVGMVF----QKPTPF--PMSIYDNIAFGVRLfeKLSR--------ADMDERvQWALTKAALWNETKDKLHQSGYSLSGG 157
Cdd:PRK09700 337 KKGMAYitesRRDNGFfpNFSIAQNMAISRSL--KDGGykgamglfHEVDEQ-RTAENQRELLALKCHSVNQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIE-FSN 235
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTN 493
|
....
gi 16131593 236 TDDL 239
Cdd:PRK09700 494 RDDM 497
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-210 |
9.84e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFELYPE-QRAEGEILLDGDNILTNSQDIall 89
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLS----KVIAGHPAyKILEGDILFKGESILDLEPEE--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RAKVG--MVFQKPTPFPMsiYDNIAF------GVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQS---GYslSGGQ 158
Cdd:CHL00131 81 RAHLGifLAFQYPIEIPG--VSNADFlrlaynSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNvneGF--SGGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTH 210
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITH 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-234 |
1.02e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.50 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDgdniltnsQDIAllrakvgMVFQKPTPFPM 105
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----SEGRVWAE--------RSIA-------YVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFgvrlFEKLSRADMDERVQ-------WALTKAALWNETKDKlhqsGYSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:PTZ00243 736 TVRGNILF----FDEEDAARLADAVRvsqleadLAQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 179 EPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARcSDHTAFMYLGElIEFS 234
Cdd:PTZ00243 808 DPLSALDAHVGERVvEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR-VEFS 862
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-252 |
1.11e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfeLYPEQRAEGEILLDGD-----NIL-TNSQ 84
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYPHGTYEGEIIFEGEelqasNIRdTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 85 DIALLRAKVGMVFQkptpfpMSIYDNIAFGVRLfEKLSRADMDERVQWAltkAALWNETKDKL--HQSGYSLSGGQQQRL 162
Cdd:PRK13549 83 GIAIIHQELALVKE------LSVLENIFLGNEI-TPGGIMDYDAMYLRA---QKLLAQLKLDInpATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfT 241
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICVIRDGRHIG--------T 224
|
250
....*....|.
gi 16131593 242 KPAKKQTEDYI 252
Cdd:PRK13549 225 RPAAGMTEDDI 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-212 |
1.38e-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: 67.28 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFH--ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGdniltnsqdial 88
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKG------------ 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 lraKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 168
Cdd:TIGR00957 700 ---SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVL-EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELIT---ELKQDYTVVIVTHNM 212
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGI 822
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-217 |
1.43e-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: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqrAEGEILLDGdniltnsqdiallraKVGMVFQKPTPFPM 105
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEP---SEGKIKHSG---------------RISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGVrlfeklsraDMDERVQWALTKAALWNE------TKDK--LHQSGYSLSGGQQQRLCIARGIAIRPEVLLL 177
Cdd:cd03291 113 TIKENIIFGV---------SYDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131593 178 DEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAAR 217
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-210 |
2.36e-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: 63.33 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELYpeqraEGEI-LLDGDNILtnsqdiallrakvgMVFQKPtpfp 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIgMPEGEDLL--------------FLPQRP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 msiYdnIAFGvRLFEKLSRAdmdervqwaltkaalWNETkdklhqsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSAL 184
Cdd:cd03223 74 ---Y--LPLG-TLREQLIYP---------------WDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*.
gi 16131593 185 DPISTGRIEELITELKqdYTVVIVTH 210
Cdd:cd03223 123 DEESEDRLYQLLKELG--ITVISVGH 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
11-221 |
2.94e-12 |
|
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: 64.20 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNlnfyyGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLL---------RTFNKMFELYPEQRAEGEILLDGDNILT 81
Cdd:cd03270 1 IIVRG-----AREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqRRYVESLSAYARQFLGQMDKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 82 NSQDIAL--------LRAKVGMVfqkptpfpMSIYDNIAFgvrLFeklSRADMDERVQWaLTKAALWNETkdkLHQSGYS 153
Cdd:cd03270 76 LSPAIAIdqkttsrnPRSTVGTV--------TEIYDYLRL---LF---ARVGIRERLGF-LVDVGLGYLT---LSRSAPT 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 154 LSGGQQQRLCIARGIAIR-PEVL-LLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNmQQAARCSDH 221
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHD-EDTIRAADH 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-240 |
8.89e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNIltNSQDIALLRAKVGMVFQKPTPFPM 105
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-----CGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNI-----AFGVRLFEKLSRADMDERVqwaltkaALWNETKD-KLHQSGYSLSGGQQQRLCIARGIAIRPE-VLLLD 178
Cdd:PTZ00243 1399 TVRQNVdpfleASSAEVWAALELVGLRERV-------ASESEGIDsRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 179 EPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCS-----DHTAFMYLG---ELIEfsNTDDLF 240
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDkiivmDHGAVAEMGsprELVM--NRQSIF 1539
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-242 |
2.24e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeqrAEGEILLDGDNILTNSqdIALLRAKVGMVFQKPTPFPM 105
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDISKFG--LMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIydniAFGVRLFEKLSRADMDERVQWALTKAALWNETKD---KLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 182
Cdd:PLN03130 1328 TV----RFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGldaEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 183 ALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCsDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-185 |
5.39e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYY---GKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPeqRAEGEILLdgdniltnsqdia 87
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASVVI------------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 llRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsrADMD-ERVQWALTKAALWNETK-------DKLHQSGYSLSGGQQ 159
Cdd:PLN03130 678 --RGTVAYVPQVSWIFNATVRDNILFG---------SPFDpERYERAIDVTALQHDLDllpggdlTEIGERGVNISGGQK 746
|
170 180
....*....|....*....|....*.
