|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-258 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 540.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSMVTDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNI 80
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LTDNSDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQ 160
Cdd:COG1117 81 YDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
250
....*....|....*...
gi 1875943321 241 FTAPQKKQTEDYITGRYG 258
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
11-257 |
1.15e-164 |
|
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: 455.22 E-value: 1.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDNSDIALL 90
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTE 250
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 1875943321 251 DYITGRY 257
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-238 |
1.12e-144 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 403.87 E-value: 1.12e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHqsGYSLSGGQQQRLCIARGIAI 171
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 172 RPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTD 238
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-258 |
4.57e-129 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 366.03 E-value: 4.57e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 5 TDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDN 84
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 85 SDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLC 164
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARI--NGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFM---------YLGELIEFS 235
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFD 241
|
250 260
....*....|....*....|...
gi 1875943321 236 DTDNLFTAPQKKQTEDYITGRYG 258
Cdd:PRK14243 242 RTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-258 |
2.84e-118 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 338.29 E-value: 2.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 171
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 172 RPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTED 251
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 1875943321 252 YITGRYG 258
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-258 |
2.24e-103 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 300.61 E-value: 2.24e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKL--SRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKL-NGLvkSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQ 248
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEL 243
|
250
....*....|
gi 1875943321 249 TEDYITGRYG 258
Cdd:PRK14267 244 TEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-256 |
1.76e-97 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 285.65 E-value: 1.76e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILtdNSDIAL 89
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKL-SRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPnLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKK 247
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*....
gi 1875943321 248 QTEDYITGR 256
Cdd:PRK14247 240 LTEKYVTGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-258 |
3.84e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 272.30 E-value: 3.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAI 171
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 172 RPEVLLLDEPCSALDPISTGKIEELIS--ELKADYTVVIVTHNMQQAARCSDSTAFMY-----LGELIEFSDTDNLFTAP 244
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 1875943321 245 QKKQTEDYITGRYG 258
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-253 |
8.74e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 224.87 E-value: 8.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyQLypEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCIN---LL--EEPDSGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQT 249
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
....
gi 1875943321 250 EDYI 253
Cdd:COG1126 233 RAFL 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-258 |
4.77e-71 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 219.20 E-value: 4.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 6 DASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILtDNS 85
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIF-NYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCI 165
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
250
....*....|...
gi 1875943321 246 KKQTEDYITGRYG 258
Cdd:PRK14271 255 HAETARYVAGLSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-256 |
1.76e-69 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 214.53 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQ-RAEGGILLDGQNILtdNSDIALLRAKVGMVFQKPTPFP 105
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKiKVDGKVLYFGKDIF--QIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 -MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 184
Cdd:PRK14246 104 hLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 185 LDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTEDYITGR 256
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIGR 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-226 |
2.23e-67 |
|
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: 207.77 E-value: 2.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFM 226
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFM 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-245 |
1.14e-65 |
|
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: 212.46 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-DNS 85
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL-----LRPTSGSILFDGKDLTKlSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKL-HQsgysLSGGQQ 160
Cdd:COG1123 336 SLRELRRRVQMVFQDPYsslnPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHE----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTD 238
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
....*..
gi 1875943321 239 NLFTAPQ 245
Cdd:COG1123 491 EVFANPQ 497
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-248 |
4.53e-65 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 202.35 E-value: 4.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQRaeGGILLDGQNIlTDNSDIAL-- 89
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPDS--GEVLIDGEDI-SGLSEAELyr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:cd03261 75 LRRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTA--P 244
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASddP 230
|
....
gi 1875943321 245 QKKQ 248
Cdd:cd03261 231 LVRQ 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-246 |
3.29e-64 |
|
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: 199.87 E-value: 3.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNIltDNSDIALL 90
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDI--TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:COG1122 74 RRKVGLVFQNPDDqlFAPTVEEDVAFGPENL-GLPREEIRERVEEALELVGLE----HLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQK 246
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-244 |
7.71e-64 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 199.44 E-value: 7.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 7 ASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPEqraEGGILLDGQNILT-DNS 85
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI--IGLLRPD---SGEILVDGQDITGlSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQRL 163
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMpSE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
...
gi 1875943321 242 TAP 244
Cdd:COG1127 231 ASD 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-230 |
3.11e-62 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 193.17 E-value: 3.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-----EEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIA 170
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFMYLGE 230
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-245 |
1.25e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.24 E-value: 1.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSMvtdassSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRT---FnkmyqlypEQRAEGGILLDG 77
Cdd:COG3842 1 MAM------PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagF--------ETPDSGRILLDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 78 QniltdnsDIALLRA---KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALtkaalwnetkDKLHQSGY 153
Cdd:COG3842 67 R-------DVTGLPPekrNVGMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIRARVAELL----------ELVGLEGL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 S------LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistgKI-EELISELKA-----DYTVVIVTHNMQQAARCSD 221
Cdd:COG3842 129 AdryphqLSGGQQQRVALARALAPEPRVLLLDEPLSALDA----KLrEEMREELRRlqrelGITFIYVTHDQEEALALAD 204
|
250 260
....*....|....*....|....
gi 1875943321 222 STAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:COG3842 205 RIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-234 |
2.63e-59 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 186.96 E-value: 2.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdnSDIALLR 91
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 170
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-246 |
4.53e-59 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 195.12 E-value: 4.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyQLYPEQ-RAEGGILLDGQNILTdnSDIA 88
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM---GLLPHGgRISGEVLLDGRDLLE--LSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIA 166
Cdd:COG1123 80 LRGRRIGMVFQDPMTqlNPVTVGDQIAEALENL-GLSRAEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
..
gi 1875943321 245 QK 246
Cdd:COG1123 235 QA 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-231 |
1.27e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.02 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltDNSDIALLR 91
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP-----TSGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFPMSIYDNIAFGVRLFEKlsRADMdERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAI 171
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRER--KFDR-ERALELLERLGL---PPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 172 RPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-240 |
5.95e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.11 E-value: 5.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNILTDNSDIallR 91
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-----SGEVRVLGEDVARDPAEV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLY-GLPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
2.37e-57 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 183.37 E-value: 2.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSmvtdASSSKIQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLD 76
Cdd:COG1116 1 MS----AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRL---IAGL--EKPTSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 77 GQniltdnsDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwNETKDKL-HQsgys 154
Cdd:COG1116 72 GK-------PVTGPGPDRGVVFQEPALLPwLTVLDNVALGLEL-RGVPKAERRERARELLELVGL-AGFEDAYpHQ---- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSD 221
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLAD 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-226 |
3.47e-57 |
|
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: 181.51 E-value: 3.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFH--ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltDNSDIALL 90
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDL--TKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKP-TPFPM-SIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:cd03225 74 RRKVGLVFQNPdDQFFGpTVEEEVAFGLENL-GLPEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFM 226
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-245 |
2.39e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 178.42 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLDGQNILTDnsdIALLR 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRI---IAGL--ETPDSGRIVLNGRDLFTN---LPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERV-QWaLTKAALwnetkDKL-----HQsgysLSGGQQQRLC 164
Cdd:COG1118 75 RRVGFVFQHYALFPhMTVAENIAFGLRV-RPPSKAEIRARVeEL-LELVQL-----EGLadrypSQ----LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFT 242
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
...
gi 1875943321 243 APQ 245
Cdd:COG1118 224 RPA 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-245 |
3.64e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 177.17 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQRAEGG-ILLDGQNILT-DNS 85
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARA---ILGLLPPPGITSGeILFDGEDLLKlSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAK-VGMVFQKPT----PFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL----HQsgysLS 156
Cdd:COG0444 79 ELRKIRGReIQMIFQDPMtslnPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLdrypHE----LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250
....*....|.
gi 1875943321 235 SDTDNLFTAPQ 245
Cdd:COG0444 233 GPVEELFENPR 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-246 |
3.96e-54 |
|
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: 175.72 E-value: 3.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILTDNS- 85
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITAKKKk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRL 163
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGL---DEEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
....*
gi 1875943321 242 TAPQK 246
Cdd:TIGR04521 232 SDVDE 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-243 |
9.24e-54 |
|
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: 174.08 E-value: 9.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyQLYPeqrAEGGILLDGQNILT-DNSDIAll 90
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKP---SSGEVLLDGRDLASlSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 rAKVGMVFQKPT-PFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCI 165
Cdd:COG1120 75 -RRIAYVPQEPPaPFGLTVRELVALGryphLGLFGRPSAED-REAVEEALERTGLE----HLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTA 243
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-244 |
2.13e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 176.03 E-value: 2.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLDGQNIlTDnsdial 89
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRM---IAGL--EDPTSGEILIGGRDV-TD------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALtkaalwnetkDKLHQSGY------SLSGGQ 159
Cdd:COG3839 70 LPPKdrnIAMVFQSYALYPhMTVYENIAFPLKL-RKVPKAEIDRRVREAA----------ELLGLEDLldrkpkQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPistgKI-EELISELKA-----DYTVVIVTHNMQQAARCSDSTAFMYLGELIE 233
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDA----KLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQ 214
|
250
....*....|.
gi 1875943321 234 FSDTDNLFTAP 244
Cdd:COG3839 215 VGTPEELYDRP 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-234 |
4.27e-53 |
|
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: 171.53 E-value: 4.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLDGQNILT-DNSD 86
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARA---ILGL--LKPTSGSIIFDGKDLLKlSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAAlwNETKDKLHQSGYSLSGGQQQR 162
Cdd:cd03257 77 RKIRRKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-231 |
4.38e-53 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 171.13 E-value: 4.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG----KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI--LTDNS 85
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-----DRPTSGEVRVDGTDIskLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 164
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPL-LLAGVPKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCsDSTAFMYLGEL 231
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYA-DRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-245 |
6.03e-53 |
|
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: 171.91 E-value: 6.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRT---FNKMYQlypeqraeGGILLDGQNIltDN 84
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRAlagLERPWS--------GEVTFDGRPV--TR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 85 SDIALLRAKVGMVFQKPT----PFpMSIYDNIAFGVRLfekLSRADMDERVQWALTKAALWNETKDKL-HQsgysLSGGQ 159
Cdd:COG1124 72 RRRKAFRRRVQMVFQDPYaslhPR-HTVDRILAEPLRI---HGLPDREERIAELLEQVGLPPSFLDRYpHQ----LSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDT 237
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
....*...
gi 1875943321 238 DNLFTAPQ 245
Cdd:COG1124 224 ADLLAGPK 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-221 |
6.38e-53 |
|
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: 170.73 E-value: 6.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG----KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLR---TFnkmyqlypEQRAEGGILLDGQniltdn 84
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiaGL--------ERPTSGEVLVDGE------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 85 sDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwNETKDKL-HQsgysLSGGQQQR 162
Cdd:cd03293 67 -PVTGPGPDRGYVFQQDALLPwLTVLDNVALGLEL-QGVPKAEARERAEELLELVGL-SGFENAYpHQ----LSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSD 221
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLAD 200
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-233 |
7.67e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.99 E-value: 7.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG----KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLR--------TfnkmyqlypeqraEGGILLDGQN 79
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilggldrpT-------------SGEVLIDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 80 ILT-DNSDIALLRA-KVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLS 156
Cdd:COG1136 72 ISSlSERELARLRRrHIGFVFQFFNLLPeLTALENVALPLLL-AGVSRKERRERARELLERVGL----GDRLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCsDSTAFMYLGELIE 233
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAARA-DRVIRLRDGRIVS 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-183 |
5.93e-52 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 165.90 E-value: 5.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNILTDnsDIALLRAKVGMVFQKPTPFP- 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-----TEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 106 MSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 183
Cdd:pfam00005 74 LTVRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-253 |
6.88e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 171.80 E-value: 6.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyQLypEQRAEGGILLDGQNILT-DNSD 86
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN---LL--ERPTSGSVLVDGVDLTAlSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKptpFP-MS---IYDNIAFGVRLfEKLSRADMDERVqwaltkaalwNET------KDKLHQsgY--S 154
Cdd:COG1135 77 LRAARRKIGMIFQH---FNlLSsrtVAENVALPLEI-AGVPKAEIRKRV----------AELlelvglSDKADA--YpsQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
250 260
....*....|....*....|.
gi 1875943321 233 EFSDTDNLFTAPQKKQTEDYI 253
Cdd:COG1135 221 EQGPVLDVFANPQSELTRRFL 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-219 |
2.31e-51 |
|
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: 165.25 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG--KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIltDNSDIAL 89
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 169
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA 161
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-245 |
1.02e-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: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG----KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI-LTDNSD 86
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGTDLtLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKptpFPM----SIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 162
Cdd:cd03258 77 LRKARRRIGMIFQH---FNLlssrTVFENVALPLEI-AGVPKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 1875943321 241 FTAPQ 245
Cdd:cd03258 229 FANPQ 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-245 |
1.66e-50 |
|
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: 165.10 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRT---FnkmyqlypEQRAEGGILLDGQNILtdnsDIA 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLiagF--------ETPTSGEILLDGKDIT----NLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 167
Cdd:cd03300 69 PHKRPVNTVFQNYALFPhLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPistgKI-EELISELKA-----DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDL----KLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
....
gi 1875943321 242 TAPQ 245
Cdd:cd03300 220 EEPA 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-253 |
3.37e-50 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 164.78 E-value: 3.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNILtdNSDIALL 90
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE--PT---SGEIFIDGEDIR--EQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSRADMDERVQWALTKAALwnETKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIAL-VPKLLKWPKEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKK 247
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*.
gi 1875943321 248 QTEDYI 253
Cdd:cd03295 231 FVAEFV 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-219 |
6.42e-50 |
|
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: 173.87 E-value: 6.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFH--ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIltDNSDIAL 89
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDL--RQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQQR 162
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLG------DPDAT-DEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQR 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-253 |
7.28e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 163.73 E-value: 7.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIALLR 91
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:PRK09493 77 QEAGMVFQQFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 IRPEVLLLDEPCSALDPistgkieELISE-LK-----AD--YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFT 242
Cdd:PRK09493 153 VKPKLMLFDEPTSALDP-------ELRHEvLKvmqdlAEegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
250
....*....|.
gi 1875943321 243 APQKKQTEDYI 253
Cdd:PRK09493 226 NPPSQRLQEFL 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-253 |
4.78e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 161.72 E-value: 4.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlypeqraeggiLLD----GQNILTDNS-- 85
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN---------------LLEtpdsGQLNIAGHQfd 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 --------DIALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSL 155
Cdd:COG4161 68 fsqkpsekAIRLLRQKVGMVFQQYNLWPhLTVMENlIEAPCKVL-GLSKEQAREKAMKLLARLRL----TDKADRFPLHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 156 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
250
....*....|....*....
gi 1875943321 235 SDTdNLFTAPQKKQTEDYI 253
Cdd:COG4161 223 GDA-SHFTQPQTEAFAHYL 240
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
12-244 |
7.03e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 163.34 E-value: 7.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLN-FYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNILTdnSDIALL 90
Cdd:COG1125 2 IEFENVTkRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEP-----TSGRILIDGEDIRD--LDPVEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNET-KDKL-HQsgysLSGGQQQRLCIAR 167
Cdd:COG1125 75 RRRIGYVIQQIGLFPhMTVAENIATVPRL-LGWDKERIRARVDELLELVGLDPEEyRDRYpHE----LSGGQQQRVGVAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:COG1125 150 ALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-211 |
1.86e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.42 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNIltdnSDIAL- 89
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD--PT---SGRILIDGVDI----RDLTLe 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 -LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALW---NETKDKLH----QSGYSLSGGQQ 160
Cdd:COG1132 411 sLRRQIGVVPQDTFLFSGTIRENIRYG--------RPDAtDEEVEEAAKAAQAHefiEALPDGYDtvvgERGVNLSGGQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-214 |
1.28e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.52 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNILT-DNSDIA 88
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKL------LYGEERPTSGqVLVNGQDLSRlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKptpFP----MSIYDNIAFGVRLFEKlSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 164
Cdd:COG2884 76 YLRRRIGVVFQD---FRllpdRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQ 214
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLE 198
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-254 |
1.66e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.87 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI----LTDNSDI 87
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNHFdfskTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTPFP-MSIYDN-IAFGVRLFeKLSRADMDERVQWALTKAALwNETKDK--LHqsgysLSGGQQQRL 163
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNlIEAPCRVL-GLSKDQALARAEKLLERLRL-KPYADRfpLH-----LSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNlFT 242
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FT 229
|
250
....*....|..
gi 1875943321 243 APQKKQTEDYIT 254
Cdd:PRK11124 230 QPQTEAFKNYLS 241
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-240 |
1.30e-46 |
|
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: 156.05 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILTDnSDIAL 89
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDE-ENLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfE--KLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSG 157
Cdd:TIGR04520 75 IRKKVGMVFQNP--------DNqfvgatveddVAFGL---EnlGVPREEMRKRVDEALKLVGME----DFRDREPHLLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 158 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARcSDSTAFMYLGELIE-- 233
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAeg 218
|
250
....*....|..
gi 1875943321 234 -----FSDTDNL 240
Cdd:TIGR04520 219 tpreiFSQVELL 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-244 |
1.75e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQniltdnsDIALLR 91
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-----SGTVRLFGK-------PPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPT---PFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLC 164
Cdd:COG1121 75 RRIGYVPQRAEvdwDFPITVRDVVLMGrygrRGLFRRPSRAD-REAVDEALERVGLE----DLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMyLGELIEFSDTDNLFTA 243
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
.