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-210 |
8.92e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNkmfelypeqraeGEILLDgDNILTNSQDIALLRAKvgmvfQKPtpfPM 105
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLD-DGRIIYEQDLIVARLQ-----QDP---PR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 ----SIYDNIAFGV-------RLFEKLSRADMDE----------RVQWALTKAALW---NETKDKLHQSGY-------SL 154
Cdd:PRK11147 78 nvegTVYDFVAEGIeeqaeylKRYHDISHLVETDpseknlnelaKLQEQLDHHNLWqleNRINEVLAQLGLdpdaalsSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 155 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgrIEELITELKqDY--TVVIVTH 210
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLK-TFqgSIIFISH 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-209 |
1.06e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRAEGEILLDGDNIltnsqDIALLRAKVGMVFQKPTPF 103
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 104 PM-SIYDNIAFG--VRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:TIGR00955 112 PTlTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|.
gi 16131593 179 EPCSALDPISTGRIEELITELKQDYTVVIVT 209
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-210 |
1.88e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 19 YYGKFHALKNINLDI---AKNQVtafIGPSGCGKSTLLRTfnkMFELypEQRAEGEILLdgdniltnSQDIallraKVGM 95
Cdd:TIGR03719 14 VPPKKEILKDISLSFfpgAKIGV---LGLNGAGKSTLLRI---MAGV--DKDFNGEARP--------QPGI-----KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 96 VFQKPTPFP-MSIYDNIAFGVR-----------LFEKLSR--ADMDE------RVQWALTKAALWN-ETK-----DKLH- 148
Cdd:TIGR03719 73 LPQEPQLDPtKTVRENVEEGVAeikdaldrfneISAKYAEpdADFDKlaaeqaELQEIIDAADAWDlDSQleiamDALRc 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 149 ----QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELItelkQDY--TVVIVTH 210
Cdd:TIGR03719 153 ppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYpgTVVAVTH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-224 |
2.58e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNILTN----SQDiallrAKVGMVFQKP 100
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSILYLGKEVTFNgpksSQE-----AGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 TPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWA---LTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 176
Cdd:PRK10762 89 NLIPqLTIAENIFLGREFVNRFGRIDWKKMYAEAdklLARLNL----RFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131593 177 LDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAAR-CSDHTAF 224
Cdd:PRK10762 165 MDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEiCDDVTVF 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-213 |
2.69e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQraegeilldgdnilTNSQDIallRAKVGMVFQKPTPFPM 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAE--------------TSSVVI---RGSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGVRlFEKlsradmdERVQWALTKAALWNE-------TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 178
Cdd:PLN03232 694 TVRENILFGSD-FES-------ERYWRAIDVTALQHDldllpgrDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131593 179 EPCSALDP-ISTGRIEELITELKQDYTVVIVTHNMQ 213
Cdd:PLN03232 766 DPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLH 801
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-210 |
2.91e-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: 58.27 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNILTNSQDIAllRAKVGMVFQKPTPFPM 105
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL-----SPPLAGRVLLNGGPLDFQRDSIA--RGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFgvrlfekLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:cd03231 89 SVLENLRF-------WHADHSDEQVEEALARVGL----NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 16131593 186 PISTGRIEELIT-ELKQDYTVVIVTH 210
Cdd:cd03231 158 KAGVARFAEAMAgHCARGGMVVLTTH 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-222 |
4.13e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLlrtfnkMFEL---YPEQRAEGEILLDGD-------------NILTNSQDIAL 88
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTL------MKVLsgvYPHGSYEGEILFDGEvcrfkdirdsealGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 89 LrakvgmvfqkptPFpMSIYDNIAFGvrlFEKLSRADMDervqWALTkaalWNETKDKLHQSGYSLS--------G-GQQ 159
Cdd:NF040905 90 I------------PY-LSIAENIFLG---NERAKRGVID----WNET----NRRARELLAKVGLDESpdtlvtdiGvGKQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 160 QRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHT 222
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-254 |
4.16e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYpeQRAEGEILLDGDNILTNSQDIAlLRAKVGMVFQKPTPF- 103
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKC---LFGIY--QKDSGSILFQGKEIDFKSSKEA-LENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 104 PMSIYDNIAFGvRLFEKLSRADMDErvqwaltkaaLWNETK---DKL------HQSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:PRK10982 87 QRSVMDNMWLG-RYPTKGMFVDQDK----------MYRDTKaifDELdididpRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 175 LLLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGELIEfsntddlfTKPAKKQTEDYIT 253
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDKII 227
|
.
gi 16131593 254 G 254
Cdd:PRK10982 228 A 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-221 |
5.66e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLL--------RTFNKMFELYPEQRAEGEILLDgdnIltn 82
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLslitgdhpQGYSNDLTLFGRRRGSGETIWD---I--- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 83 SQDIALLRAKVGMVFQKPTpfpmSIYDNIAFG----VRLFEKLSRADMDERVQWaLTKAALWNETKDKLHQSgysLSGGQ 158
Cdd:PRK10938 335 KKHIGYVSSSLHLDYRVST----SVRNVILSGffdsIGIYQAVSDRQQKLAQQW-LDILGIDKRTADAPFHS---LSWGQ 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPIStgR------IEELITElkQDYTVVIVTHNMQQAARCSDH 221
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLN--RqlvrrfVDVLISE--GETQLLFVSHHAEDAPACITH 471
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-185 |
7.31e-10 |
|
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: 56.87 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNLNFY----YGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfelypEQRA-----EGEILLDGDN 78
Cdd:cd03232 1 GSVLTWKNLNYTvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--------AGRKtagviTGEILINGRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 79 IltnsqDIALLRaKVGMVFQKPTPFPMSIydniafgVR---LFEKLSRAdmdervqwaltkaalwnetkdklhqsgysLS 155
Cdd:cd03232 73 L-----DKNFQR-STGYVEQQDVHSPNLT-------VRealRFSALLRG-----------------------------LS 110
|
170 180 190
....*....|....*....|....*....|
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:cd03232 111 VEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-212 |
1.06e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfeLYPEQRAEGEILLDGdniltnsqdiallR 90
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-----LGLVAPDEGVIKRNG-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMVFQK----PT-PFPMSIYDNIAFGVRlfeklsRADMD---ERVQwaltKAALWNETKDKLhqsgyslSGGQQQRL 162
Cdd:PRK09544 67 LRIGYVPQKlyldTTlPLTVNRFLRLRPGTK------KEDILpalKRVQ----AGHLIDAPMQKL-------SGGETQRV 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ--DYTVVIVTHNM 212
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-210 |
1.08e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFELypeQRAEGEILLDGDNILTNSQDialLR 90
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY---EVTGGTVEFKGKDLLELSPE---DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVG--MVFQKPTPFP-------MSIYDNIAFGVRLFEKLSRADMDERVQwalTKAALWNETKDKLHQS-GYSLSGGQQQ 160
Cdd:PRK09580 76 AGEGifMAFQYPVEIPgvsnqffLQTALNAVRSYRGQEPLDRFDFQDLME---EKIALLKMPEDLLTRSvNVGFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131593 161 RLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQ-DYTVVIVTH 210
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-236 |
2.34e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 25 ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFElypeqRAEGEILLDGDNILTNSQDIALL---------RAKVGM 95
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKKINNHNANEAINhgfalvteeRRSTGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 96 VFQKPTPFPmSIYDNIAFGVRLFEKLSRADMDERVQWALTKAalwnETKDKLHQSGY-SLSGGQQQRLCIARGIAIRPEV 174
Cdd:PRK10982 338 YAYLDIGFN-SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSM----RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 175 LLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNT 236
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDT 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-230 |
2.83e-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: 57.14 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 28 NINLDIAKNQVTAFIGPSGCGKSTLLRTfnkMFELYPeQRAEGEILLDGDNILTNSQDIALlRAKVGMV---FQKPTPFP 104
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQA---LFGAYP-GKFEGNVFINGKPVDIRNPAQAI-RAGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 105 -MSIYDNIAFGV-RLFEKLSRADmDERVQWALTKAAlwnetkDKLHQSGYS-------LSGGQQQRLCIARGIAIRPEVL 175
Cdd:TIGR02633 353 iLGVGKNITLSVlKSFCFKMRID-AAAELQIIGSAI------QRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 176 LLDEPCSALDPISTGRIEELITELKQD-YTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-210 |
2.86e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 28 NINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIltNSQDIALLRA------KVGMvfqKP- 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-----ARPDAGEVLWQGEPI--RRQRDEYHQDllylghQPGI---KTe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 -TPFpmsiyDNIAFGVRLFEKLSradmDERVQWALTKAALwnetkdklhqSGY------SLSGGQQQRLCIARGIAIRPE 173
Cdd:PRK13538 89 lTAL-----ENLRFYQRLHGPGD----DEALWEALAQVGL----------AGFedvpvrQLSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131593 174 VLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTH 210
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-242 |
4.35e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 7 APSKIQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTllrtfnkmfELYPEQRAEGEILLDGDNILTNSQDI 86