gi 1875943321 244 P 244
Cdd:COG1121 229 E 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-232 |
1.00e-45 |
|
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: 152.98 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNILTDNSD-IAll 90
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR--P---TSGSVLFDGEDITGLPPHeIA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLS---------RADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQ 160
Cdd:cd03219 74 RLGIGRTFQIPRLFPeLTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLA----DLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-240 |
2.68e-45 |
|
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: 159.54 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 4 VTDASSSKIQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIlt 82
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 DNSDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsRADmDERVQWALTKAALWNETKD-------KLHQSGYSL 155
Cdd:COG4988 402 SDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP------DAS-DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 156 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIEFS 235
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA-DRILVLDDGRIVEQG 553
|
....*
gi 1875943321 236 DTDNL 240
Cdd:COG4988 554 THEEL 558
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-221 |
3.01e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 152.13 E-value: 3.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNF-YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNILTDN-SDIAL 89
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGEILVDGQDVTALRgRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKptpFP----MSIYDNIAFGvRL---------FEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLS 156
Cdd:COG3638 78 LRRRIGMIFQQ---FNlvprLSVLTNVLAG-RLgrtstwrslLGLFPPEDR-ERALEALERVGL----ADKAYQRADQLS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSD 221
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-253 |
3.52e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.57 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-DNSD 86
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQDLTAlSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKptpFPM----SIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 162
Cdd:PRK11153 77 LRKARRQIGMIFQH---FNLlssrTVFDNVALPLEL-AGTPKAEIKARVTELLELVGL----SDKADRYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
250
....*....|...
gi 1875943321 241 FTAPQKKQTEDYI 253
Cdd:PRK11153 229 FSHPKHPLTREFI 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-233 |
1.43e-44 |
|
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: 150.39 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILTDNSDialLR 91
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL--LKPD---SGSILIDGEDVRKEPRE---AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPtPFP--MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGI 169
Cdd:COG4555 74 RQIGVLPDER-GLYdrLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIE 233
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-245 |
2.25e-44 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 149.80 E-value: 2.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQniltDNSDIALLR 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGE----DATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRL---FEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 167
Cdd:cd03296 74 RNVGFVFQHYALFRhMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ----LSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDpistGKI-EELISEL-----KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALD----AKVrKELRRWLrrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
....
gi 1875943321 242 TAPQ 245
Cdd:cd03296 226 DHPA 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-231 |
2.91e-44 |
|
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: 147.16 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNILTDNSDIallR 91
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKKEPEEV---K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgySLSGGQQQRLCIARGIA 170
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENL-----------------------------------------KLSGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADY-TVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-255 |
3.27e-44 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 150.10 E-value: 3.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNI--LTDNSDIALLRAKVGMVFQKPTP 103
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--P---TSGKVLIDGQDIaaMSRKELRELRRKKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 FP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 182
Cdd:cd03294 114 LPhRTVLENVAFGLEV-QGVPRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 183 SALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTEDYITG 255
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-230 |
3.71e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 146.24 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNILTDnsDIALLRA 92
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKL--PLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 KVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAIR 172
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 173 PEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGE 230
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-237 |
4.50e-44 |
|
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: 148.35 E-value: 4.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPeqRAEGGILLDGQNIlTDNSDIALLR 91
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKT---IMGLLP--PRSGSIRFDGRDI-TGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfekLSRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:cd03224 75 AGIGYVPEGRRIFPeLTVEENLLLGAYA---RRRAKRKARLERVY---ELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGElIEFSDT 237
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGR-VVLEGT 215
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
26-255 |
6.19e-44 |
|
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: 151.93 E-value: 6.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNIlTDNSDIALL---RAKVGMVFQKPT 102
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIE--P---TAGQIFIDGENI-MKQSPVELRevrRKKIGMVFQQFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 103 PFP-MSIYDNIAFGVrlfeKLSRADMDERVQWALTKAALWNeTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 181
Cdd:TIGR01186 82 LFPhMTILQNTSLGP----ELLGWPEQERKEKALELLKLVG-LEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 182 CSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTEDYITG 255
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-253 |
6.52e-44 |
|
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: 148.25 E-value: 6.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHaLKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTDNSDiallR 91
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK--PDS---GKILLNGKDITNLPPE----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVqwaLTKAALWNETKdKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKK-RKVDKKEIERKV---LEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQ 248
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*
gi 1875943321 249 TEDYI 253
Cdd:cd03299 226 VAEFL 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-245 |
8.40e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 148.80 E-value: 8.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 5 TDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-- 82
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL-----ETPDSGEIRVGGEEIRLkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 ---------DNSDIALLRAKVGMVFQKptpFP----MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWnetkDKLH 149
Cdd:COG4598 77 drdgelvpaDRRQLQRIRTRLGMVFQS---FNlwshMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA----DKRD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 150 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistgkieELISE-LK-----AD--YTVVIVTHNMQQAARCSD 221
Cdd:COG4598 150 AYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmrdlAEegRTMLVVTHEMGFARDVSS 222
|
250 260
....*....|....*....|....
gi 1875943321 222 STAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:COG4598 223 HVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-231 |
2.03e-43 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 146.25 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQniltdnsDIALLR 91
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGGR-------DVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AK---VGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIAR 167
Cdd:cd03301 69 PKdrdIAMVFQNYALYPhMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDpistGKI-EELISELKA-----DYTVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLD----AKLrVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-255 |
4.12e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 147.04 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlYPEQRAEGGILLDGQNI------- 80
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCIN-----FLEKPSEGSIVVNGQTInlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 ----LTDNSDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetkDKLHQSGY-- 153
Cdd:PRK10619 77 gqlkVADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI-----DERAQGKYpv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250 260
....*....|....*....|...
gi 1875943321 233 EFSDTDNLFTAPQKKQTEDYITG 255
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-243 |
4.22e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.10 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 3 MVTDASSSK--IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI 80
Cdd:PRK09452 4 LNKQPSSLSplVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDGQDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 ltdnSDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQ 159
Cdd:PRK09452 79 ----THVPAENRHVNTVFQSYALFPhMTVFENVAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQ----LSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDpistGKI-EELISELKA-----DYTVVIVTHNMQQAARCSDSTAFMYLGElIE 233
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD----YKLrKQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDGR-IE 224
|
250
....*....|....*...
gi 1875943321 234 --------FSDTDNLFTA 243
Cdd:PRK09452 225 qdgtpreiYEEPKNLFVA 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-253 |
1.34e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 145.28 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNfyyGKFHA---LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQNILT-DNS 85
Cdd:PRK11264 2 SAIEVKNLV---KKFHGqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklhQSGY--SLSGGQQQR 162
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK------ETSYprRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
250
....*....|..
gi 1875943321 242 TAPQKKQTEDYI 253
Cdd:PRK11264 233 ADPQQPRTRQFL 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-215 |
6.72e-42 |
|
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: 142.29 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPeqrAEGGILLDGQNIltdnsdiALLRA 92
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--LGLLKP---TSGSIRVFGKPL-------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 KVGMVFQK---PTPFPMSIYDNIAFG----VRLFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCI 165
Cdd:cd03235 69 RIGYVPQRrsiDRDFPISVRDVVLMGlyghKGLFRRLSKADK-AKVDEALERVGL----SELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQ 215
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGL 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-245 |
1.32e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.87 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-----------GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNI 80
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--P---TSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LT-DNSDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKL-HQsgy 153
Cdd:COG4608 83 TGlSGRELRPLRRRMQMVFQDP--YaslnPrMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYpHE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 sLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpIStgkIE----ELISELKADY--TVVIVTHNMQQAARCSDSTAFMY 227
Cdd:COG4608 158 -FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMY 232
|
250
....*....|....*...
gi 1875943321 228 LGELIEFSDTDNLFTAPQ 245
Cdd:COG4608 233 LGKIVEIAPRDELYARPL 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-253 |
1.40e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 146.13 E-value: 1.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQniltDNSDIALLR 91
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGV----DLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 170
Cdd:PRK11607 91 RPINMMFQSYALFPhMTVEQNIAFGLKQ-DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIE-ELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQ 248
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQlEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
....*
gi 1875943321 249 TEDYI 253
Cdd:PRK11607 246 SAEFI 250
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-233 |
1.93e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 149.15 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTDNSDIal 89
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--PQS---GSITLGGVDLRDLDEDD-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAAL--WNETKDK-----LHQSGYSLSGGQQQR 162
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLA------RPDAT-DEELWAALERVGLgdWLAALPDgldtwLGEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIE 233
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-253 |
1.98e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.82 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHalKNITLDIAKNKVTAFIGPSGCGKSTLLRT---FnkmyqlypEQRAEGGILLDGQNILTDNSDia 88
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLiagF--------LPPDSGRILWNGQDLTALPPA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:COG3840 70 --ERPVSMLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGL----AGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 giAI---RPeVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFT 242
Cdd:COG3840 143 --CLvrkRP-ILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|.
gi 1875943321 243 APQKKQTEDYI 253
Cdd:COG3840 220 GEPPPALAAYL 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-226 |
2.13e-41 |
|
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: 145.18 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdnSDI 87
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGGRDI----TRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNeTKDKlhqsgY--SLSGGQQQRLC 164
Cdd:TIGR03265 72 PPQKRDYGIVFQSYALFPnLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPG-SERK-----YpgQLSGGQQQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDpistGKI-EELISELKA-----DYTVVIVTHNMQQAARCSDSTAFM 226
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-244 |
9.20e-41 |
|
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: 142.63 E-value: 9.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 43 IGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdnSDIALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEK 121
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGF-----EQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKM-RK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 122 LSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPistgKIEELIS-EL 200
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDK----KLRDQMQlEL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 201 KA-----DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:TIGR01187 144 KTiqeqlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-233 |
3.55e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 9 SSKIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQnILTDNS- 85
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPEA---GTITVGGM-VLSEETv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 -DIallRAKVGMVFQKP-TPF-PMSIYDNIAFGVrlfEK--LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQ 160
Cdd:PRK13635 77 wDV---RRQVGMVFQNPdNQFvGATVQDDVAFGL---ENigVPREEMVERVDQALRQVGM----EDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPIstGKIE--ELISELKA--DYTVVIVTHNMQQAARcSDSTAFMYLGELIE 233
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKEqkGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-232 |
4.84e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.80 E-value: 4.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK---FH--ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTDNSD 86
Cdd:PRK13637 3 IKIENLTHIYMEgtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKP---TSGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAAL-WNETKDKlhqSGYSLSGGQQQRL 163
Cdd:PRK13637 78 LSDIRKKVGLVFQYPEYqlFEETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-232 |
1.26e-39 |
|
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: 136.87 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK--FHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfnKMyqLYPEQRAEGG-ILLDGQNILTDNSDIa 88
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTL----KM--LTGELRPTSGtAYINGYSIRTDRKAA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 llRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfeK-LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIA 166
Cdd:cd03263 74 --RQSLGYCPQFDALFDeLTVREHLRFYARL--KgLPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-221 |
1.68e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 137.04 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPeqRAEGGILLDGQNILTDNSDiALLRA 92
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKA---ISGLLP--PRSGSIRFDGEDITGLPPH-RIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 KVGMVfqkptP-----FP-MSIYDNIAFGVRLfeKLSRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIA 166
Cdd:COG0410 79 GIGYV-----PegrriFPsLTVEENLLLGAYA--RRDRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSD 221
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIAD 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-211 |
2.32e-39 |
|
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: 136.52 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY---GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNILTDNsdIA 88
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYD--PT---SGEILLDGVDIRDLN--LR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQwALTKAALWN---ETKDKLH----QSGYSLSGGQQQ 161
Cdd:cd03249 74 WLRSQIGLVSQEPVLFDGTIAENIRYG------KPDATDEEVEE-AAKKANIHDfimSLPDGYDtlvgERGSQLSGGQKQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
12-221 |
3.97e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.17 E-value: 3.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYqlYPEQraeGGILLDGQNILTDNsdIALL 90
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY--LPQR---GRVKVMGREVNAEN--EKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTP--FPMSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:PRK13647 78 RSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSD 221
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWAD 206
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-218 |
5.37e-39 |
|
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: 135.07 E-value: 5.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-DNSDIALLRAKVGMVF 98
Cdd:TIGR02673 11 YPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA-----LTPSRGQVRIAGEDVNRlRGRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:TIGR02673 86 QDFRLLPdRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 178 LDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAAR 218
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDR 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-243 |
9.33e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.98 E-value: 9.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNILTDNSDIALL 90
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK--PT---SGEVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTP--FPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARG 168
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIE-------FSDTDNL 240
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkevFSDIETI 231
|
...
gi 1875943321 241 FTA 243
Cdd:PRK13639 232 RKA 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-245 |
1.17e-38 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 140.98 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-----------GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypeQRAEGGILLDGQNI 80
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLA---LLRL---IPSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LT-DNSDIALLRAKVGMVFQKPtpF----P-MSIYDNIAFGVRLFE-KLSRADMDERVQWALTKAALWNETKDKL-HQsg 152
Cdd:COG4172 350 DGlSRRALRPLRRRMQVVFQDP--FgslsPrMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRYpHE-- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 153 ysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTGK-IEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLG 229
Cdd:COG4172 426 --FSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDG 502
|
250
....*....|....*.
gi 1875943321 230 ELIEFSDTDNLFTAPQ 245
Cdd:COG4172 503 KVVEQGPTEQVFDAPQ 518
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-232 |
3.22e-38 |
|
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: 131.79 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypeQRAEGG-ILLDGQNILT-DNSDIALL 90
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL------LKPSSGeILLDGKDLASlSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVfqkptpfpmsiydniafgvrlfekLSRADMDervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIA 170
Cdd:cd03214 75 IAYVPQA------------------------LELLGLA-----------------HLADRPFNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-232 |
5.29e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 134.59 E-value: 5.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTDNSDIALL 90
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTP--FPMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRLCIARG 168
Cdd:PRK13636 81 RESVGMVFQDPDNqlFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-233 |
1.44e-37 |
|
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: 131.58 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTdnSDIA 88
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQK---GQILIDGIDIRD--ISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFPMSIYDNIAFGVrlfeklSRADMDERVQWALTKAA------LWNETKDKLHQSGYSLSGGQQQR 162
Cdd:cd03254 74 SLRSMIGVVLQDTFLFSGTIMENIRLGR------PNATDEEVIEAAKEAGAhdfimkLPNGYDTVLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMqQAARCSDSTAFMYLGELIE 233
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIE 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-232 |
3.07e-37 |
|
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: 131.70 E-value: 3.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQniltdnsDIALL-- 90
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRP-----TSGRILFDGR-------DITGLpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 --RAKVGMV--FQKPTPFP-MSIYDNIAFGV------RLFEKLSR--------ADMDERVQWALTKAALwnetKDKLHQS 151
Cdd:COG0411 74 hrIARLGIArtFQNPRLFPeLTVLENVLVAAharlgrGLLAALLRlprarreeREARERAEELLERVGL----ADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 152 GYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFMYLG 229
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDFG 229
|
...
gi 1875943321 230 ELI 232
Cdd:COG0411 230 RVI 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-216 |
4.31e-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: 129.47 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNILTDNSDIALLRAKVGMVFQ 99
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQS---GAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHC----LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQA 216
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-240 |
7.61e-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: 129.41 E-value: 7.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNILTDNSDIallR 91
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPTS---GRATVAGHDVVREPREV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIARGIA 170
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLY-GVPGAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-221 |
7.98e-37 |
|
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: 130.00 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDN-SDIALLRAKVGMVF 98
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL-----VEPTSGSVLIDGTDINKLKgKALRQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFP-MSIYDNIAFG-------VR-LFEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:cd03256 85 QQFNLIErLSVLENVLSGrlgrrstWRsLFGLFPKEEK-QRALAALERVGL----LDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSD 221
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYAD 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-211 |
9.88e-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: 129.66 E-value: 9.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK--FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltdnSDIAL 89
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDV----RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 --LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfeklsRADMDERVQWAltKAALWNETKDKLHQsGY---------SLSGG 158
Cdd:cd03251 72 asLRRQIGLVSQDVFLFNDTVAENIAYGRP------GATREEVEEAA--RAANAHEFIMELPE-GYdtvigergvKLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-216 |
1.38e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.98 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKF----HALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLypEQRAEGGILLDGQNILTDNS 85
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGF--LAPSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DiallRakvGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 164
Cdd:COG4525 77 D----R---GVVFQKDALLPwLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQA 216
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-245 |
2.47e-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: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK----FHALKNITLDIAKNKVTAFIGPSGCGKS----TLLRtfnkmyqLYPEQ--RAEGGILLDGQNIL 81
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-------LLPDPaaHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 T-DNSDIALLR-AKVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKL----HQs 151
Cdd:COG4172 80 GlSERELRRIRgNRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDPERRLdaypHQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 152 gysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLG 229
Cdd:COG4172 157 ---LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQG 233
|
250
....*....|....*.
gi 1875943321 230 ELIEFSDTDNLFTAPQ 245
Cdd:COG4172 234 EIVEQGPTAELFAAPQ 249
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-232 |
4.25e-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: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKN---KVTAFIGPSGCGKSTLLRTFNKMyqlypeQRAEGG-ILLDGQnILTD---NSDIALLRAKVGMVFQ 99
Cdd:cd03297 10 LPDFTLKIDFDlneEVTGIFGASGAGKSTLLRCIAGL------EKPDGGtIVLNGT-VLFDsrkKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KPTPFP-MSIYDNIAFGVRlfeKLSRADMDERVQWALTKAALwnetkDKLHQSG-YSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:cd03297 83 QYALFPhLNVRENLAFGLK---RKRNREDRISVDELLDLLGL-----DHLLNRYpAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-213 |
8.06e-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: 126.94 E-value: 8.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNIltDNSDIA 88
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK--PT---SGSVLLDGTDI--RQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeklsrADmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQQQ 161
Cdd:cd03245 75 DLRRNIGYVPQDVTLFYGTLRDNITLGAPL------AD-DERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNM 213
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-213 |
1.74e-35 |
|
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: 126.58 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNF-YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltDNSDIALL 90
Cdd:cd03253 1 IEFENVTFaYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV-----SSGSILIDGQDI--REVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFPMSIYDNIAFG------VRLFEKLSRADMDERVQwaltkaALWNETKDKLHQSGYSLSGGQQQRLC 164
Cdd:cd03253 74 RRAIGVVPQDTVLFNDTIGYNIRYGrpdatdEEVIEAAKAAQIHDKIM------RFPDGYDTIVGERGLKLSGGEKQRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNM 213
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-240 |
1.87e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.83 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLdGQNILT---DNSDIALLRAKVGMVFQKPT 102
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ--P---TSGTVTI-GERVITagkKNKKLKPLRKKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 103 P--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK13634 96 HqlFEETVEKDICFGPMNF-GVSEEDAKQKAREMIELVGL---PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 181 PCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIE-------FSDTDNL 240
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLqgtpreiFADPDEL 240
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-244 |
2.65e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.07 E-value: 2.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 21 YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIlTDNS----DIAllrakvgM 96
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-----EKPTEGQIFIDGEDV-THRSiqqrDIC-------M 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 97 VFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALwnetkdklhqSGYS------LSGGQQQRLCIARGI 169
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDL----------AGFEdryvdqISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-258 |
7.59e-35 |
|
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: 125.10 E-value: 7.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDN-SDIAL 89
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRL-----VEPSSGSILLEGTDITKLRgKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFP-MSIYDNIAFGvRL---------FEKLSRADMdERVQWALTKAALwnetKDKLHQSGYSLSGGQ 159
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVLHG-RLgykptwrslLGRFSEEDK-ERALSALERVGL----ADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIefsdt 237
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKYADRIVGLKAGEIV----- 225
|
250 260
....*....|....*....|.