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R---------GALPAHV*GPDAGRRPWRF*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMvfQKPTPF----PMSIYDN---IAFGVRLFEKLSRADMDERVQ-WALTKAAlwnetkdklHQSGYSLSGGQ 158
Cdd:NF000106 81 RALRRTIG*--HRPVR*grreSFSGRENlymIGR*LDLSRKDARARADELLErFSLTEAA---------GRAAAKYSGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 159 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGRI-EELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTD 237
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
....*
gi 16131593 238 DLFTK 242
Cdd:NF000106 230 ELKTK 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-200 |
1.87e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 12 QVRNLNFY-YGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEILLDGDNIlTNsQDIALL 89
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEA------LAGLRPPAsGSIRLDGEDI-TG-LSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 90 RA-----------KVGMVfqkPTpfpMSIYDNIAFGVRLFEKLSRA---DMDERVQWALTKAALWNETKDKLHQSGYSLS 155
Cdd:COG3845 331 RRlgvayipedrlGRGLV---PD---MSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELIEEFDVRTPGPDTPARSLS 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131593 156 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELK 200
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR 449
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-217 |
3.20e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 33 IAKNQVTAFIGPSGCGKSTLLRTFnkmfelypEQRAEGEILLDgdNILTNSQDIA--LLRaKVGMVFQKPTPFP-MSIYD 109
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNAL--------AGRIQGNNFTG--TILANNRKPTkqILK-RTGFVTQDDILYPhLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 110 NIAFG--VRLFEKLSRadmDERVQWALTKAALWNETKDKLHQSGYS----LSGGQQQRLCIARGIAIRPEVLLLDEPCSA 183
Cdd:PLN03211 160 TLVFCslLRLPKSLTK---QEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|....
gi 16131593 184 LDPISTGRIEELITELKQDYTvVIVTHNMQQAAR 217
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSR 269
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-215 |
3.79e-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: 51.55 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 16 LNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMFElypeqrAEGEILLDGDniltnsqdiallrakvgm 95
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLY------ASGKARLISF------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 96 vfqKPTPFPMSIydnIAFGvrlfeKLSRadmdervqwaLTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPE-- 173
Cdd:cd03238 54 ---LPKFSRNKL---IFID-----QLQF----------LIDVGL---GYLTLGQKLSTLSGGELQRVKLASELFSEPPgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131593 174 VLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHN---MQQA 215
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSA 155
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
55-235 |
7.93e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 55 TFNKMFELYPeQRAEGEILLDGDNILTNS------QDIALL---RAKVGMVFQkptpfpMSIYDNIAFGV-RLFEKLSRA 124
Cdd:PRK13549 304 LVQCLFGAYP-GRWEGEIFIDGKPVKIRNpqqaiaQGIAMVpedRKRDGIVPV------MGVGKNITLAAlDRFTGGSRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 125 DMDERVQWAltkaalwNETKDKLH-------QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIT 197
Cdd:PRK13549 377 DDAAELKTI-------LESIQRLKvktaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131593 198 EL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGELI-EFSN 235
Cdd:PRK13549 450 QLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKgDLIN 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-210 |
9.60e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 18 FYYGKFHALKNINLDI---AKNQVtafIGPSGCGKSTLLRTfnkMFELypEQRAEGE-ILLDGdniltnsqdiallrAKV 93
Cdd:PRK11819 15 VVPPKKQILKDISLSFfpgAKIGV---LGLNGAGKSTLLRI---MAGV--DKEFEGEaRPAPG--------------IKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 94 GMVFQKPTPFP-MSIYDNIAFGVR-LFEKLSR------------ADMDE------RVQWALTKAALWN-ETK-----DKL 147
Cdd:PRK11819 73 GYLPQEPQLDPeKTVRENVEEGVAeVKAALDRfneiyaayaepdADFDAlaaeqgELQEIIDAADAWDlDSQleiamDAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 148 H-----QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELItelkQDY--TVVIVTH 210
Cdd:PRK11819 153 RcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-242 |
1.03e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 23 FHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKmfELYPeqrAEGEILLDGDniltnsqdIALLRAKVGMVFQkptp 102
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG--SLSP---TVGKVDRNGE--------VSVIAISAGLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 103 fpMSIYDNIAFGVRLF---EKLSRADMDERVQWAltkaalwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13546 100 --LTGIENIEFKMLCMgfkRKEIKAMTPKIIEFS--------ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 180 PCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTK 242
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-210 |
1.40e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 11 IQVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEqraEGEILLdGDNiltnsqdiallr 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKW-SEN------------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 91 AKVGMvfqkptpFPMSIYDNIAFGVRLFEKLSR----ADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIAR 166
Cdd:PRK15064 382 ANIGY-------YAQDHAYDFENDLTLFDWMSQwrqeGDDEQAVRGTLGRLLF---SQDDIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16131593 167 GIAIRPEVLLLDEPCSALDPIStgrIEELITELKQ-DYTVVIVTH 210
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSH 493
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-210 |
1.91e-07 |
|
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: 51.34 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 6 TAPSKIQVRNLNFYY------GKFHaLKNINLDIAKNQVTAFIGPSGCGKSTLLrtfnKMFE-LYPEQraEGEILLDGDN 78
Cdd:COG4615 323 ADFQTLELRGVTYRYpgedgdEGFT-LGPIDLTIRRGELVFIVGGNGSGKSTLA----KLLTgLYRPE--SGEILLDGQP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 79 IltNSQDIALLRAKVGMVFqkpTPFpmsiYdniafgvrLFEKL---SRADMDERVQWALTKAALwnetKDKLH-QSGY-- 152
Cdd:COG4615 396 V--TADNREAYRQLFSAVF---SDF----H--------LFDRLlglDGEADPARARELLERLEL----DHKVSvEDGRfs 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 153 --SLSGGQQQRLciARGIAI---RPeVLLLDEPCSALDPISTgRI--EELITELK-QDYTVVIVTH 210
Cdd:COG4615 455 ttDLSQGQRKRL--ALLVALledRP-ILVFDEWAADQDPEFR-RVfyTELLPELKaRGKTVIAISH 516
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-213 |
2.19e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 1 MSMVETAPS-KI--QVRNLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLL--------------RTFNKM---- 59
Cdd:PRK11147 307 MQVEEASRSgKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLklmlgqlqadsgriHCGTKLevay 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 60 F-----ELYPEQR-----AEG--EILLDGD--NILTNSQDIaLLRAKVGMvfqkpTPfpmsiydniafgvrlfeklsrad 125
Cdd:PRK11147 387 FdqhraELDPEKTvmdnlAEGkqEVMVNGRprHVLGYLQDF-LFHPKRAM-----TP----------------------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 126 mdervqwalTKAalwnetkdklhqsgysLSGGQQQRLCIARgIAIRPEVLL-LDEPCSALDpistgrIE--ELITELKQD 202
Cdd:PRK11147 438 ---------VKA----------------LSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD------VEtlELLEELLDS 485
|
250
....*....|...
gi 16131593 203 Y--TVVIVTHNMQ 213
Cdd:PRK11147 486 YqgTVLLVSHDRQ 498
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
9-210 |
2.25e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNLNFYYGK--FhALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMFelypeQRAEGEILLDGDNIltNSQDI 86
Cdd:PRK10522 321 QTLELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKPV--TAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 87 ALLRAKVGMVFQKptpfpmsiydniafgVRLFEKLsradMDERVQWALTKAA-LWNET---KDKLHQSGY-----SLSGG 157
Cdd:PRK10522 393 EDYRKLFSAVFTD---------------FHLFDQL----LGPEGKPANPALVeKWLERlkmAHKLELEDGrisnlKLSKG 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 158 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTgRI--EELITELKQ-DYTVVIVTH 210
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDPHFR-REfyQVLLPLLQEmGKTIFAISH 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-230 |
3.22e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 27 KNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmFELYPeQRAeGEILLDGDNILTNSQDIALLRAKV---------GMVF 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETL---YGLRP-ARG-GRIMLNGKEINALSTAQRLARGLVylpedrqssGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 98 QKPTPFPMS--IYDNIAFGVRlfEKLSRADMdERVQWALtkaalwNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVL 175
Cdd:PRK15439 355 DAPLAWNVCalTHNRRGFWIK--PARENAVL-ERYRRAL------NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 176 LLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHNMQQAARCSDHTAFMYLGEL 230
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-221 |
3.31e-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: 49.92 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTLLrtfNKMfeLYP--EQRAEGEILLDGdniltNSQDIALLRA--KVGMVFQK 99
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLI---NDT--LYPalARRLHLKKEQPG-----NHDRIEGLEHidKVIVIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 P---TP--------------------------------------------FPMSIYDNIAFgvrlFEKLSRadMDERVQw 132
Cdd:cd03271 79 PigrTPrsnpatytgvfdeirelfcevckgkrynretlevrykgksiadvLDMTVEEALEF----FENIPK--IARKLQ- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 133 ALTKAALwnetkD--KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALdpiSTGRIEELITEL----KQDY 203
Cdd:cd03271 152 TLCDVGL-----GyiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL---HFHDVKKLLEVLqrlvDKGN 223
|
250
....*....|....*...