gi 1875943321 238 dnlFTAPQKKQTEDYITGRYG 258
Cdd:TIGR02315 226 ---FDGAPSELDDEVLRHIYG 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-212 |
8.73e-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: 8.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI--LTDNSdIA 88
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVsdLRGRA-IP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKlSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPdRNVYENVAFALEVTGV-PPREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHN 212
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-240 |
1.18e-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: 125.97 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILtdnSDIALLRAKVGMVFQ 99
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDVV---REPRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KPTPFP-MSIYDNIAFGVRLFEkLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLL 178
Cdd:TIGR01188 74 YASVDEdLTGRENLEMMGRLYG-LPKDEAEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 179 DEPCSALDPISTGKIEELISELK-ADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-240 |
1.19e-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: 124.17 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLypeQRAEGGILLDGQNILTDNSDiALLRA 92
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MGLL---PVKSGSIRLDGEDITKLPPH-ERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 KVGMVFQKPTPFP-MSIYDNIAFGvrlFEKLSRAD--MDERVqwaltkAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:TIGR03410 76 GIAYVPQGREIFPrLTVEENLLTG---LAALPRRSrkIPDEI------YELFPVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-214 |
1.55e-34 |
|
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: 130.76 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNF-YYG-KFHALKNITLDI-AKNKVtAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNI-LTDNSD 86
Cdd:TIGR03375 463 EIEFRNVSFaYPGqETPALDNVSLTIrPGEKV-AIIGRIGSGKSTLLKLLLGLYQ--PT---EGSVLLDGVDIrQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 ialLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEklsradmDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQ 159
Cdd:TIGR03375 537 ---LRRNIGYVPQDPRLFYGTLRDNIALGAPYAD-------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQ 606
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQ 214
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-237 |
1.73e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 126.74 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQniltdnsDIALLR 91
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQTSGHIRFHGT-------DVSRLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AK---VGMVFQKPTPFP-MSIYDNIAFGVRLF---EKLSRADMDERVQWALTKAALwnetkDKLHQSGYS-LSGGQQQRL 163
Cdd:PRK10851 71 ARdrkVGFVFQHYALFRhMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEMVQL-----AHLADRYPAqLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGK----IEELISELKadYTVVIVTHNMQQAARCSDSTAFMYLGElIEFSDT 237
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKElrrwLRQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGN-IEQAGT 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-219 |
2.02e-34 |
|
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: 122.72 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 21 YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIA--LLRAKVGMVF 98
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLL-----EKFDSGQVYLNGQETPPLNSKKAskFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKptpFPM----SIYDNIAFGVrLFEKLSRADMDERVQWALTKAALWNetkdKLHQSGYSLSGGQQQRLCIARGIAIRPE 174
Cdd:TIGR03608 83 QN---FALieneTVEENLDLGL-KYKKLSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 175 VLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARC 219
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELnDEGKTIIIVTHDPEVAKQA 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-233 |
4.19e-34 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 122.96 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIALlrakvgmVFQKPTPFP- 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGKQITEPGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 MSIYDNIAFGV-RLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 184
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 185 LDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFM------YLGELIE 233
Cdd:TIGR01184 145 LDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-219 |
5.23e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 128.17 E-value: 5.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 4 VTDASSSKIQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPeqrAEGGILLDGQNIlt 82
Cdd:TIGR02857 314 VTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL--LGFVDP---TEGSIAVNGVPL-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 DNSDIALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWNETKD-------KLHQSGYS 154
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLA--------RPDAsDAEIREALERAGLDEFVAAlpqgldtPIGEGGAG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-243 |
1.35e-33 |
|
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: 121.82 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG--KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYqlYPEQraeGGILLDGQNILTdnSDIAL 89
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY--VPEN---GRVLVDGHDLAL--ADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIAfgvrlfekLSRADMD-ERVQWAlTKAALWNETKDKLH--------QSGYSLSGGQQ 160
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIA--------LADPGMSmERVIEA-AKLAGAHDFISELPegydtivgEQGAGLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMqQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
...
gi 1875943321 241 FTA 243
Cdd:cd03252 224 LAE 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-245 |
1.67e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.63 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNIL--TDNSDIALLRAKVGMVFQKPTP- 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKP---SSGTITIAGYHITpeTGNKNLKKLRKKVSLVFQFPEAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 -FPMSIYDNIAFGVRLFEKLSRADMDERVQWaLTKAALWNETKDKlhqSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 182
Cdd:PRK13641 98 lFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 183 SALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-232 |
3.36e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 121.27 E-value: 3.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNIlTDNSDIAL 89
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQS---GTVFLGDKPI-SMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIAFG----VRLFEKLSRADmDERVQWALTKAALwNETKDKLHQsgySLSGGQQQRLCI 165
Cdd:PRK11231 75 ARRLALLPQHHLTPEGITVRELVAYGrspwLSLWGRLSAED-NARVNQAMEQTRI-NHLADRRLT---DLSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-232 |
8.51e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 122.90 E-value: 8.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyQLYPEQRaeGGILLDGQNILTDNSD--IALLRAKVGMVFQKPTP 103
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLN---RLIEPTA--GEVLIDGEDITKLSKKelRELRRKKMSMVFQHFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 FP-MSIYDNIAFG--VRlfeKLSRADMDERVQWALTKAAL--WnetKDKL-HQsgysLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:COG4175 117 LPhRTVLENVAFGleIQ---GVPKAERRERAREALELVGLagW---EDSYpDE----LSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 178 LDEPCSALDPIstgkI-----EELI---SELKAdyTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:COG4175 187 MDEAFSALDPL----IrremqDELLelqAKLKK--TIVFITHDLDEALRLGDRIAIMKDGRIV 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-221 |
1.14e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 120.25 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyQLYPEQraeGGILLDGQNILT-DNSDIALL 90
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG--QIAPDH---GEILFDGENIPAmSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETkdKLHQSgySLSGGQQQRLCIARGI 169
Cdd:PRK11831 83 RKRMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA--KLMPS--ELSGGMARRAALARAI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSD 221
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-218 |
1.79e-32 |
|
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: 118.34 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGK---FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIltDNSDI 87
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ--PQG---GQVLLDGKPI--SQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQWALTKAA----------LWNETKDKlhqsGYSLSG 157
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARSLQDNIAYG------LQSCSFECVKEAAQKAHAhsfiselasgYDTEVGEK----GSQLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 158 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAAR 218
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-211 |
2.11e-32 |
|
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: 117.68 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAkNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNILTDNSDIall 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRI------LATLTPPSSGtIRIDGQDVLKQPQKL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRLCIARGI 169
Cdd:cd03264 71 RRRIGYLPQEFGVYPnFTVREFLDYIAWL-KGIPSKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-216 |
2.66e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 121.29 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdnSDIAL 89
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLFIGEKRM----NDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWA---LTKAALWnETKDKlhqsgySLSGGQQQRLCI 165
Cdd:PRK11000 73 AERGVGMVFQSYALYPhLSVAENMSFGLKL-AGAKKEEINQRVNQVaevLQLAHLL-DRKPK------ALSGGQRQRVAI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQA 216
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhkRLGRTMIYVTHDQVEA 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-232 |
4.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 5 TDASSSKIQVRDLNFYYGKFH--ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILT 82
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK--PQS---GEIKIDGITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 DNsdIALLRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQ 160
Cdd:PRK13632 76 EN--LKEIRKKIGIIFQNPdNQFiGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCsDSTAFMYLGELI 232
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILA-DKVIVFSEGKLI 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-252 |
8.01e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 8.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGK-----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTDNS 85
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKP---TTGTVTVDDITITHKTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 D--IALLRAKVGMVFQKPTP--FPMSIYDNIAFGVRLFeklsRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ 161
Cdd:PRK13646 77 DkyIRPVRKRIGMVFQFPESqlFEDTVEREIIFGPKNF----KMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDN 239
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
250
....*....|...
gi 1875943321 240 LFTapQKKQTEDY 252
Cdd:PRK13646 233 LFK--DKKKLADW 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-232 |
8.45e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.92 E-value: 8.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYqlYPeqrAEGGILLDGQNILTD--NSDIALLRAKVGMVFQKPTP 103
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH--VP---TQGSVRVDDTLITSTskNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 --FPMSIYDNIAFGVRLFEklsrADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 181
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFG----VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 182 CSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-217 |
1.09e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.04 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMY-QLYPEQRAEGGILLDGQNIltdnSDIALLR 91
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL---AAIAgTLSPAFSASGEVLLNGRRL----TALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRlfEKLSRADMDERVQWALTKAALwnetkdklhqSGY------SLSGGQQQRLC 164
Cdd:COG4136 76 RRIGILFQDDLLFPhLSVGENLAFALP--PTIGRAQRRARVEQALEEAGL----------AGFadrdpaTLSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELI-SELKA-DYTVVIVTHNMQQAA 217
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQrGIPALLVTHDEEDAP 198
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
9-211 |
1.22e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 122.76 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 9 SSKIQVRDLNFYYGK--FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQNIltDNSD 86
Cdd:TIGR03797 449 SGAIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDL--AGLD 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLfeklsraDMDErVQWALTKAALWNETKD---KLH----QSGYSLSGGQ 159
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIAGGAPL-------TLDE-AWEAARMAGLAEDIRAmpmGMHtvisEGGGTLSGGQ 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAdyTVVIVTH 211
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV--TRIVIAH 643
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-248 |
2.01e-31 |
|
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: 115.83 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLYPeqRAEGGILLDGQNIltdnSDIAL-L 90
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDI----THLPMhE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVF--QKPTPF-PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:TIGR04406 73 RARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQK 246
Cdd:TIGR04406 149 ALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKV 228
|
..
gi 1875943321 247 KQ 248
Cdd:TIGR04406 229 RR 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-226 |
2.28e-31 |
|
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: 115.05 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNF-YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNIltdnsDIALLR 91
Cdd:cd03226 1 RIENISFsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPI-----KAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTP--FPMSIYDNIAFGVRLFeklsrADMDERVQWALTKAALWnETKDKLHQSgysLSGGQQQRLCIARGI 169
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKEL-----DAGNEQAETVLKDLDLY-ALKERHPLS---LSGGQKQRLAIAAAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIV-THNMQQAARCSDSTAFM 226
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIViTHDYEFLAKVCDRVLLL 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-211 |
2.56e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.28 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIltdnSDIAL 89
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDL----RDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 --LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERvqwalTKAALWNETKDKLHQ--------SGYSLSGGQ 159
Cdd:PRK11176 413 asLRNQVALVSQNVHLFNDTIANNIAYART--EQYSREQIEEA-----ARMAYAMDFINKMDNgldtvigeNGVLLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-245 |
3.11e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK---FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNILTDNsdIA 88
Cdd:PRK13642 5 LEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEF-----EGKVKIDGELLTAEN--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTP--FPMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWN-ETKDKLHqsgysLSGGQQQRLCI 165
Cdd:PRK13642 78 NLRRKIGMVFQNPDNqfVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDfKTREPAR-----LSGGQKQRVAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARcSDSTAFMYLGELIEFSDTDNLFTA 243
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
..
gi 1875943321 244 PQ 245
Cdd:PRK13642 231 SE 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
12-245 |
1.83e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.45 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKF------HALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIL 81
Cdd:PRK11308 6 LQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI-----ETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 T-DNSDIALLRAKVGMVFQKPTPfpmSIYDNIAFGVRLFE------KLSRADMDERVQWALTKAALWNEtkdklHQSGYS 154
Cdd:PRK11308 81 KaDPEAQKLLRQKIQIVFQNPYG---SLNPRKKVGQILEEpllintSLSAAERREKALAMMAKVGLRPE-----HYDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 155 --LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTV--VIVTHNMQQAARCSDSTAFMYLGE 230
Cdd:PRK11308 153 hmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGR 232
|
250
....*....|....*
gi 1875943321 231 LIEFSDTDNLFTAPQ 245
Cdd:PRK11308 233 CVEKGTKEQIFNNPR 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-255 |
2.93e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 116.67 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNI--LTDNSDIALLRAKVGMVFQKPTP 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 FP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNetkdklHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK10070 118 MPhMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLEN------YAHSYpdELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 181 PCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTEDYITG 255
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-221 |
4.12e-30 |
|
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: 110.21 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNILTdNSDIALLR 91
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-----PDSGEILVDGKEVSF-ASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 171
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 172 RPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSD 221
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIAD 150
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-232 |
4.93e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.67 E-value: 4.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNIltDNSDiallR 91
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI--LAPD---SGEVLWDGEPL--DPED----R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVG-M-----VFQKptpfpMSIYDNIAFGVRLfeK-LSRADMDERVQWALTK---AALWNetkDKLHqsgySLSGGQQQ 161
Cdd:COG4152 71 RRIGyLpeergLYPK-----MKVGEQLVYLARL--KgLSKAEAKRRADEWLERlglGDRAN---KKVE----ELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIV-THNMQQAARCSDSTAFMYLGELI 232
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-211 |
5.42e-30 |
|
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: 111.82 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltdnSDIA 88
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDI----SKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 L--LRAKVGMVFQKPTPFPMSIYDNIAFgvrlFEKLSradmDERVQWALTKAALWNETK-------DKLHQSGYSLSGGQ 159
Cdd:cd03244 73 LhdLRSRISIIPQDPVLFSGTIRSNLDP----FGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-233 |
5.87e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 111.15 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYpeqRAEGG-ILLDGQNIlTDNSDIall 90
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLI---KPDSGeITFDGKSY-QKNIEA--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLsradmDERVQWALTKAALWNETKDKLhqSGYSLsgGQQQRLCIARGI 169
Cdd:cd03268 71 LRRIGALIEAPGFYPnLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKV--KGFSL--GMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIE 233
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-219 |
1.63e-29 |
|
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: 110.99 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLDGQNILTDNSD- 86
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGL---LAGL--DRPTSGTVRLAGQDLFALDEDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRA-KVGMVFQK----PTpfpMSIYDNIAfgVRLfEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQ 161
Cdd:COG4181 84 RARLRArHVGFVFQSfqllPT---LTALENVM--LPL-ELAGRRDARARARALLERVGL----GHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPiSTG-KIEELISELKADY--TVVIVTHNMQQAARC 219
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDA-ATGeQIIDLLFELNRERgtTLVLVTHDPALAARC 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-244 |
1.74e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.82 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTDNsdIALL 90
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKP---TSGSVLIRGEPITKEN--IREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTP--FPMSIYDNIAFG-VRLfeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGpINL--GLDEETVAHRVSSALHMLGL----EELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-226 |
1.99e-29 |
|
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: 109.89 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGkfHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTdnSDIAllR 91
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF-----ETPQSGRVLINGVDVTA--APPA--D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLsRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 170
Cdd:cd03298 70 RPVSMLFQENNLFAhLTVEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFM 226
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-232 |
2.37e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.15 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTDNSDI 87
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE--PDA---GFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 allRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIA 166
Cdd:cd03266 77 ---RRRLGFVSDSTGLYDrLTARENLEYFAGLY-GLKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-212 |
3.41e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.12 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLypEQRAEGGILLDGQNIltdnSDIAL 89
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGRIFLDGEDI----THLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 -LRAKVGM--------VFQKptpfpMSIYDNIAfGVRLFEKLSRADMDERVQwaltkaALWNETK-DKL-HQSGYSLSGG 158
Cdd:COG1137 73 hKRARLGIgylpqeasIFRK-----LTVEDNIL-AVLELRKLSKKEREERLE------ELLEEFGiTHLrKSKAYSLSGG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHN 212
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHN 195
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
10-242 |
4.81e-29 |
|
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: 110.67 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYY---------GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQNI 80
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LT-DNSDIALLRAKVGMVFQK-PTPF--PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSgysLS 156
Cdd:TIGR02769 76 YQlDRKQRRAFRRDVQLVFQDsPSAVnpRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
....*...
gi 1875943321 235 SDTDNLFT 242
Cdd:TIGR02769 233 CDVAQLLS 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-219 |
8.69e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 107.30 E-value: 8.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHA--LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQNILTDNSDIal 89
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLI-----LGLLRPTSGRVRLDGADISQWDPNE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGI 169
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELK-ADYTVVIVTHNMQQAARC 219
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASA 162
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-211 |
1.06e-28 |
|
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: 107.95 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPeqRAEGGILLDGQNILTDNSDialLR 91
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRI---LAGLLP--PSAGEVLWNGEPIRDARED---YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLF-EKLSRADMDErvqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:COG4133 75 RRLAYLGHADGLKPeLTVRENLRFWAALYgLRADREAIDE----ALEAVGL----AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISE-LKADYTVVIVTH 211
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-249 |
1.09e-28 |
|
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: 108.78 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLypEQRAEGGILLDGQNILTDNSDIallR 91
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGL--VKPDSGKILLDGQDITKLPMHK---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVF--QKPTPF-PMSIYDNIAfGVRLFEKLSRADMDERVQwaltkaALWNETK-DKL-HQSGYSLSGGQQQRLCIA 166
Cdd:cd03218 73 ARLGIGYlpQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLE------ELLEEFHiTHLrKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
....