gi 16131593 204 TVVIVTHNMqQAARCSDH 221
Cdd:cd03271 224 TVVVIEHNL-DVIKCADW 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-208 |
1.51e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 29 INLDIAKNQVTAFIGPSGCGKSTLLRTfnkmfeLY-PEQRAEGEILLDGDNILTNS------QDIALL---RAKVGMVfq 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKL------LYgATRRTAGQVYLDGKPIDIRSprdairAGIMLCpedRKAEGII-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 99 kptpfPM-SIYDNIA---------FGVRLFEKLSRADMDERVQwaltkaALWNETKDKlHQSGYSLSGGQQQRLCIARGI 168
Cdd:PRK11288 344 -----PVhSVADNINisarrhhlrAGCLINNRWEAENADRFIR------SLNIKTPSR-EQLIMNLSGGNQQKAILGRWL 411
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131593 169 AIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIV 208
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFV 452
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-211 |
2.78e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 8 PSKIQVRNLNFYYGKfhalKNINLDiakNQVTAFIGPSGCGKSTLLRTFNkmFELYPEQRAEGEIlldGDNILTNSQDia 87
Cdd:COG0419 2 LLRLRLENFRSYRDT----ETIDFD---DGLNLIVGPNGAGKSTILEAIR--YALYGKARSRSKL---RSDLINVGSE-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 88 llRAKVGMVFQ-KPTPF----------------PMSIYDNIA--FGVRLFEKLSR--ADMDERVQWALTKAALWNETKDK 146
Cdd:COG0419 68 --EASVELEFEhGGKRYrierrqgefaefleakPSERKEALKrlLGLEIYEELKErlKELEEALESALEELAELQKLKQE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131593 147 LHQ--SGY----SLSGGQQQRLCIARGIAirpevLLLDEpcSALDPISTGRIEELITELKqdytvvIVTHN 211
Cdd:COG0419 146 ILAqlSGLdpieTLSGGERLRLALADLLS-----LILDF--GSLDEERLERLLDALEELA------IITHV 203
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
3.98e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 3.98e-06
10 20
....*....|....*....|....*....
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTL 52
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-52 |
4.79e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 4.79e-06
10 20
....*....|....*....|....*....
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTL 52
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-71 |
1.17e-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: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTLlrTFNKMFelypeqrAEGE 71
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL--AFDTIY-------AEGQ 48
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
42-210 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 42 IGPSGCGKSTLLRTFNkmfELYPeqraegeiLLDGdnILTNSQDIALLrakvgMVFQKP----------TPFPMSIYDNI 111
Cdd:TIGR00954 484 CGPNGCGKSSLFRILG---ELWP--------VYGG--RLTKPAKGKLF-----YVPQRPymtlgtlrdqIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 112 AFGVR---LFEKLSRADMDErvqwALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPis 188
Cdd:TIGR00954 546 RRGLSdkdLEQILDNVQLTH----ILEREGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV-- 615
|
170 180
....*....|....*....|....
gi 16131593 189 tgRIEELITELKQDY--TVVIVTH 210
Cdd:TIGR00954 616 --DVEGYMYRLCREFgiTLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-185 |
1.89e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 27 KNINLDIAKNQVTAFIGPSGCGKSTLLRtfnkmfelypeqraegeiLLDGDniLTNSQDIALLRAKVGM-VFQK------ 99
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGE--LQPSSGTVFRSAKVRMaVFSQhhvdgl 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 -----PTPFPMSIYDNIAfgvrlfEKLSRADMDErvqwaltkaalWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEV 174
Cdd:PLN03073 586 dlssnPLLYMMRCFPGVP------EQKLRAHLGS-----------FGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170
....*....|.
gi 16131593 175 LLLDEPCSALD 185
Cdd:PLN03073 649 LLLDEPSNHLD 659
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-210 |
3.02e-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: 43.75 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 38 VTAFIGPSGCGKSTLLRTFNkmFELYPEQRAeGEILLDGDNILTNSQDIallRAKVGMVFQKPTPFPM------SIYDNI 111
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK--YALTGELPP-NSKGGAHDPKLIREGEV---RAQVKLAFENANGKKYtitrslAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 112 AFgVRlfeklsradmDERVQWALTkaalwnETKDklhqsgySLSGGQQQ------RLCIARGIAIRPEVLLLDEPCSALD 185
Cdd:cd03240 98 IF-CH----------QGESNWPLL------DMRG-------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*...
gi 16131593 186 PIS-TGRIEELITELKQDYT--VVIVTH 210
Cdd:cd03240 154 EENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-212 |
3.40e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131593 154 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNM 212
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
152-221 |
3.82e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131593 152 YSLSGGQQQRLCIARGI---AIRPEVLLLDEPCSALdpiSTGRIEELITELK----QDYTVVIVTHNMqQAARCSDH 221
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVADY 880
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-210 |
4.58e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 143 TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIteLKQDYTVVIVTH 210
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-241 |
5.41e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 21 GKFH-ALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDniltnsqdIALLRAKVGMVFQk 99
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV-----TMPNKGTVDIKGS--------AALIAISSGLNGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 100 ptpfpMSIYDNIAFgvrlfEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13545 100 -----LTGIENIEL-----KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 180 PCSALDPISTGRIEELITELK-QDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFT 241
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
9-60 |
7.76e-05 |
|
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: 43.36 E-value: 7.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 16131593 9 SKIQVRNlnfyygkFHALKNINLDIaKNQVTAFIGPSGCGKSTLLRTFNKMF 60
Cdd:pfam13175 4 KSIIIKN-------FRCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIFL 47
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-235 |
7.95e-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: 41.59 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 35 KNQVTAFIGPSGCGKSTLLRTFNKMFelypEQRAEGEILLDGDNILTNSQDIALLrakvgmvfqkptpfpmsiydniafg 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL----GPPGGGVIYIDGEDILEEVLDQLLL------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 115 vrlfeklsradmdervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEE 194
Cdd:smart00382 52 ------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131593 195 LIT------ELKQDYTVVIVTHNMQQAARcsDHTAFMYLGELIEFSN 235
Cdd:smart00382 102 LEElrllllLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLL 146
|
|
| 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 16131593 146 KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALdpiSTGRIEELITEL----KQDYTVVIVTHNM 212
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL---HFDDIKKLLEVLqrlvDKGNTVVVIEHNL 892
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-185 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFnkmfelypeqraEGEILLDGDNIlTNSQDIALlrakvGMVFQKPTPFPM 105
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALL------------KNEISADGGSY-TFPGNWQL-----AWVNQETPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 106 SIYDNIAFGVRLFEKLSRA------------------DMDERVQWALTK--AALWNE---TKDKLHQSGYSLSGGQQQRL 162
Cdd:PRK10636 79 PALEYVIDGDREYRQLEAQlhdanerndghaiatihgKLDAIDAWTIRSraASLLHGlgfSNEQLERPVSDFSGGWRMRL 158
|
170 180
....*....|....*....|...
gi 16131593 163 CIARGIAIRPEVLLLDEPCSALD 185
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
154-226 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131593 154 LSGGQQQR--LCIARGIA-IRPEVL-LLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTHNMQQAARcSDHTAFMY 226
Cdd:cd03227 78 LSGGEKELsaLALILALAsLKPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
147-225 |
1.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 147 LHQSGYSLSGGQQQRLCIARGIAIRPE--VLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAF 224
Cdd:PRK00635 1381 LGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIH 1460
|
.
gi 16131593 225 M 225
Cdd:PRK00635 1461 L 1461
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
9-56 |
4.43e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 4.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 16131593 9 SKIQVRNlnfyygkFHALKNINLDIAknQVTAFIGPSGCGKSTLLRTF 56
Cdd:COG4637 3 TRIRIKN-------FKSLRDLELPLG--PLTVLIGANGSGKSNLLDAL 41
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
35-72 |
4.58e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.57 E-value: 4.58e-04
10 20 30
....*....|....*....|....*....|....*....
gi 16131593 35 KNQVTAFIGPSGCGKSTLLrtfNKmfeLYPEQRAE-GEI 72
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLL---NA---LAPDLELKtGEI 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-226 |
5.12e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 40.43 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 37 QVTAFIGPSGCGKSTLLRTFNKmfELYPE-QRAEGEIllDGDNILTNSQDIAL------LRAKVGMVFQKPtpfpmSIYD 109
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAG--KLKPNlGKFDDPP--DWDEILDEFRGSELqnyftkLLEGDVKVIVKP-----QYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 110 NI--AFGVRLFEKLSRADmdERVQWALTKAALwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD-- 185
Cdd:cd03236 98 LIpkAVKGKVGELLKKKD--ERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131593 186 -PISTGR-IEELITELKqdyTVVIVTHNMQQAARCSDHTAFMY 226
Cdd:cd03236 174 qRLNAARlIRELAEDDN---YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
9-221 |
5.46e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNlnfyygkFHALKNINLDIAKnqVTAFIGPSGCGKST------LLRTFNKMF---------ELYPEQRAE---- 69
Cdd:COG4938 2 KSISIKN-------FGPFKEAELELKP--LTLLIGPNGSGKSTliqallLLLQSNFIYlpaersgpaRLYPSLVRElsdl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 70 ---GEILLDgdnILTNSQDIALLRAKvgmvfqkptpfPMSIYDNIAfgvRLFEKLSRADMD---ERVQWALTKAALWNET 143
Cdd:COG4938 73 gsrGEYTAD---FLAELENLEILDDK-----------SKELLEQVE---EWLEKIFPGKVEvdaSSDLVRLVFRPSGNGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 144 KDKLHQSGYslsgGQQQRLCI---ARGIAIRPEVLLLDEPCSALDPISTGRIEELITEL-KQDYTVVIVTHnmqqaarcS 219
Cdd:COG4938 136 RIPLSNVGS----GVSELLPIllaLLSAAKPGSLLIIEEPEAHLHPKAQSALAELLAELaNSGVQVIIETH--------S 203
|
..