gi 1875943321 246 KKQT 249
Cdd:cd03218 226 VRKV 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-244 |
1.55e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 113.66 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYY---GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNIltDNSDI 87
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ--PT---GGQVLLDGVPL--VQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADMDERVQWALTKAA------LWNETKDKLHQSGYSLSGGQQQ 161
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENIAYG------LTDTPDEEIMAAAKAANAhdfimeFPNGYDTEVGEKGSQLSGGQKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDpistGKIEELISELK--ADYTVVIVTHNMQQAARCsDSTAFMYLGELIEFSDTDN 239
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVERA-DQILVLKKGSVVEMGTHKQ 699
|
....*
gi 1875943321 240 LFTAP 244
Cdd:TIGR00958 700 LMEDQ 704
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-244 |
2.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.94 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 23 KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGI----LLDGQNILTDNSDIAL--------- 89
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGL--IKSKY---GTIqvgdIYIGDKKNNHELITNPyskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 -LRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLfeKLSRADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCI 165
Cdd:PRK13631 113 eLRRRVSMVFQFPeyQLFKDTIEKDIMFGpVAL--GVKKSEAKKLAKFYLNKMGL---DDSYLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-258 |
3.32e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.15 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 7 ASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTDNSD 86
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIQHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRakVGMVFQKP-TPFPMSIYDNIAFGVR----LFEKLSRADMDervqwALTKAALWNETKDKLHQSGYSLSGGQQQ 161
Cdd:PRK10253 78 EVARR--IGLLAQNAtTPGDITVQELVARGRYphqpLFTRWRKEDEE-----AVTKAMQATGITHLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARcsdstafmYLGELIEFSDTDN 239
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACR--------YASHLIALREGKI 222
|
250 260
....*....|....*....|
gi 1875943321 240 LFT-APQKKQTEDYITGRYG 258
Cdd:PRK10253 223 VAQgAPKEIVTAELIERIYG 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-249 |
4.09e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 112.26 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDL-----------NFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQraEGGILLDGQNI 80
Cdd:PRK10261 314 LQVRNLvtrfplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRA---LLRLVESQ--GGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LT-DNSDIALLRAKVGMVFQKP----TPfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklHQSGY-- 153
Cdd:PRK10261 389 DTlSPGKLQALRRDIQFIFQDPyaslDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPE-----HAWRYph 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTV--VIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQI 542
|
250
....*....|....*...
gi 1875943321 232 IEFSDTDNLFTAPQKKQT 249
Cdd:PRK10261 543 VEIGPRRAVFENPQHPYT 560
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-217 |
5.07e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.91 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 6 DASSSKIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltD 83
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYNNQAI--T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 84 NSDIALLRAKVGMVFQKP-TPFPMSI--YDnIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQ 160
Cdd:PRK13648 75 DDNFEKLRKHIGIVFQNPdNQFVGSIvkYD-VAFGLENH-AVPYDEMHRRVSEALKQVDMLERADYEPN----ALSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVI--VTHNMQQAA 217
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAM 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-241 |
5.16e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.90 E-value: 5.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 9 SSKIQVRDLNFYYGK---FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNILTDNs 85
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAES---GQIIIDGDLLTEEN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 dIALLRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALwNETKDKlhqSGYSLSGGQQQRL 163
Cdd:PRK13650 76 -VWDIRHKIGMVFQNPdNQFvGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGM-QDFKER---EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPisTGKIE--ELISELKADY--TVVIVTHNMQQAArCSDSTAFMYLGELIEFSDTDN 239
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
..
gi 1875943321 240 LF 241
Cdd:PRK13650 227 LF 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-240 |
5.83e-28 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 112.14 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYYG-KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIltDNSD 86
Cdd:TIGR01193 470 LNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ--ARS---GEILLNGFSL--KDID 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERVQWALTKAALWNET---KDKLHQSGYSLSGGQQQRL 163
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSGSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIENMPlgyQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKaDYTVVIVTHNMQQAARcSDSTAFMYLGELIEFSDTDNL 240
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-232 |
6.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 6.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-----GKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNIlTDNS 85
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDT-SDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPtpfpmsiyDN----------IAFGVrlfEKLSRA--DMDERVQWALTKAALWNETKDKLHQsgy 153
Cdd:PRK13633 79 NLWDIRNKAGMVFQNP--------DNqivativeedVAFGP---ENLGIPpeEIRERVDESLKKVGMYEYRRHAPHL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 sLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARcSDSTAFMYLGEL 231
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKV 222
|
.
gi 1875943321 232 I 232
Cdd:PRK13633 223 V 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-233 |
6.91e-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: 105.09 E-value: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYG--KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTDNsdiAL 89
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQ---GEITLDGVPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeklsradmdervqwaltkaalwnetkdklhqsGYSLSGGQQQRLCIARGI 169
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARcSDSTAFMYLGELIE 233
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-245 |
9.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 9.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQRAEGGILLDGQNILTDNs 85
Cdd:PRK13640 2 KDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 dIALLRAKVGMVFQKP-TPF-PMSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHqsgySLSGGQQQRL 163
Cdd:PRK13640 79 -VWDIREKVGIVFQNPdNQFvGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPA----NLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARcSDSTAFMYLGELIEFSDTDNLF 241
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF 231
|
....
gi 1875943321 242 TAPQ 245
Cdd:PRK13640 232 SKVE 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-241 |
1.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.51 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraegGILLDGQNILTDNS---DIALLRAKVGMVFQKPT 102
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQ--PTE----GKVTVGDIVVSSTSkqkEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 103 P--FPMSIYDNIAFGVRLFeKLSRadmDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNF-GIPK---EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 181 PCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-211 |
1.14e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.78 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIlTD----NSDIAllrakvg 95
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-----ERITSGEIWIGGRVV-NElepaDRDIA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 96 MVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQwaltKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPE 174
Cdd:PRK11650 80 MVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIEERVA----EAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1875943321 175 VLLLDEPCSALDpistGK--------IEELISELKAdyTVVIVTH 211
Cdd:PRK11650 155 VFLFDEPLSNLD----AKlrvqmrleIQRLHRRLKT--TSLYVTH 193
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-242 |
1.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.02 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 9 SSKIQVRDLNFYYGK-----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlypeqraegGILLD--GQNIL 81
Cdd:PRK13645 4 SKDIILDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTN-------------GLIISetGQTIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 TDNS---------DIALLRAKVGMVFQKP--TPFPMSIYDNIAFG-VRLFEklSRADMDERVQWALTKAALwneTKDKLH 149
Cdd:PRK13645 71 GDYAipanlkkikEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGE--NKQEAYKKVPELLKLVQL---PEDYVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 150 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYT--VVIVTHNMQQAARCSDSTAFMY 227
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMH 225
|
250
....*....|....*
gi 1875943321 228 LGELIEFSDTDNLFT 242
Cdd:PRK13645 226 EGKVISIGSPFEIFS 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-212 |
1.64e-27 |
|
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: 110.14 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQRaeGGILLDGQNILTDNSDiaLL 90
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT---LAGLLDPLQ--GEVTLDGVPVSSLDQD--EV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWN---ETKD----KLHQSGYSLSGGQQQR 162
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLRLA--------RPDAtDEELWAALERVGLADwlrALPDgldtVLGEGGARLSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPiSTGkiEELISELKA---DYTVVIVTHN 212
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDA-ETA--DELLEDLLAalsGRTVVLITHH 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-241 |
3.43e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.86 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 16 DLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNILTDNSDIALLRAKVG 95
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQK---GAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 96 MVFQKPTP--FPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAalwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRP 173
Cdd:PRK13638 81 TVFQDPEQqiFYTDIDSDIAFSLRNL-GVPEAEITRRVDEALTLV----DAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 174 EVLLLDEPCSALDPISTGKIEELISELKADYT-VVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLF 241
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-234 |
4.97e-27 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 103.65 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGKF--HALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltdnSDIA 88
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDI----STIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 L--LRAKVGMVFQKPTPFPMSIYDNiafgVRLFEKLSradmDERVQWALtkaalwnetkdKLHQSGYSLSGGQQQRLCIA 166
Cdd:cd03369 77 LedLRSSLTIIPQDPTLFSGTIRSN----LDPFDEYS----DEEIYGAL-----------RVSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIEF 234
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-244 |
7.94e-27 |
|
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: 106.34 E-value: 7.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIA----KNKVTAFIGPSGCGKSTLLRTfnkMYQLypEQRAEGGILLDGQNILTDNSDIALLRAK--VGMVF 98
Cdd:COG4148 9 LRRGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRA---IAGL--ERPDSGRIRLGGEVLQDSARGIFLPPHRrrIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFP-MSIYDNIAFGV-RLFEKLSRADMDERVQWaLTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVL 176
Cdd:COG4148 84 QEARLFPhLSVRGNLLYGRkRAPRAERRISFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 177 LLDEPCSALD--------PIstgkIEELISELkaDYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:COG4148 156 LMDEPLAALDlarkaeilPY----LERLRDEL--DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-211 |
1.16e-26 |
|
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: 107.88 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYG--KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNIltdnSDIA 88
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDL----ADYT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 L--LRAKVGMVFQKPTPFPMSIYDNIAFGVRlfEKLSRADMDERVQWALTKAaLWNETKDKLH----QSGYSLSGGQQQR 162
Cdd:TIGR02203 401 LasLRRQVALVSQDVVLFNDTIANNIAYGRT--EQADRAEIERALAAAYAQD-FVDKLPLGLDtpigENGVLLSGGQRQR 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-221 |
1.21e-26 |
|
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: 102.74 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNILT-DNSDIALL 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFDGKPLDIaARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMvFQKptpfpMSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 170
Cdd:cd03269 76 PEERGL-YPK-----MKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELK-ADYTVVIVTHNMQQAARCSD 221
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCD 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-214 |
1.60e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 102.16 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRtfnkmyqlypeqraegGILldGQniLTDNSD 86
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLS----------------ALL--GE--LEKLSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKPTPFPMSIYDNIAFGVRlFEKlsradmdERVQWALTKAALwneTKD----------KLHQSGYSLS 156
Cdd:cd03250 61 SVSVPGSIAYVSQEPWIQNGTIRENILFGKP-FDE-------ERYEKVIKACAL---EPDleilpdgdltEIGEKGINLS 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPiSTGK--IEELI-SELKADYTVVIVTHNMQ 214
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDA-HVGRhiFENCIlGLLLNNKTRILVTHQLQ 189
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-233 |
1.70e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIlTDNSDIAl 89
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQ---GEILLNGQPI-ADYSEAA- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQKPTPFPMSIYDNIAFGvrlfekLSRADmDERVQWALTKAALWNETKDK------LHQSGYSLSGGQQQRL 163
Cdd:PRK11160 412 LRQAISVVSQRVHLFSATLRDNLLLA------APNAS-DEALIEVLQQVGLEKLLEDDkglnawLGEGGRQLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIE 233
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-216 |
2.07e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 103.24 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQraEGGILLDGQNILTDNsdiallr 91
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVPYQ--HGSITLDGKPVEGPG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLfEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIA 170
Cdd:PRK11248 70 AERGVVFQNEGLLPwRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQA 216
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-233 |
2.77e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.97 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNILTDNsdIALL 90
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--P---QSGRILIDGTDIRTVT--RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsRAD-MDERVQWALTKAALWN--ETKDKLHQS-----GYSLSGGQQQR 162
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVG--------RPDaTDEEMRAAAERAQAHDfiERKPDGYDTvvgerGRQLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMqQAARCSDSTAFMYLGELIE 233
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-222 |
3.89e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIlTDNSDIALLR 91
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-----SGEILLDGEPV-RFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGvrlFEKLSRADMDERVQWALTKAALwnetkDKLHQS-------GySLSGGQQQRL 163
Cdd:COG1129 79 AGIAIIHQELNLVPnLSVAENIFLG---REPRRGGLIDWRAMRRRARELL-----ARLGLDidpdtpvG-DLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDS 222
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADR 209
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
23-231 |
9.16e-26 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 100.56 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 23 KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkMYqlypEQRAEGGILLDGQNI--LTDNSDIALLRAKVGMVFQK 100
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MF----DSLDSGSLTLAGKEVtnLSYSQKIILRRELIGYIFQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 PTPFP-MSIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:NF038007 92 FNLIPhLSIFDNVALPLK-YRGVAKKERIERVNQVLNLFGIDNRRNHKPMQ----LSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 180 EPCSALDPISTGKIEELISEL-KADYTVVIVTHNmQQAARCSDSTAFMYLGEL 231
Cdd:NF038007 167 EPTGNLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-251 |
1.15e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 105.88 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYY---GKFHALKNITLDIAKNKVTAFIGPSGCGKST----LLRTFN--------------------KMYQL 63
Cdd:PTZ00265 1165 KIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTvmslLMRFYDlkndhhivfknehtndmtneQDYQG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 64 YPEQ-------------------------RAEGGILLDGQNILTDNsdIALLRAKVGMVFQKPTPFPMSIYDNIAFGVrl 118
Cdd:PTZ00265 1245 DEEQnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYN--LKDLRNLFSIVSQEPMLFNMSIYENIKFGK-- 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 119 fEKLSRADMDERVQWALTKA---ALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEE 195
Cdd:PTZ00265 1321 -EDATREDVKRACKFAAIDEfieSLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 196 LISEL--KADYTVVIVTHNMQQAARcSDstafmylgELIEFSDTDNLFTAPQKKQTED 251
Cdd:PTZ00265 1400 TIVDIkdKADKTIITIAHRIASIKR-SD--------KIVVFNNPDRTGSFVQAHGTHE 1448
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-221 |
1.68e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRA-EGGILLDGQNiLTDNS--DIA 88
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRA------LSGELSPdSGEVRLNGRP-LADWSpaELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAkvgMVFQKPT-PFPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWnETKDKLHQsgySLSGGQQQRLCIAR 167
Cdd:PRK13548 76 RRRA---VLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLA-HLAGRDYP---QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 168 GIA------IRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSD 221
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYAD 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-221 |
1.96e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 100.34 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRA-EGGILLDGQNIlTDNSDIALLRAKVGMVF 98
Cdd:PRK11614 14 HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGT------LCGDPRAtSGRIVFDGKDI-TDWQTAKIMREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFP-MSIYDNIAFGVRLFEklsRADMDERVQWALtkaALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PRK11614 87 EGRRVFSrMTVEENLAMGGFFAE---RDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSD 221
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLAD 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-221 |
5.08e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILTDNSDI 87
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPT---SGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 alLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKlsRADMDeRVQWALTKAALWNETkdkLHQSGYSLSGGQQQRLCIAR 167
Cdd:PRK10247 79 --YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQ--QPDPA-IFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVI--VTHNMQQAARCSD 221
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADK 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-237 |
5.11e-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: 98.39 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 32 LDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNILTdnsdIALLRAKVGMVFQKPTPFP-MSIYD 110
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSHTG----LAPYQRPVSMLFQENNLFAhLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 111 NIAFGVRLFEKLSrADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIST 190
Cdd:TIGR01277 90 NIGLGLHPGLKLN-AEQQEKVVDAAQQVGI----ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 191 GKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDT 237
Cdd:TIGR01277 165 EEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
21-221 |
6.24e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 99.37 E-value: 6.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 21 YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqrAEGGILLDGQNILTDnsdialLRAKVGMVFQK 100
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET------PSAGELLAGTAPLAE------AREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 PTPFP-MSIYDNIAFGVRlfeklsrADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGLK-------GQWRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1875943321 180 EPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSD 221
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMAD 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-218 |
1.16e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.02 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-DNSDIALLRAKVGMVF 98
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDITRlKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKP-TPFPMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PRK10908 86 QDHhLLMDRTVYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 178 LDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAAR 218
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISR 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-211 |
1.79e-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: 101.82 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQraEGGILLDGQNI--LTDNSdialLRAKVGMVFQKPTPF 104
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARL---LFRFYDVT--SGRILIDGQDIrdVTQAS----LRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 PMSIYDNIAFGvrlfeklsRADMDERVQWALTKAAlwnetkdKLHQ------SGYS---------LSGGQQQRLCIARGI 169
Cdd:COG5265 445 NDTIAYNIAYG--------RPDASEEEVEAAARAA-------QIHDfieslpDGYDtrvgerglkLSGGEKQRVAIARTL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-249 |
1.80e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.78 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNiLTDNSDIALL--RAKVGMVFQKP-- 101
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGEVAWLGKD-LLGMKDDEWRavRSDIQMIFQDPla 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 102 --TPfPMSIYDNIAFGVRLFE-KLSRADMDERVQWALTKAALW-NETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PRK15079 110 slNP-RMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLpNLINRYPHE----FSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQT 249
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-232 |
1.81e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlypeqraeGGILLDGQNILTDNSDIALL----RAK-VGMVFQ 99
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA------------GSLPPDSGSILIDGKDVTKLpeykRAKyIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KP---TPFPMSIYDNIA--------FGVRLfeKLSRADMD---ERVqwaltkAALWNETKDKLHQSGYSLSGGQQQRLCI 165
Cdd:COG1101 88 DPmmgTAPSMTIEENLAlayrrgkrRGLRR--GLTKKRRElfrELL------ATLGLGLENRLDTKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-250 |
2.55e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 14 VRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEQRAEGGILLDGQN----ILTDNS 85
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqviELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLR---AKVGMVFQKPTP-----FPMSiyDNIAFGVRLFEKLSRADMDERVQWALTKAALwNETKDKLHQSGYSLSG 157
Cdd:PRK10261 95 AAQMRHvrgADMAMIFQEPMTslnpvFTVG--EQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 158 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYT--VVIVTHNMQQAARCSDSTAFMYLGELIEFS 235
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250
....*....|....*
gi 1875943321 236 DTDNLFTAPQKKQTE 250
Cdd:PRK10261 252 SVEQIFHAPQHPYTR 266
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-237 |
3.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 3.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGK-----FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQRAEGGILLDGQN------ 79
Cdd:PRK13651 2 QIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPDTGTIEWIFKDEKNkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 80 ---ILTDN----------SDIALLRAKVGMVFQ--KPTPFPMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwneT 144
Cdd:PRK13651 80 kekVLEKLviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGL---D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 145 KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDST 223
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|....
gi 1875943321 224 AFMYLGELIEFSDT 237
Cdd:PRK13651 236 IFFKDGKIIKDGDT 249
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-244 |
5.92e-24 |
|
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: 98.65 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKnITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQnILTDNSDIALL---RAKVGMVFQKP 101
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGR-TLFDSRKGIFLppeKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 102 TPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:TIGR02142 85 RLFPhLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 181 PCSALDPISTGKI----EELISELkaDYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:TIGR02142 158 PLAALDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-218 |
9.30e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 21 YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqlypeqraeGGIL--LDGQNILTDNSDIALL--RAKVgm 96
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL-------------AGVLrpTSGTVRRAGGARVAYVpqRSEV-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 97 vfqkPTPFPMSIYDNIAFGV----RLFEKLSRADmDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIR 172
Cdd:NF040873 67 ----PDSLPLTVRDLVAMGRwarrGLWRRLTRDD-RAAVDDALERVGL----ADLAGRQLGELSGGQRQRALLAQGLAQE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1875943321 173 PEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAAR 218
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRR 184
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-213 |
1.35e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 7 ASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLlrtFNKMYQLYpeQRAEGGILLDGQNI--LTDN 84
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLTGFY--KPTGGTILLRGQHIegLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 85 sdialLRAKVGMV--FQKPTPF-PMSIYDNI------AFGVRLFEKL------SRADMDervqwALTKAALWNET---KD 146
Cdd:PRK11300 76 -----QIARMGVVrtFQHVRLFrEMTVIENLlvaqhqQLKTGLFSGLlktpafRRAESE-----ALDRAATWLERvglLE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 147 KLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNM 213
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDM 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-249 |
2.16e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKST----LLRTFnkmyqlypeqRAEGGILLDGQNILTDNSDIAL-LRAKVGMVFQ 99
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI----------NSQGEIWFDGQPLHNLNRRQLLpVRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KP----TPfPMSIYDNIAFGVRLFEK-LSRADMDERVQWALTKAALWNETKdklHQSGYSLSGGQQQRLCIARGIAIRPE 174
Cdd:PRK15134 370 DPnsslNP-RLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPETR---HRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 175 VLLLDEPCSALDPISTGKIEELISELKADYTV--VIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQT 249
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-244 |
3.19e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQraEGGILLDGQNILTDNSD----- 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL---SMISRLLPPD--SGEVLVDGLDVATTPSRelakr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRakvgmvfQKPTpFPM--SIYDNIAFGvRlF----EKLSRADmDERVQWALTKAALwNETKDK-LHQsgysLSGGQ 159
Cdd:COG4604 77 LAILR-------QENH-INSrlTVRELVAFG-R-FpyskGRLTAED-REIIDEAIAYLDL-EDLADRyLDE----LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPistgK--------IEELISELkaDYTVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDM----KhsvqmmklLRRLADEL--GKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
250
....*....|...
gi 1875943321 232 IEFSDTDNLFTAP 244
Cdd:COG4604 215 VAQGTPEEIITPE 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-221 |
3.22e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLlrtfnkMYQLYPEQRAEGG-ILLDGQNILTDNSDIALl 90
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKILYGLYQPDSGeILIDGKPVRIRSPRDAI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGvrlfeklsradMDERVQWALTKAALWNETKDKLHQSG---------YSLSGGQQ 160
Cdd:COG3845 79 ALGIGMVHQHFMLVPnLTVAENIVLG-----------LEPTKGGRLDRKAARARIRELSERYGldvdpdakvEDLSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPistGKIEELIS---ELKAD-YTVVIVTHNMQQAARCSD 221
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTP---QEADELFEilrRLAAEgKSIIFITHKLREVMAIAD 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-233 |
4.87e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.37 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQNILT-DNSDIALLRAKVGMVFQKP---- 101
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLL-----VGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDSisav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 102 TPfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSgysLSGGQQQRLCIARGIAIRPEVLLLDEP 181
Cdd:PRK10419 103 NP-RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 182 CSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSDSTAFMYLGELIE 233
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-211 |
6.02e-23 |
|
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: 94.00 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNK-MYQLYP-------EQRaeGGIlldgqniltd 83
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGndvrlfgERR--GGE---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 84 nsDIALLRAKVGMV---FQKPTPFPMSIYDNI---AFG-VRLFEKLSRADMDERVQWAltkaALWnETKDKLHQSGYSLS 156
Cdd:COG1119 72 --DVWELRKRIGLVspaLQLRFPRDETVLDVVlsgFFDsIGLYREPTDEQRERARELL----ELL-GLAHLADRPFGTLS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTH 211
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-248 |
1.34e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKfHALKNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLYPEqraeggillDGQNILTDNSDIALL------RAK 93
Cdd:PRK10895 13 YKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVPR---------DAGNIIIDDEDISLLplharaRRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 94 VGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVqwaltkaalwNETKDKLHQS------GYSLSGGQQQRLCIA 166
Cdd:PRK10895 80 IGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRA----------NELMEEFHIEhlrdsmGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKaDY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
....
gi 1875943321 245 QKKQ 248
Cdd:PRK10895 229 HVKR 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-250 |
1.60e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 29 NITLDIAKNKVTAFIGPSGCGKS----TLLRTFNKMYQLYPEqraeGGILLDGQNILtdNSDIALLRA----KVGMVFQK 100
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPS----GDIRFHGESLL--HASEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 PTpfpMSIYDNIAFGVRLFEKLS----------RADMD---ERVqwALTKAAlwNETKDKLHQsgysLSGGQQQRLCIAR 167
Cdd:PRK15134 101 PM---VSLNPLHTLEKQLYEVLSlhrgmrreaaRGEILnclDRV--GIRQAA--KRLTDYPHQ----LSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
....*
gi 1875943321 246 KKQTE 250
Cdd:PRK15134 250 HPYTQ 254
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-211 |
1.69e-22 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 95.97 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQRaeGGILLDGQNIltDNSDIALLRAKVGMVFQKPTPFPM 106
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGVWPPTA--GSVRLDGADL--SQWDREELGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAfgvRLFEklsrADmDERVQWALTKAALwNETKDKLHQ--------SGYSLSGGQQQRLCIARGIAIRPEVLLL 178
Cdd:COG4618 421 TIAENIA---RFGD----AD-PEKVVAAAKLAGV-HEMILRLPDgydtrigeGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190
....*....|....*....|....*....|....
gi 1875943321 179 DEPCSALDPISTGKIEELISELKAD-YTVVIVTH 211
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARgATVVVITH 525
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-232 |
3.51e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQR-AEGGILLDGQNILT-DNSDIAL 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKL------LTGELTpSSGEVRLNGRPLAAwSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAkvgmVFQKPTP--FPMSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWnetkDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:COG4559 76 RRA----VLPQHSSlaFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLA----HLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 168 -------GIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:COG4559 147 vlaqlwePVDGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-218 |
4.31e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 31 TLDIAKNKVTAFIGPSGCGKSTLLRT---FnkmyqLYPEQraeGGILLDGQniltDNSDIALLRAKVGMVFQKPTPFP-M 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLiagF-----LTPAS---GSLTLNGQ----DHTTTPPSRRPVSMLFQENNLFShL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGVRLFEKLSRADMDERVQWAlTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:PRK10771 87 TVAQNIGLGLNPGLKLNAAQREKLHAIA-RQMGI----EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1875943321 187 PISTGKIEELISEL--KADYTVVIVTHNMQQAAR 218
Cdd:PRK10771 162 PALRQEMLTLVSQVcqERQLTLLMVSHSLEDAAR 195
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-240 |
5.04e-22 |
|
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: 90.92 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNIltDNSDIAllr 91
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILR-----PTSGEIIFDGHPW--TRKDLH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 aKVGMVFQKPTPFP-MSIYDNIAFgVRLFEKLSradmDERVQWALTKAALWNETKDKLHQsgYSLsgGQQQRLCIARGIA 170
Cdd:TIGR03740 71 -KIGSLIESPPLYEnLTARENLKV-HTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQ--FSL--GMKQRLGIAIALL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 171 IRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELI---EFSDTDNL 240
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGyqgKINKSENL 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-238 |
5.93e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQniltdnsdIA-LLRakVGMVF 98
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE--PT---SGRVEVNGR--------VSaLLE--LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QkptpfP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:COG1134 100 H-----PeLTGRENIYLNGRLL-GLSRKEIDEKFDEIVEFAEL----GDFIDQPVKTYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 178 LDEpcsALdpiSTG------KIEELISELKADY-TVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTD 238
Cdd:COG1134 170 VDE---VL---AVGdaafqkKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-219 |
6.27e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 90.61 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILT-DNSDIALLRAK-VGMVFQK---- 100
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGL-----DDGSSGEVSLVGQPLHQmDEEARAKLRAKhVGFVFQSfmli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 PTpfpMSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK10584 101 PT---LNALENVELPA-LLRGESSRQSRNGAKALLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1875943321 181 PCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARC 219
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARC 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-211 |
1.10e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 93.63 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQraEGGILLDGQNILTDNSd 86
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLA---SLLMGYYPLT--EGEIRLDGRPLSSLSH- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 iALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFE-KLSRADmdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCI 165
Cdd:PRK10790 411 -SVLRQGVAMVQQDPVVLADTFLANVTLGRDISEeQVWQAL--ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-218 |
1.90e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQRAEGGILLDGQNILTDNS---DIA 88
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQREGRlarDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFP-MSIYDNIAFG-----------VRLFEKLSRadmdERVQWALTKAALWNETkdklHQSGYSLS 156
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNrLSVLENVLIGalgstpfwrtcFSWFTREQK----QRALQALTRVGMVHFA----HQRVSTLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAAR 218
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-244 |
6.13e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSMVTDASSSKI-QVRDLNFYY----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTllRTFNKMYQLYPEQRAEGGILL 75
Cdd:PRK09473 1 TVPLAQQQADALlDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQ--TAFALMGLLAANGRIGGSATF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 76 DGQNILT-DNSDIALLRA-KVGMVFQKP----TPFpMSIYDNIAFGVRLFEKLSRAD-MDERVQwaLTKAALWNETKDKL 148
Cdd:PRK09473 79 NGREILNlPEKELNKLRAeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKAEaFEESVR--MLDAVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 149 HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFM 226
Cdd:PRK09473 156 KMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVM 235
|
250
....*....|....*...
gi 1875943321 227 YLGELIEFSDTDNLFTAP 244
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-247 |
6.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNIlTDNSDIALLRAKVGMVFQKP-TPF 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQK---GKVLVSGIDT-GDFSKLQGIRKLVGIVFQNPeTQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 -PMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 183
Cdd:PRK13644 91 vGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGL----EKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 184 ALDPISTGKIEELISEL-KADYTVVIVTHNMQQaARCSDSTAFMYLGELIEFSDTDNLFTAPQKK 247
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-244 |
6.87e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.44 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQraeGGILLDGQNiLTDnSDIALLRAKVGMVFQKPTPFPM 106
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPYQ---GSLKINGIE-LRE-LDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGvrlfeklsRADM-DERVQWALTKAALWNETKDKLH--------QSGySLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PRK11174 438 TLRDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLPQgldtpigdQAA-GLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIEFSDTDNLFTAP 244
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-218 |
7.48e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.32 E-value: 7.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlYPEQRAEGGILLDGQNILTDNSD--IALLRAKVGMVFQKPTPF 104
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILG-----CLDKPTSGTYRVAGQDVATLDADalAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 P-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 183
Cdd:PRK10535 99 ShLTAAQNVEVPA-VYAGLERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1875943321 184 ALDPISTGKIEELISELKAD-YTVVIVTHNMQQAAR 218
Cdd:PRK10535 174 ALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQ 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-208 |
1.80e-20 |
|
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: 86.72 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 23 KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNILTDNSD------IALLRAKVG 95
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKC------IYGNYLPDSGsILVRHDGGWVDLAQaspreiLALRRRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 96 MVFQkptpF----P-MSIYDNIAfgvrlfEKLSRADMDERVqwALTKAA-----------LWnetkdklHQSGYSLSGGQ 159
Cdd:COG4778 97 YVSQ----FlrviPrVSALDVVA------EPLLERGVDREE--ARARARellarlnlperLW-------DLPPATFSGGE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVI 208
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-249 |
4.27e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 28 KNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLYPE--QRAEGGILLDGQNILTdnsdiALLRAK-VGMVFQKPTPF 104
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSL---TCAAALGILPAgvRQTAGRVLLDGKPVAP-----CALRGRkIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 PMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWN-ETKDKLHQsgYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 183
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENaARVLKLYP--FEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 184 ALDPISTGKIEELISELKADYT--VVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQT 249
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
12-250 |
7.60e-20 |
|
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: 85.65 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyQLYPEQRAEGGILLDGQNI----LTDNSDI 87
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG--RLAPDHGTATYIMRSGAELelyqLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRADMD--ERVQWALTKaalwneTKDKLHQsgysLSG 157
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDglrMRVSAGANIgerlmAIGARHYGNIRATAQDwlEEVEIDPTR------IDDLPRA----FSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 158 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFS 235
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250
....*....|....*
gi 1875943321 236 DTDNLFTAPQKKQTE 250
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQ 246
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-251 |
1.40e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.78 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGK---FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYqlypeQRAEGGILLDGQNILTDnSDI 87
Cdd:PTZ00265 382 KIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY-----DPTEGDIIINDSHNLKD-INL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKL-------------SRADMDERVQWALTKAALWNE-----TKDKLH 149
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLealsnyynedgndSQENKNKRNSCRAKCAGDLNDmsnttDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 150 Q---------------------------------------SGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIST 190
Cdd:PTZ00265 536 EmrknyqtikdsevvdvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 191 GKIEELISELKADYT--VVIVTHNMqQAARCSDSTAFMYLGELIEFSDTDNLFTAPQKKQTED 251
Cdd:PTZ00265 616 YLVQKTINNLKGNENriTIIIAHRL-STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-234 |
1.50e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.12 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 21 YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQniltdnsDIALLRAKVGMVFQk 100
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP--PD---SGTVTVRGR-------VSSLLGLGGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 ptpfpMSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:cd03220 99 -----LTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSEL----GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 181 PCSALDPISTGKIEELISELKADY-TVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-212 |
2.76e-19 |
|
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: 82.96 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTF--NKMYQLypeqrAEGGILLDGQNILTDNSDial 89
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEV-----TEGEILFKGEDITDLPPE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVG--MVFQKPTPFPmsiydniafGVRLfeklsradmdervqwaltkaalwnetKDKLHQSGYSLSGGQQQRLCIAR 167
Cdd:cd03217 73 ERARLGifLAFQYPPEIP---------GVKN--------------------------ADFLRYVNEGFSGGEKKRNEILQ 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISELK-ADYTVVIVTHN 212
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-211 |
3.50e-19 |
|
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: 82.60 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkMYQLYPeqRAEGGILLDGQNiltdnSDIALLRAKVGMVFQkptpfpm 106
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALA-GRRTGL--GVSGEVLINGRP-----LDKRSFRKIIGYVPQ------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 siyDNIafgvrLFEKLSradmderVQWALTKAAlwnetkdKLHqsgySLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:cd03213 90 ---DDI-----LHPTLT-------VRETLMFAA-------KLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 1875943321 187 PISTGKIEELISEL-KADYTVVIVTH 211
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIH 169
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-214 |
4.68e-19 |
|
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: 82.76 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK-FHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfnkMYQLYPEQRAEGGILLDGQNILTDNSDIALL 90
Cdd:cd03290 1 VQVTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNKNESEPSFEATRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAK--VGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDE-RVQWALTKAALWNETKdkLHQSGYSLSGGQQQRLCIAR 167
Cdd:cd03290 76 RNRysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1875943321 168 GIAIRPEVLLLDEPCSALD-PISTGKIEELISELKAD--YTVVIVTHNMQ 214
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-258 |
5.43e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLN--FYY--GKFH-----ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQNIlt 82
Cdd:PRK15112 5 LEVRNLSktFRYrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE--P---TSGELLIDDHPL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 DNSDIALLRAKVGMVFQKPT----PfPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNEtkdklHQSGYS--LS 156
Cdd:PRK15112 78 HFGDYSYRSQRIRMIFQDPStslnP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD-----HASYYPhmLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTV--VIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|....
gi 1875943321 235 SDTDNLFTAPQKKQTEDYITGRYG 258
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAGHFG 255
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-244 |
8.58e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSMVTDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI 80
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 81 LTDNSDiALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFE----KLSRADMdERVQWALTKAALwnetKDKLHQSGYSLS 156
Cdd:PRK10575 76 ESWSSK-AFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHgalgRFGAADR-EKVEEAISLVGL----KPLAHRLVDSLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
250
....*....|
gi 1875943321 235 SDTDNLFTAP 244
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
12-250 |
1.22e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.64 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGK----FHALKNITLDIAKNKVTAFIGPSGCGKStlLRTFNKMYQL-YPEQRAEGGILLDGQNI--LTDN 84
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIdYPGRVMAEKLEFNGQDLqrISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 85 SDIALLRAKVGMVFQKPTpfpMSIYDNIAFGVRLFEKL------SRADMDERVQWALTKAALwNETKDKLHQSGYSLSGG 158
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPM---TSLNPCYTVGFQIMEAIkvhqggNKKTRRQRAIDLLNQVGI-PDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSD 236
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
250
....*....|....