gi 16131593 220 DH 221
Cdd:COG4938 204 DY 205
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-53 |
6.08e-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: 6.08e-04
10 20 30
....*....|....*....|....*....|
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTLL 53
Cdd:TIGR00630 622 NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| 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 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITE-LKQDYTVVIVTHNMQQAARCSDHTAFMYLG 228
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-179 |
8.54e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 26 LKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMfelypEQRAEGEILLDGDNIlTNSQD--IALLRAKVGMVFQkptpf 103
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGI-----MQPSSGNIYYKNCNI-NNIAKpyCTYIGHNLGLKLE----- 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 104 pMSIYDNIAFGVRLFeklsraDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:PRK13541 85 -MTVFENLKFWSEIY------NSAETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-212 |
8.58e-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: 40.15 E-value: 8.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131593 153 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgRIE--ELITEL-KQDYTVVIVTHNM 212
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IYQ-RLNvaRLIRELaEEGKYVLVVEHDL 272
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
35-72 |
2.00e-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: 2.00e-03
10 20 30
....*....|....*....|....*....|....*....
gi 16131593 35 KNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEI 72
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNA------LLPELDLRtGEI 137
|
|
| 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 16131593 35 KNQVTAFIGPSGCGKSTLLRTfnkmfeLYPEQRAE-GEI 72
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNA------LLPELVLAtGEI 116
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-213 |
2.78e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131593 153 SLSGGQQQRLCIAR--GIAIRPEVLLLDEPCSALDPISTGRIEELITELK-QDYTVVIVTHNMQ 213
Cdd:PRK00635 476 TLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQ 539
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
153-180 |
3.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 3.29e-03
10 20
....*....|....*....|....*...
gi 16131593 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 |
3.88e-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: 38.14 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 73 LLDGDNILTNSQDIALLRAKVGMVFQKPTPFP---MSIYDNIAFGVRLFEKLSRADMDERVQWaLTKAALWNETKDKLHQ 149
Cdd:pfam13304 154 LLLLDEGLLLEDWAVLDLAADLALFPDLKELLqrlVRGLKLADLNLSDLGEGIEKSLLVDDRL-RERGLILLENGGGGEL 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131593 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 |
3.89e-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: 38.23 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 32 DIAKNQVTAFIGPSGCGKSTllrtFNKMF--ELYPEqraEGEILLDGDnI------LTNSQDI---ALLRAKVGmvfqkp 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT----FAKILagVLKPD---EGEVDEDLK-IsykpqyISPDYDGtveEFLRSANT------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 101 TPFPMSIYDN-IAFGVRLfEKLsradMDERVQwaltkaalwnetkdklhqsgySLSGGQQQRLCIARGIAIRPEVLLLDE 179
Cdd:COG1245 428 DDFGSSYYKTeIIKPLGL-EKL----LDKNVK---------------------DLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131593 180 PCSALD---PISTGRIEELITElKQDYTVVIVTHNMQ 213
Cdd:COG1245 482 PSAHLDveqRLAVAKAIRRFAE-NRGKTAMVVDHDIY 517
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
9-54 |
4.56e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 4.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16131593 9 SKIQVRNlnfyygkFHALKNINLDIAKNqVTAFIGPSGCGKSTLLR 54
Cdd:COG3593 4 EKIKIKN-------FRSIKDLSIELSDD-LTVLVGENNSGKSSILE 41
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
37-139 |
5.15e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.17 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 37 QVTAFIGPSGCGKSTLLRTFnkmFELYPEQRAEGeILLDgdniLTNSQDIALLRAKVgmvfqkptpfpmsiydNIAFGVR 116
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRL---LEQLPEVRDSV-VFVD----LPSGTSPKDLLRAL----------------LRALGLP 61
|
90 100
....*....|....*....|...
gi 16131593 117 LFEKLSRADMDERVQWALTKAAL 139
Cdd:pfam13401 62 LSGRLSKEELLAALQQLLLALAV 84
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
7.46e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 7.46e-03
10 20
....*....|....*....|....*....
gi 16131593 24 HALKNINLDIAKNQVTAFIGPSGCGKSTL 52
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
9-68 |
9.58e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131593 9 SKIQVRNlnfyYGKFHALKninLDIAKNQVTAFIGPSGCGKSTLLRTFnkMFELYPEQRA 68
Cdd:pfam13555 2 TRLQLIN----WGTFDGHT---IPIDPRGNTLLTGPSGSGKSTLLDAI--QTLLVPAKRA 52
|
|
| |