gi 1875943321 237 TDNLFTAPQKKQTE 250
Cdd:PRK11022 238 AHDIFRAPRHPYTQ 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
13-245 |
1.56e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.28 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyQLYPEQ-----RAEGGILLDGQNiLTDNSDI 87
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDAgevhyRMRDGQLRDLYA-LSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKPTP---FPMSIYDNI-----AFGVRLFEKLSRADMD--ERVQWALtkaalwnetkDKLHQSGYSLSG 157
Cdd:PRK11701 85 RLLRTEWGFVHQHPRDglrMQVSAGGNIgerlmAVGARHYGDIRATAGDwlERVEIDA----------ARIDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 158 GQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFMYLGELIEFS 235
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
250
....*....|
gi 1875943321 236 DTDNLFTAPQ 245
Cdd:PRK11701 235 LTDQVLDDPQ 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-212 |
2.19e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqL--YPEQRAEGG-ILLDGQNIL---TDNsd 86
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV------LmgHPKYEVTSGsILLDGEDILelsPDE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 iallRAKVG--MVFQKPTPFP-MSIYD--NIAFGVRLFEKLSRADMDERVQwalTKAALWNETKDKLHQS-GYSLSGGQQ 160
Cdd:COG0396 74 ----RARAGifLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFLKLLK---EKMKELGLDEDFLDRYvNEGFSGGEK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHN 212
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHY 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-221 |
2.64e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 7 ASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQraeGGILLDGQNIltdNSD 86
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDA---GSISLCGEPV---PSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 IALLRAKVGMVFQKPTPFP-MSIYDNIAFGVRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQQQRLCI 165
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPdFTVRENLLVFGRYF-GLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 166 ARGIAIRPEVLLLDEPCSALDPISTGKI-EELISELKADYTVVIVTHNMQQAARCSD 221
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCD 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-232 |
2.32e-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: 78.47 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyqlypeQRAEGGILLDGQnILTDN--SDIALLRAKVGMVFQKPTPF 104
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIS--------GRVEGGGTTSGQ-ILFNGqpRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 P-MSIYDNIAFGV--RLFEKLSRADMDERV------QWALTKAAlwnetkdklHQSGYSLSGGQQQRLCIARGIAIRPEV 175
Cdd:cd03234 94 PgLTVRETLTYTAilRLPRKSSDAIRKKRVedvllrDLALTRIG---------GNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 176 LLLDEPCSALDPISTGKIEELISELKADYTVVIVT-HnmQQAA---RCSDSTAFMYLGELI 232
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiH--QPRSdlfRLFDRILLLSSGEIV 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
27-245 |
2.88e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPeqrAEGGILLDGQNILT-DNSDIALLRAKVGMvfQKPTPFP 105
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLP---GQGEILLNGRPLSDwSAAELARHRAYLSQ--QQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 MSIYDNIAFGVrlfEKLSRADMDERVQWALTkAALwnETKDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLL 178
Cdd:COG4138 84 MPVFQYLALHQ---PAGASSEAVEQLLAQLA-EAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 179 DEPCSALDPISTGKIEELISELK-ADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-211 |
2.88e-17 |
|
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: 80.85 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 22 GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEqrAEGGILLDGQNIltDNSDIALLRAKVGMVFQKP 101
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL---IVGIWPP--TSGSVRLDGADL--KQWDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 102 TPFPMSIYDNIAfgvRLFEKlsrADMDERVQWAltKAALWNETKDKLHQsGY---------SLSGGQQQRLCIARGIAIR 172
Cdd:TIGR01842 402 ELFPGTVAENIA---RFGEN---ADPEKIIEAA--KLAGVHELILRLPD-GYdtvigpggaTLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1875943321 173 PEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTH 211
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-220 |
3.24e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 22 GKFHA--LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQ--NILTDNSDIALLRAKVGMV 97
Cdd:PRK11629 18 GSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQpmSKLSSAAKAELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 98 FQKPTPFP-MSIYDNIAFGVrLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVL 176
Cdd:PRK11629 93 YQFHHLLPdFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 177 LLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCS 220
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-243 |
6.97e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 7 ASSSKIQVRDLNFYYGKFH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltdns 85
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRL-----ASGKISILGQPT----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKPT---PFPMSIYDNIA---FGVRLFEKLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQ 159
Cdd:PRK15056 72 RQALQKNLVAYVPQSEEvdwSFPVLVEDVVMmgrYGHMGWLRRAKKRDRQIVTAALARVDM----VEFRHRQIGELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAfMYLGELIEFSDTD 238
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTE 226
|
....*
gi 1875943321 239 NLFTA 243
Cdd:PRK15056 227 TTFTA 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-240 |
7.86e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfnKMYQ-LYPEqrAEGGILLDGQNIltDNSDIALl 90
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTM----KMLTgLLPA--SEGEAWLFGQPV--DAGDIAT- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKptpFpmSIY------DNIAFGVRLFEkLSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLC 164
Cdd:NF033858 338 RRRVGYMSQA---F--SLYgeltvrQNLELHARLFH-LPAAEIAARVAEMLERFDL----ADVADALPDSLPLGIRQRLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 165 IARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCsDSTAFMYLG---------ELIE 233
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHAGrvlasdtpaALVA 486
|
....*..
gi 1875943321 234 FSDTDNL 240
Cdd:NF033858 487 ARGAATL 493
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-231 |
1.34e-16 |
|
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: 75.16 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYygkfHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNIlTDNSDIALLR 91
Cdd:cd03215 6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEA------LFGLRPPASGeITLDGKPV-TRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVfqkptP--------FP-MSIYDNIAFGVRLfeklsradmdervqwaltkaalwnetkdklhqsgyslSGGQQQR 162
Cdd:cd03215 75 AGIAYV-----PedrkreglVLdLSVAENIALSSLL-------------------------------------SGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-221 |
1.36e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPeqrAEGGILLDGQNIltDNSDIALLR 91
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTP---TAGTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPT-PFPMSIYDNIAFGVRlfEKLSRAD-MDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGRT--PHRSRFDtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSD 221
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCD 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-231 |
3.74e-16 |
|
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: 77.75 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTllrTFNKMYQLYPEqrAEGGILLDGQNILTDnsdIALLRAKVGMVFQKPTPFP 105
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPP--TSGTVLVGGKDIETN---LDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 -MSIYDNIAFgvrlFEKLSRADMDERvqwALTKAALWNET--KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPC 182
Cdd:TIGR01257 1017 hLTVAEHILF----YAQLKGRSWEEA---QLEMEAMLEDTglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 183 SALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-240 |
4.94e-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: 77.15 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY-----GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPEQRAEGGILLDGQNI-LTDNS 85
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKI---IAGVLEPTSGEVNVRVGDEWVdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAK--VGMVFQKPTPFP-MSIYDNI--AFGVRLFEKLSRadmdERVQWALtKAALWNETKDK--LHQSGYSLSGG 158
Cdd:TIGR03269 357 PDGRGRAKryIGILHQEYDLYPhRTVLDNLteAIGLELPDELAR----MKAVITL-KMVGFDEEKAEeiLDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELIseLKA----DYTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSI--LKAreemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*.
gi 1875943321 235 SDTDNL 240
Cdd:TIGR03269 510 GDPEEI 515
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-212 |
1.18e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypeQRAEGG-ILLDGQNILTDN--SDIALLRAKVGMvfqKPTp 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL------LPPAAGtIKLDGGDIDDPDvaEACHYLGHRNAM---KPA- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 fpMSIYDNIAFGVRLfeklsRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCS 183
Cdd:PRK13539 88 --LTVAENLEFWAAF-----LGGEELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 1875943321 184 ALDPISTGKIEELISE-LKADYTVVIVTHN 212
Cdd:PRK13539 157 ALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
11-219 |
1.25e-15 |
|
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: 74.51 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqrAEGGILLDGQNilTDNSDIA 88
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGDIQIDGVS--WNSVPLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRADMDERVQWalTKAALWNETKD----------------KLHQSG 152
Cdd:cd03289 74 KWRKAFGVIPQK---------------VFIFSGTFRKNLDPYGKW--SDEEIWKVAEEvglksvieqfpgqldfVLVDGG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 153 YSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:cd03289 137 CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLEC 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-225 |
2.27e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNILTDNSDIALLrAKVGMVFQKPTPFP 105
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQ--PDA---GSILIDGQEMRFASTTAALA-AGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 -MSIYDNIAFGvRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYsLSGGQQQRLCIARGIAIRPEVLLLDEPCSA 184
Cdd:PRK11288 93 eMTVAENLYLG-QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY-LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 185 LdpiSTGKIEEL---ISELKADYTVVI-VTHNMQQAARCSDS-TAF 225
Cdd:PRK11288 171 L---SAREIEQLfrvIRELRAEGRVILyVSHRMEEIFALCDAiTVF 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-211 |
2.82e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNkmyQLYPeqRAEGGILL-DGQNILtdnsdiallrakvgmvF--QKPtp 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWP--YGSGRIARpAGARVL----------------FlpQRP-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 fpmsiYdnIAFGvRLFEKLSRADM-----DERVQWALTKAALwNETKDKLHQS---GYSLSGGQQQRLCIARGIAIRPEV 175
Cdd:COG4178 436 -----Y--LPLG-TLREALLYPATaeafsDAELREALEAVGL-GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*.
gi 1875943321 176 LLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-218 |
3.67e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfnkmyQLYPEQRA--EGGI-LLDGqniltDNSDIA 88
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVeVLGG-----DMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAkvgmVFQK-------------PTpfpMSIYDNIAFGVRLFeKLSRADMDERVQwALTKAalwnetkdklhqSGYS- 154
Cdd:NF033858 70 HRRA----VCPRiaympqglgknlyPT---LSVFENLDFFGRLF-GQDAAERRRRID-ELLRA------------TGLAp 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 155 --------LSGGQQQR--LCIArgiAIR-PEVLLLDEPCSALDPISTGKIEELISELKAD---YTVVIVTHNMQQAAR 218
Cdd:NF033858 129 fadrpagkLSGGMKQKlgLCCA---LIHdPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-232 |
6.00e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY--------------GKFH-------ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEQrae 70
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkSLFKrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPTS--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 71 gGILLDGQNILTDNSDiaLLRAKVGMVF-QKPTpfpmSIYD-NIAFGVRLFEKLSRADmDERVQWALTKAALWNETKDKL 148
Cdd:cd03267 76 -GEVRVAGLVPWKRRK--KFLRRIGVVFgQKTQ----LWWDlPVIDSFYLLAAIYDLP-PARFKKRLDELSELLDLEELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 149 HQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQQAARCSDSTAFM 226
Cdd:cd03267 148 DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVI 227
|
....*.
gi 1875943321 227 YLGELI 232
Cdd:cd03267 228 DKGRLL 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-219 |
7.29e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 74.18 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqrAEGGILLDGqnILTDNS 85
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS------TEGEIQIDG--VSWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRAKVGMVFQKptpfpmsiydniafgVRLFEKLSRADMDERVQWalTKAALWNETK------------DKLH---- 149
Cdd:TIGR01271 1286 TLQTWRKAFGVIPQK---------------VFIFSGTFRKNLDPYEQW--SDEEIWKVAEevglksvieqfpDKLDfvlv 1348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 150 QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:TIGR01271 1349 DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-211 |
1.12e-14 |
|
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: 69.01 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPeqraegGILLDGQNIltdnsdiallr 91
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE------GIVTWGSTV----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 aKVGMVFQkptpfpmsiydniafgvrlfeklsradmdervqwaltkaalwnetkdklhqsgysLSGGQQQRLCIARGIAI 171
Cdd:cd03221 64 -KIGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 172 RPEVLLLDEPCSALDPIStgkIEELISELKaDY--TVVIVTH 211
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALK-EYpgTVILVSH 125
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-211 |
1.46e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.82 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltdnSDIAL--LRAKVGMVFQKPTP 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPL----TKLQLdsWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 FPMSIYDNIAFGvrlfeklsRAD-MDERVQWAltkAALWNETKDKLH----------QSGYSLSGGQQQRLCIARGIAIR 172
Cdd:PRK10789 401 FSDTVANNIALG--------RPDaTQQEIEHV---ARLASVHDDILRlpqgydtevgERGVMLSGGQKQRISIARALLLN 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 1875943321 173 PEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTH 211
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-243 |
1.82e-14 |
|
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: 72.67 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdnSDIAL--LRAKVGMVFQKPTPF 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI-----NESAEGEIIIDGLNI----AKIGLhdLRFKITIIPQDPVLF 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 PMSIYDNIafgvRLFEKLSradmDERVQWALTKAALW---NETKDKL-HQ---SGYSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:TIGR00957 1373 SGSLRMNL----DPFSQYS----DEEVWWALELAHLKtfvSALPDKLdHEcaeGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAArcsDSTAFMYL--GELIEFSDTDNLFTA 243
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM---DYTRVIVLdkGEVAEFGAPSNLLQQ 1509
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-253 |
3.14e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.99 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 22 GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLlrtfnkmyqlypeQRAEGGILLDGQNILTDN---SDIALLRA------ 92
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLI-------------AKAICGVTKDNWRVTADRmrfDDIDLLRLsprerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 -----KVGMVFQKPtpfpMSIYD-NIAFGVRLFEKLS----RADMDERVQWALTKAALW------NETKDKLHQSGYSLS 156
Cdd:PRK15093 85 klvghNVSMIFQEP----QSCLDpSERVGRQLMQNIPgwtyKGRWWQRFGWRKRRAIELlhrvgiKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD--YTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|....*....
gi 1875943321 235 SDTDNLFTAPQKKQTEDYI 253
Cdd:PRK15093 241 APSKELVTTPHHPYTQALI 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-211 |
3.27e-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: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 14 VRDLNFYYGKFHALKNITLDI-AKNKVtAFIGPSGCGKSTLLRtfnkmyqlypeqraeggiLLDGQnILTDNSDIALLR- 91
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSInPGDRI-GLVGRNGAGKSTLLK------------------ILAGE-LEPDSGEVSIPKg 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGV-RLFEKLSR------------ADMDE--RVQWALTKAALWN-ETK--------- 145
Cdd:COG0488 61 LRIGYLPQEPPLDDdLTVLDTVLDGDaELRALEAEleeleaklaepdEDLERlaELQEEFEALGGWEaEARaeeilsglg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 146 ---DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgkIEELISELKaDY--TVVIVTH 211
Cdd:COG0488 141 fpeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWLEEFLK-NYpgTVLVVSH 207
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-232 |
3.63e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlYPEQ------RAEGGILLDGQNILT-DNSDIALLRAkvgMVFQ 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGD---LTGGgaprgaRVTGDVTLNGEPLAAiDAPRLARLRA---VLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KPTP-FPMSIYDNIAFG----VRLFEKLSRADMDerVQWaltkAALWNETKDKL-HQSGYSLSGGQQQRLCIARGIA--- 170
Cdd:PRK13547 91 AAQPaFAFSAREIVLLGryphARRAGALTHRDGE--IAW----QALALAGATALvGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 171 ------IRPEVLLLDEPCSALDPISTGKIEELISELKADYT--VVIVTHNMQQAARCSDSTAFMYLGELI 232
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
42-245 |
4.63e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 42 FIGPSGCGKSTLLrtfNKMYQLYPeqrAEGGILLDGQNILT-DNSDIALLRAKVGMvfQKPTPFPMSIYDNIAfgvrlfe 120
Cdd:PRK03695 27 LVGPNGAGKSTLL---ARMAGLLP---GSGSIQFAGQPLEAwSAAELARHRAYLSQ--QQTPPFAMPVFQYLT------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 121 kLSRADM--DERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI-----AIRPE--VLLLDEPCSALDPISTG 191
Cdd:PRK03695 92 -LHQPDKtrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 192 KIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:PRK03695 171 ALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
6.00e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 2 SMVTDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEqraEGGILLDGQNIl 81
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PD---AGKITVLGVPV- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 tdNSDIALLRAKVGMVFQKPTPFP-MSIYDN-IAFGvRLFeKLSRADMDERVQWALTKAALWNETKDKLHQsgysLSGGQ 159
Cdd:PRK13536 106 --PARARLARARIGVVPQFDNLDLeFTVRENlLVFG-RYF-GMSTREIEAVIPSLLEFARLESKADARVSD----LSGGM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKI-EELISELKADYTVVIVTHNMQQAARCSD 221
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCD 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-254 |
7.50e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.62 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyqLYPEQRAEGGILLDGQNILTDN-SDIAll 90
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG---VYPHGTWDGEIYWSGSPLKASNiRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGMVFQKPTPFP-MSIYDNIAFGVRLFEKLSRADMDERVQWAltkAALWNETK---DKLHQSGYSLSGGQQQRLCIA 166
Cdd:TIGR02633 77 RAGIVIIHQELTLVPeLSVAENIFLGNEITLPGGRMAYNAMYLRA---KNLLRELQldaDNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLftapq 245
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM----- 228
|
....*....
gi 1875943321 246 kkQTEDYIT 254
Cdd:TIGR02633 229 --SEDDIIT 235
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
11-241 |
1.28e-13 |
|
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: 68.40 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 11 KIQVRDLNFYYGKF--HALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraEGGILLDGQNIltdnSDIA 88
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI----SKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 L--LRAKVGMVFQKPTPFPMSIYDNIafgvrlfeKLSRADMDERVQWALTKAALWNETKD-------KLHQSGYSLSGGQ 159
Cdd:cd03288 90 LhtLRSRLSIILQDPILFSGSIRFNL--------DPECKCTDDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 160 QQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARcSDSTAFMYLGELIEFSDTDN 239
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPEN 240
|
..
gi 1875943321 240 LF 241
Cdd:cd03288 241 LL 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-238 |
1.60e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.83 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYPEqraEGGIL----------------L 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT---SGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 76 DGQN---------------ILTDNSDIALLRAKVGMVFQKPtpfpMSIYDNIAFGVRLFEKLSRADM--DERVQWALTka 138
Cdd:TIGR03269 78 VGEPcpvcggtlepeevdfWNLSDKLRRRIRKRIAIMLQRT----FALYGDDTVLDNVLEALEEIGYegKEAVGRAVD-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 139 aLWNETK--DKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQ 214
Cdd:TIGR03269 152 -LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260
....*....|....*....|....
gi 1875943321 215 QAARCSDSTAFMYLGELIEFSDTD 238
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPD 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-213 |
3.13e-13 |
|
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: 69.20 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 4 VTDASSSKIQVRDLNFYYGKFH--ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQnil 81
Cdd:TIGR00957 629 IKPGEGNSITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKGS--- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 tdnsdiallrakVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMdERVQWALTKAALWNETKDKLHQSGYSLSGGQQQ 161
Cdd:TIGR00957 701 ------------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVL-EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQ 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 162 RLCIARGIAIRPEVLLLDEPCSALDPiSTGK--IEELISE--LKADYTVVIVTHNM 213
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDA-HVGKhiFEHVIGPegVLKNKTRILVTHGI 822
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-226 |
4.15e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPeqrAEGGILLDGQ--NILtDNSDIAL 89
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--P---TKGTITINNInyNKL-DHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LraKVGMVFQKPTPF-PMSIYDNIAFGVRLFEK------LSRADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQR 162
Cdd:PRK09700 80 L--GIGIIYQELSVIdELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYT-VVIVTHNMQQAARCSDSTAFM 226
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVM 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-218 |
4.36e-13 |
|
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: 68.78 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPeqrAEGGILLDGqniltdnsdiallraKVGMVFQKPTPFPM 106
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEP---SEGKIKHSG---------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGVRlFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:TIGR01271 502 TIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190
....*....|....*....|....*....|...
gi 1875943321 187 PISTGKI-EELISELKADYTVVIVTHNMQQAAR 218
Cdd:TIGR01271 581 VVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-242 |
5.99e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 8 SSSKIQVRDLNFYY--GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQRaeGGILLDGQNI----L 81
Cdd:PLN03232 1231 SRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSML---NALFRIVELEK--GRIMIDDCDVakfgL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 TDnsdialLRAKVGMVFQKPTPFPMSIydniAFGVRLFEKLSRADMDERVQWALTKAALWNET---KDKLHQSGYSLSGG 158
Cdd:PLN03232 1306 TD------LRRVLSIIPQSPVLFSGTV----RFNIDPFSEHNDADLWEALERAHIKDVIDRNPfglDAEVSEGGENFSVG 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIEFSDTD 238
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQ 1454
|
....
gi 1875943321 239 NLFT 242
Cdd:PLN03232 1455 ELLS 1458
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-211 |
8.14e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 23 KFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRtfnKMYQLYPEQRAEGGILLDGQNIltdNSDIALLRAkvgmvfqkpt 102
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLR---LLAGALKGTPVAGCVDVPDNQF---GREASLIDA---------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 103 pfpMSIYDNIAFGVRLfekLSRAdmdervqwALTKAALWnetKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPC 182
Cdd:COG2401 106 ---IGRKGDFKDAVEL---LNAV--------GLSDAVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|....
gi 1875943321 183 SALDPiSTGKI-----EELISELKAdyTVVIVTH 211
Cdd:COG2401 165 SHLDR-QTAKRvarnlQKLARRAGI--TLVVATH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-181 |
1.53e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNfyygKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNI-LTDNSD---- 86
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA------LFGADPADSGeIRLDGKPVrIRSPRDaira 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 87 -IALL---RAKVGMVFqkptpfPMSIYDNIAFGVrlFEKLSRAD-MDERVQWALTKAALwnetkDKL-------HQSGYS 154
Cdd:COG1129 328 gIAYVpedRKGEGLVL------DLSIRENITLAS--LDRLSRGGlLDRRRERALAEEYI-----KRLriktpspEQPVGN 394
|
170 180
....*....|....*....|....*..
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEP 181
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-211 |
4.89e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.56 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLYpeqraeggillDGQNILTDNSDIALLRakvgmvfQKPtpfpm 106
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----------SGRIGMPEGEDLLFLP-------QRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 siYdnIAFGvRLFEKLSRAdmdervqwaltkaalWNETkdklhqsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:cd03223 74 --Y--LPLG-TLREQLIYP---------------WDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*
gi 1875943321 187 PISTGKIEELISELKAdyTVVIVTH 211
Cdd:cd03223 124 EESEDRLYQLLKELGI--TVISVGH 146
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-211 |
5.52e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyqlypEQRAEGGILLDGQNIltdnsdiallr 91
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG------ELEPDSGTVKLGETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 aKVGMVFQKPTPFP--MSIYDNIafgvrlfeklSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:COG0488 379 -KIGYFDQHQEELDpdKTVLDEL----------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1875943321 170 AIRPEVLLLDEPCSALDPIStgkIEELISELKaDY--TVVIVTH 211
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET---LEALEEALD-DFpgTVLLVSH 487
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-247 |
6.83e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPeqRAEGGILLDGQNILTDNSDIALL---------RAKVGMV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKV---LYGALP--RTSGYVTLDGHEVVTRSPQDGLAngivyisedRKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 98 FQkptpfpMSIYDNIAF-GVRLFEKLS-RADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEV 175
Cdd:PRK10762 343 LG------MSVKENMSLtALRYFSRAGgSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 176 LLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELI-EFSDTDnlftAPQKK 247
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGRISgEFTREQ----ATQEK 486
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-214 |
9.07e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.95 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfnKMYQ--LYPEqraEGGILLDGQNILTDnsDIALLRaKVGMVF-QK- 100
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTI----KMLTgiLVPT---SGEVRVLGYVPFKR--RKEFAR-RIGVVFgQRs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 101 ------PT--PFPM--SIYDniafgvrlfekLSRADMDERVQWaLTKAaLwnETKDKLHQSGYSLSGGQQQRLCIArgiA 170
Cdd:COG4586 106 qlwwdlPAidSFRLlkAIYR-----------IPDAEYKKRLDE-LVEL-L--DLGELLDTPVRQLSLGQRMRCELA---A 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 171 I---RPEVLLLDEPCSALDPISTGKIEELISELKADY--TVVIVTHNMQ 214
Cdd:COG4586 168 AllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-245 |
9.61e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 29 NITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPEQraEGGILLDGQNILTDNSDIALL--RAKVGMVFQKPTPFP- 105
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTRPQ--KGRIVLNGRVLFDAEKGICLPpeKRRIGYVFQDARLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 MSIYDNIAFGVRlfeKLSRADMDERVQwALTKAALwnetkdkLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSAL 185
Cdd:PRK11144 91 YKVRGNLRYGMA---KSMVAQFDKIVA-LLGIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 186 D-PistgKIEELISEL-----KADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNLFTAPQ 245
Cdd:PRK11144 160 DlP----RKRELLPYLerlarEINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-211 |
2.78e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 5 TDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTF--NKMYQLypeqrAEGGILLDGQNILT 82
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKI-----LEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 83 DNSDIallRAKVG--MVFQKPTPFPMsiYDNIAF------GVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQS--- 151
Cdd:CHL00131 76 LEPEE---RAHLGifLAFQYPIEIPG--VSNADFlrlaynSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNvne 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 152 GYslSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELK-ADYTVVIVTH 211
Cdd:CHL00131 151 GF--SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITH 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-218 |
3.44e-11 |
|
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: 61.80 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPeqrAEGGILLDGqniltdnsdiallraKVGMVFQKPTPFPM 106
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEP---SEGKIKHSG---------------RISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGVrlfeklsraDMDERVQWALTKAALWNE------TKDK--LHQSGYSLSGGQQQRLCIARGIAIRPEVLLL 178
Cdd:cd03291 113 TIKENIIFGV---------SYDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1875943321 179 DEPCSALDPISTGKI-EELISELKADYTVVIVTHNMQQAAR 218
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-211 |
5.66e-11 |
|
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: 60.06 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 14 VRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqLYPEqraEGGILLDGQNILTDNSD----IAL 89
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRPD---SGEVRWNGTPLAEQRDEphenILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMvfqKPTpfpMSIYDNIAFGVRLFEKLSRADMDervqwALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:TIGR01189 78 LGHLPGL---KPE---LSALENLHFWAAIHGGAQRTIED-----ALAAVGL----TGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISE-LKADYTVVIVTH 211
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-211 |
7.90e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 60.35 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLL---------RTFNKMYQLYPEQR-----------AEG---GILLDgQNIL 81
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqRRYVESLSAYARQFlgqmdkpdvdsIEGlspAIAID-QKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 TDNSdiallRAKVGMVfqkptpfpMSIYDNIAFgvrLFeklSRADMDERVQWaLTKAALWNETkdkLHQSGYSLSGGQQQ 161
Cdd:cd03270 88 SRNP-----RSTVGTV--------TEIYDYLRL---LF---ARVGIRERLGF-LVDVGLGYLT---LSRSAPTLSGGEAQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 162 RLCIARGIAIR-PEVL-LLDEPCSALDPISTGKIEELISELK-ADYTVVIVTH 211
Cdd:cd03270 145 RIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEH 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-253 |
1.03e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyqLYPEQRAEGGILLDGQ-----NIL-TDNSDIALLRAKVGMVFQ 99
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG---VYPHGTYEGEIIFEGEelqasNIRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 kptpfpMSIYDNIAFGVRLfEKLSRADMDERVQWAltkAALWNETKDKL--HQSGYSLSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PRK13549 97 ------LSVLENIFLGNEI-TPGGIMDYDAMYLRA---QKLLAQLKLDInpATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 178 LDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDSTAFMYLGELIEfsdtdnlfTAPQKKQTEDYI 253
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAhGIACIYISHKLNEVKAISDTICVIRDGRHIG--------TRPAAGMTEDDI 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-225 |
1.11e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqRAEGGILLDGQNIlTDNSDIALLRAKVGMVFQKPTPFP 105
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSILYLGKEV-TFNGPKSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 -MSIYDNIAFGVRLFEKLSRADMDERVQWA---LTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEP 181
Cdd:PRK10762 93 qLTIAENIFLGREFVNRFGRIDWKKMYAEAdklLARLNL----RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 182 CSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAAR-CSDSTAF 225
Cdd:PRK10762 169 TDALTDTETESLFRVIRELKSqGRGIVYISHRLKEIFEiCDDVTVF 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-211 |
1.98e-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: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHALKNITLDI---AKNKVtafIGPSGCGKSTLLRTFNKMYQLYP-EQRAEGGIlldgqniltdnsdiallraKVG 95
Cdd:TIGR03719 14 VPPKKEILKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKDFNgEARPQPGI-------------------KVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 96 MVFQKPTPFP-MSIYDNIAFGVR-----------LFEKLSR--ADMDE------RVQWALTKAALWN-ETK-----DKLH 149
Cdd:TIGR03719 72 YLPQEPQLDPtKTVRENVEEGVAeikdaldrfneISAKYAEpdADFDKlaaeqaELQEIIDAADAWDlDSQleiamDALR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 150 -----QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAdyTVVIVTH 211
Cdd:TIGR03719 152 cppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-242 |
2.34e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNI----LTDnsdialLRAKVGMVFQKPT 102
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDIskfgLMD------LRKVLGIIPQAPV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 103 PFPMSIydniAFGVRLFEKLSRADMDERVQWALTKAALWNETKD---KLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:PLN03130 1324 LFSGTV----RFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGldaEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1875943321 180 EPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCsDSTAFMYLGELIEFSDTDNLFT 242
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC-DRILVLDAGRVVEFDTPENLLS 1461
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-255 |
2.35e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNI--LTDNSDIAL 89
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-----VPPDSGTLEIGGNPCarLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 lraKVGMVFQKPTPFP-MSIYDNIAFGVRlfeklSRADMDERVQWALtkAALwnETKDKLHQSGYSLSGGQQQRLCIARG 168
Cdd:PRK15439 87 ---GIYLVPQEPLLFPnLSVKENILFGLP-----KRQASMQKMKQLL--AAL--GCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 169 IAIRPEVLLLDEPCSALDPIST----GKIEELiseLKADYTVVIVTHNMQQAARCSDSTAFM------YLGELIEFSDTD 238
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETerlfSRIREL---LAQGVGIVFISHKLPEIRQLADRISVMrdgtiaLSGKTADLSTDD 231
|
250
....*....|....*..
gi 1875943321 239 nLFTAPQKKQTEDYITG 255
Cdd:PRK15439 232 -IIQAITPAAREKSLSA 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-235 |
2.77e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.18 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDgqniltdnSDIAllrakvgMVFQKPTPFPM 106
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----SEGRVWAE--------RSIA-------YVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFgvrlFEKLSRADMDERVQ-------WALTKAALWNETKDKlhqsGYSLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:PTZ00243 736 TVRGNILF----FDEEDAARLADAVRvsqleadLAQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 180 EPCSALDP-ISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAFMylGELIEFS 235
Cdd:PTZ00243 808 DPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG--DGRVEFS 862
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-210 |
3.89e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPEQRAEGGILLDGQNIltdnsDIALLRAKVGMVFQKPTPF 104
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 PM-SIYDNIAFG--VRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGY--SLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:TIGR00955 112 PTlTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|.
gi 1875943321 180 EPCSALDPISTGKIEELISELKADYTVVIVT 210
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-213 |
4.37e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 9 SSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqLYPEQRAEGGILLDGQniltdnsdia 88
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV-----LGLVAPDEGVIKRNGK---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 lLRakVGMVFQK----PT-PFPMSIYDNIAFGVRlfeklsRADMD---ERVQwaltKAALWNETKDKlhqsgysLSGGQQ 160
Cdd:PRK09544 67 -LR--IGYVPQKlyldTTlPLTVNRFLRLRPGTK------KEDILpalKRVQ----AGHLIDAPMQK-------LSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA--DYTVVIVTHNM 213
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-211 |
8.48e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 44 GPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTDNSDIAllRAKVGMVFQKPTPFPMSIYDNIAFgvrlfekLS 123
Cdd:cd03231 33 GPNGSGKTTLLRILAGL-----SPPLAGRVLLNGGPLDFQRDSIA--RGLLYLGHAPGIKTTLSVLENLRF-------WH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 124 RADMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELI-SELKA 202
Cdd:cd03231 99 ADHSDEQVEEALARVGL----NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCAR 174
|
....*....
gi 1875943321 203 DYTVVIVTH 211
Cdd:cd03231 175 GGMVVLTTH 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-240 |
3.25e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 24 FHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqlypeqraeGGILLDGQNILTDNSDIALLRAKVGMVFQkptp 103
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNII-------------GGSLSPTVGKVDRNGEVSVIAISAGLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 fpMSIYDNIAFGVRLF---EKLSRADMDERVQWAltkaalwnETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK13546 100 --LTGIENIEFKMLCMgfkRKEIKAMTPKIIEFS--------ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 181 PCSALDPISTGKIEELISELK-ADYTVVIVTHNMQQAARCSDSTAFMYLGELIEFSDTDNL 240
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-214 |
4.21e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 1 MSMVTDASSSKI--QVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRtfnkmyqlypeqraeggiLLDGQ 78
Cdd:PRK11147 307 MQVEEASRSGKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK------------------LMLGQ 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 79 niLTDNSDiallRAKVGmvfqkpTPFPMSIYDNiafgvrlfeklSRADMDERvqwaltKAALWN--ETKD-------KLH 149
Cdd:PRK11147 369 --LQADSG----RIHCG------TKLEVAYFDQ-----------HRAELDPE------KTVMDNlaEGKQevmvngrPRH 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 150 QSGY----------------SLSGGQQQRLCIARgIAIRPEVLL-LDEPCSALDpistgkIE--ELISELKADY--TVVI 208
Cdd:PRK11147 420 VLGYlqdflfhpkramtpvkALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLD------VEtlELLEELLDSYqgTVLL 492
|
....*.
gi 1875943321 209 VTHNMQ 214
Cdd:PRK11147 493 VSHDRQ 498
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-210 |
4.88e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 15 RDLNFY----YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqlypEQRAEGG-----ILLDGQNIltdns 85
Cdd:cd03232 7 KNLNYTvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--------AGRKTAGvitgeILINGRPL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 86 DIALLRaKVGMVFQKPTPFPMSIydniafgVR---LFEKLSRAdmdervqwaltkaalwnetkdklhqsgysLSGGQQQR 162
Cdd:cd03232 74 DKNFQR-STGYVEQQDVHSPNLT-------VRealRFSALLRG-----------------------------LSVEQRKR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1875943321 163 LCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVT 210
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCT 164
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-186 |
5.28e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYY---GKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPeqRAEGGIlldgqniltdnsdia 88
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASV--------------- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 LLRAKVGMVFQKPTPFPMSIYDNIAFGvrlfeklsrADMD-ERVQWALTKAALWNETK-------DKLHQSGYSLSGGQQ 160
Cdd:PLN03130 676 VIRGTVAYVPQVSWIFNATVRDNILFG---------SPFDpERYERAIDVTALQHDLDllpggdlTEIGERGVNISGGQK 746
|
170 180
....*....|....*....|....*.
gi 1875943321 161 QRLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-242 |
6.62e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 4 VTDASSSKIQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGcgkSTLLRTFNKMYQLYPEQRAEGgilldgQNILTD 83
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G---AA**RGALPAHV*GPDAGRRP------WRF*TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 84 NSDIALLRAKVGMvfQKPTPF----PMSIYDN---IAFGVRLFEKLSRADMDERVQ-WALTKAAlwnetkdklHQSGYSL 155
Cdd:NF000106 77 CANRRALRRTIG*--HRPVR*grreSFSGRENlymIGR*LDLSRKDARARADELLErFSLTEAA---------GRAAAKY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 156 SGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKI-EELISELKADYTVVIVTHNMQQAARCSDSTAFMYLGELIEF 234
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
....*...
gi 1875943321 235 SDTDNLFT 242
Cdd:NF000106 226 GKVDELKT 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-211 |
9.62e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKmyqlypEQraeggILLDGQNILTDNSDIALL-----RAKVGmvfqkp 101
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNG------EV-----LLDDGRIIYEQDLIVARLqqdppRNVEG------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 102 tpfpmSIYDNIAFGV-------RLFEKLSRADMDE----------RVQWALTKAALW---NETKDKLHQSGY-------S 154
Cdd:PRK11147 82 -----TVYDFVAEGIeeqaeylKRYHDISHLVETDpseknlnelaKLQEQLDHHNLWqleNRINEVLAQLGLdpdaalsS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDpISTgkIEELISELKaDY--TVVIVTH 211
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLK-TFqgSIIFISH 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-255 |
9.69e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYqlypeQRAEGGILLDGQNILTDNSDIAlLRAKVGMVFQKPTPF- 104
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIY-----QKDSGSILFQGKEIDFKSSKEA-LENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 PMSIYDNIAFGvRLFEKLSRADMDErvqwaltkaaLWNETK---DKL------HQSGYSLSGGQQQRLCIARGIAIRPEV 175
Cdd:PRK10982 87 QRSVMDNMWLG-RYPTKGMFVDQDK----------MYRDTKaifDELdididpRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 176 LLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEfsdtdnlfTAPQKKQTEDYIT 254
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDKII 227
|
.
gi 1875943321 255 G 255
Cdd:PRK10982 228 A 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-223 |
9.81e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 9.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLlrtfnkMYQL---YPEQRAEGGILLDGQniLTDNSDIallRA--KVGMVF-- 98
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTL------MKVLsgvYPHGSYEGEILFDGE--VCRFKDI---RDseALGIVIih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFP-MSIYDNIAFGvrlFEKLSRADMDervqWALTkaalWNETKDKLHQSGYSLS--------G-GQQQRLCIARG 168
Cdd:NF040905 85 QELALIPyLSIAENIFLG---NERAKRGVID----WNET----NRRARELLAKVGLDESpdtlvtdiGvGKQQLVEIAKA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 169 IAIRPEVLLLDEPCSALDPISTGKIEELISELKA-DYTVVIVTHNMQQAARCSDST 223
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSI 209
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-219 |
1.39e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQLypeqrAEGGILLDGQNIltDNSDIALLRAKVGMVFQKPTPFPM 106
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV-----CGGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNI-----AFGVRLFEKLSRADMDERVqwaltkaALWNETKD-KLHQSGYSLSGGQQQRLCIARGIAIRPE-VLLLD 179
Cdd:PTZ00243 1399 TVRQNVdpfleASSAEVWAALELVGLRERV-------ASESEGIDsRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1875943321 180 EPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARC 219
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY 1511
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-231 |
1.47e-08 |
|
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: 54.83 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 29 NITLDIAKNKVTAFIGPSGCGKSTLLRTfnkMYQLYPeQRAEGGILLDGQNILTDNSDIALlRAKVGMV---FQKPTPFP 105
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQA---LFGAYP-GKFEGNVFINGKPVDIRNPAQAI-RAGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 106 -MSIYDNIAFGV-RLFEKLSRADmDERVQWALTKAAlwnetkDKLHQSGYS-------LSGGQQQRLCIARGIAIRPEVL 176
Cdd:TIGR02633 353 iLGVGKNITLSVlKSFCFKMRID-AAAELQIIGSAI------QRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 177 LLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGEL 231
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-240 |
1.94e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYygKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMYQLYPeqRAEGGILLDGQNILTDNSDIALlra 92
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDK--RAGGEIRLNGKDISPRSPLDAV--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 93 KVGMVF----QKPTPF--PMSIYDNIAFGVRLfeKLSR--------ADMDERvQWALTKAALWNETKDKLHQSGYSLSGG 158
Cdd:PRK09700 337 KKGMAYitesRRDNGFfpNFSIAQNMAISRSL--KDGGykgamglfHEVDEQ-RTAENQRELLALKCHSVNQNITELSGG 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIE-FSD 236
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTN 493
|
....
gi 1875943321 237 TDNL 240
Cdd:PRK09700 494 RDDM 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-213 |
2.08e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 26 ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltDNSD--------IALL---RAKV 94
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGI-----REKSAGTITLHGKKI--NNHNaneainhgFALVteeRRST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 95 GMVFQKPTPFPmSIYDNIAFGVRLFEKLSRADMDERVQWALTKAalwnETKDKLHQSGY-SLSGGQQQRLCIARGIAIRP 173
Cdd:PRK10982 336 GIYAYLDIGFN-SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSM----RVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1875943321 174 EVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNM 213
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEM 451
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-186 |
2.29e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPEQRAEggilldgqniltdnsdiALLRAKVGMVFQKPTPFPM 106
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAETSS-----------------VVIRGSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGVRlFEKlsradmdERVQWALTKAALWNE-------TKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLD 179
Cdd:PLN03232 694 TVRENILFGSD-FES-------ERYWRAIDVTALQHDldllpgrDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
....*..
gi 1875943321 180 EPCSALD 186
Cdd:PLN03232 766 DPLSALD 772
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-211 |
3.13e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 44 GPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNILTD----NSDIALLRAKVGMvfqKP--TPFpmsiyDNIAFGVR 117
Cdd:PRK13538 34 GPNGAGKTSLLRILAGL-----ARPDAGEVLWQGEPIRRQrdeyHQDLLYLGHQPGI---KTelTAL-----ENLRFYQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 118 LFEKLSradmDERVQWALTKAALwnetkdklhqSGY------SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTG 191
Cdd:PRK13538 101 LHGPGD----DEALWEALAQVGL----------AGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|.
gi 1875943321 192 KIEELISE-LKADYTVVIVTH 211
Cdd:PRK13538 167 RLEALLAQhAEQGGMVILTTH 187
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-211 |
3.87e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTF--NKMYQLypeqrAEGGILLDGQNILT-DNSDia 88
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEV-----TGGTVEFKGKDLLElSPED-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 89 llRAKVG--MVFQKPTPFP-------MSIYDNIAFGVRLFEKLSRADMDERVQwalTKAALWNETKDKLHQS-GYSLSGG 158
Cdd:PRK09580 75 --RAGEGifMAFQYPVEIPgvsnqffLQTALNAVRSYRGQEPLDRFDFQDLME---EKIALLKMPEDLLTRSvNVGFSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELK-ADYTVVIVTH 211
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTH 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-218 |
5.77e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.34 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlypeqraegGILLDGQnILTDNSDIA--LLRaKVGMVFQKPTPF 104
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ---------GNNFTGT-ILANNRKPTkqILK-RTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 105 P-MSIYDNIAFG--VRLFEKLSRadmDERVQWALTKAALWNETKDKLHQSGYS----LSGGQQQRLCIARGIAIRPEVLL 177
Cdd:PLN03211 153 PhLTVRETLVFCslLRLPKSLTK---QEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1875943321 178 LDEPCSALDPISTGKIEELISELkADYTVVIVTHNMQQAAR 218
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSR 269
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-202 |
8.37e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFY-YGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNIltDNSDIALL 90
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEA------LAGLRPPASGsIRLDGEDI--TGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RA-----------KVGMVfqkPTpfpMSIYDNIAFGVRLFEKLSRA---DMDERVQWALTKAALWNETKDKLHQSGYSLS 156
Cdd:COG3845 331 RRlgvayipedrlGRGLV---PD---MSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELIEEFDVRTPGPDTPARSLS 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1875943321 157 GGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKA 202
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD 450
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-231 |
1.52e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 28 KNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmYQLYPeQRAeGGILLDGQNILTDNSDIALLRAKV---------GMVF 98
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETL---YGLRP-ARG-GRIMLNGKEINALSTAQRLARGLVylpedrqssGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 99 QKPTPFPMS--IYDNIAFGVRlfEKLSRADMdERVQWALtkaalwNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVL 176
Cdd:PRK15439 355 DAPLAWNVCalTHNRRGFWIK--PARENAVL-ERYRRAL------NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 177 LLDEPCSALDPISTGKIEELISELKADYTVVI-VTHNMQQAARCSDSTAFMYLGEL 231
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-216 |
1.89e-07 |
|
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: 49.63 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 17 LNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqlypeqraegGILLDGQNILTDNsdiallrakvgm 96
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNE---------------GLYASGKARLISF------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 97 vfqKPTPFPMSIydnIAFGvrlfeKLSRadmdervqwaLTKAALwneTKDKLHQSGYSLSGGQQQRLCIARGIAIRPE-- 174
Cdd:cd03238 54 ---LPKFSRNKL---IFID-----QLQF----------LIDVGL---GYLTLGQKLSTLSGGELQRVKLASELFSEPPgt 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1875943321 175 VLLLDEPCSALDPIstgKIEELISELKA----DYTVVIVTHN---MQQA 216
Cdd:cd03238 110 LFILDEPSTGLHQQ---DINQLLEVIKGlidlGNTVILIEHNldvLSSA 155
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-187 |
3.63e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYYGK--FhALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIltDNSDI 87
Cdd:PRK10522 321 QTLELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ--PQS---GEILLDGKPV--TAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 88 ALLRAKVGMVFQKptpfpmsiydniafgVRLFEKLsradMDERVQWALTKAA-LWNET---KDKLHQSGY-----SLSGG 158
Cdd:PRK10522 393 EDYRKLFSAVFTD---------------FHLFDQL----LGPEGKPANPALVeKWLERlkmAHKLELEDGrisnlKLSKG 453
|
170 180
....*....|....*....|....*....
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDP 187
Cdd:PRK10522 454 QKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-211 |
3.72e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 19 FYYGKFHALKNITLDI---AKNKVtafIGPSGCGKSTLLRTFNKMYQLYpeqraeggillDGQNILTDNsdiallrAKVG 95
Cdd:PRK11819 15 VVPPKKQILKDISLSFfpgAKIGV---LGLNGAGKSTLLRIMAGVDKEF-----------EGEARPAPG-------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 96 MVFQKPTPFP-MSIYDNIAFGVR-LFEKLSR------------ADMDE------RVQWALTKAALWN-ETK-----DKLH 149
Cdd:PRK11819 74 YLPQEPQLDPeKTVRENVEEGVAeVKAALDRfneiyaayaepdADFDAlaaeqgELQEIIDAADAWDlDSQleiamDALR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 150 -----QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELIselkADY--TVVIVTH 211
Cdd:PRK11819 154 cppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
43-219 |
1.19e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 43 IGPSGCGKSTLL--------RTFNKMYQLYPEQRAEGGILLD-GQNILTDNSDIAL---LRAKVGMVFqkptpfpMSIY- 109
Cdd:PRK10938 292 VGPNGAGKSTLLslitgdhpQGYSNDLTLFGRRRGSGETIWDiKKHIGYVSSSLHLdyrVSTSVRNVI-------LSGFf 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 110 DNIAfgvrLFEKLSRADMDERVQWaLTKAALWNETKDKLHQSgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIS 189
Cdd:PRK10938 365 DSIG----IYQAVSDRQQKLAQQW-LDILGIDKRTADAPFHS---LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN 436
|
170 180 190
....*....|....*....|....*....|....
gi 1875943321 190 TGK----IEELISElkADYTVVIVTHNMQQAARC 219
Cdd:PRK10938 437 RQLvrrfVDVLISE--GETQLLFVSHHAEDAPAC 468
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
43-211 |
1.41e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 43 IGPSGCGKSTLLRTFNKMYQLYpeqraeGGILldgqnilTDNSDIALLrakvgMVFQKP----------TPFPMSIYDNI 112
Cdd:TIGR00954 484 CGPNGCGKSSLFRILGELWPVY------GGRL-------TKPAKGKLF-----YVPQRPymtlgtlrdqIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 113 AFGVR---LFEKLSRADMDErvqwALTKAALWNETKDKLHQsgysLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPIS 189
Cdd:TIGR00954 546 RRGLSdkdLEQILDNVQLTH----ILEREGGWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180
....*....|....*....|..
gi 1875943321 190 TGKIEELISElkADYTVVIVTH 211
Cdd:TIGR00954 618 EGYMYRLCRE--FGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-221 |
1.87e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.79 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 20 YYGKFHaLKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqlypeqraEGGILLDGQNILTDNSDIALlrakvgmvfq 99
Cdd:cd03237 9 TLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEGDIEIELDTVSY---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KP----TPFPMSIYDniafgvRLFEKLsrADMDERVQWaltKAALWNETK--DKLHQSGYSLSGGQQQRLCIARGIAIRP 173
Cdd:cd03237 66 KPqyikADYEGTVRD------LLSSIT--KDFYTHPYF---KTEIAKPLQieQILDREVPELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 174 EVLLLDEPCSALDP----ISTGKIEELIseLKADYTVVIVTHNMQQAARCSD 221
Cdd:cd03237 135 DIYLLDEPSAYLDVeqrlMASKVIRRFA--ENNEKTAFVVEHDIIMIDYLAD 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
64-209 |
3.70e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 64 YPeQRAEGGILLDGQNILTDNSD------IALL---RAKVGMVFQkptpfpMSIYDNIAFGV-RLFEKLSRADMDERVQW 133
Cdd:PRK13549 312 YP-GRWEGEIFIDGKPVKIRNPQqaiaqgIAMVpedRKRDGIVPV------MGVGKNITLAAlDRFTGGSRIDDAAELKT 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 134 AltkaalwNETKDKLH-------QSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTV 206
Cdd:PRK13549 385 I-------LESIQRLKvktaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVA 457
|
...
gi 1875943321 207 VIV 209
Cdd:PRK13549 458 IIV 460
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-71 |
3.90e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 3.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLlrTFNKMYqlypeqrAEG 71
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL--AFDTIY-------AEG 51
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
25-53 |
4.21e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.71 E-value: 4.21e-06
10 20
....*....|....*....|....*....
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTL 53
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-209 |
4.43e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 30 ITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGG-ILLDGQNILTdNSDIALLRAkvGMVF-----QKPTP 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKL------LYGATRRTAGqVYLDGKPIDI-RSPRDAIRA--GIMLcpedrKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 104 FPM-SIYDNIA---------FGVRLFEKLSRADMDERVQwaltkaALWNETKDKlHQSGYSLSGGQQQRLCIARGIAIRP 173
Cdd:PRK11288 343 IPVhSVADNINisarrhhlrAGCLINNRWEAENADRFIR------SLNIKTPSR-EQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190
....*....|....*....|....*....|....*.
gi 1875943321 174 EVLLLDEPCSALDPISTGKIEELISELKADYTVVIV 209
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-71 |
4.92e-06 |
|
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: 47.32 E-value: 4.92e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLlrTFNKMYqlypeqrAEG 71
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL--AFDTIY-------AEG 47
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
10-211 |
7.72e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.71 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 10 SKIQVRDLNFYY------GKFHaLKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIltD 83
Cdd:COG4615 326 QTLELRGVTYRYpgedgdEGFT-LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYR--PES---GEILLDGQPV--T 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 84 NSDIALLRAKVGMVFqkpTPFpmsiYdniafgvrLFEKL---SRADMDERVQWALTKAALwnetKDKLH-QSGY----SL 155
Cdd:COG4615 398 ADNREAYRQLFSAVF---SDF----H--------LFDRLlglDGEADPARARELLERLEL----DHKVSvEDGRfsttDL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 156 SGGQQQRLciARGIAI---RPeVLLLDEPCSALDPISTgKI--EELISELKAD-YTVVIVTH 211
Cdd:COG4615 459 SQGQRKRL--ALLVALledRP-ILVFDEWAADQDPEFR-RVfyTELLPELKARgKTVIAISH 516
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-221 |
1.65e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLLrtfNKMyqLYP--EQRaeggilLDGQNILTDNSD-IALLRA--KVGMVFQ 99
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLI---NDT--LYPalARR------LHLKKEQPGNHDrIEGLEHidKVIVIDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 100 KP---TP--------------------------------------------FPMSIYDNIAFgvrlFEKLSRadMDERVQ 132
Cdd:cd03271 78 SPigrTPrsnpatytgvfdeirelfcevckgkrynretlevrykgksiadvLDMTVEEALEF----FENIPK--IARKLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 133 wALTKAALwnetkD--KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALdpiSTGKIEELISEL----KAD 203
Cdd:cd03271 152 -TLCDVGL-----GyiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL---HFHDVKKLLEVLqrlvDKG 222
|
250
....*....|....*...
gi 1875943321 204 YTVVIVTHNMqQAARCSD 221
Cdd:cd03271 223 NTVVVIEHNL-DVIKCAD 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-221 |
1.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.56 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFNKMYQlyPEQraeGGILLDGQNIltdNSDIALLR 91
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLN--PEK---GEILFERQSI---KKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 92 AKVGMVFQKPTPFP-MSIYDNIAFGVRLFEklSRADMDERVqwaltkaalwneTKDKL-HQSGYS---LSGGQQQRLCIA 166
Cdd:PRK13540 74 KQLCFVGHRSGINPyLTLRENCLYDIHFSP--GAVGITELC------------RLFSLeHLIDYPcglLSSGQKRQVALL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSD 221
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-236 |
1.85e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 13 QVRDLNFYYGK--FH-ALKNITLDIAKNKVTAFIGPSGCGKSTLLRTFnkmyqlypeqraeGGILLDGQNILTDNSDIAL 89
Cdd:PRK13545 23 KLKDLFFRSKDgeYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-------------AGVTMPNKGTVDIKGSAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 90 LRAKVGMVFQkptpfpMSIYDNIAFgvrlfEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGI 169
Cdd:PRK13545 90 IAISSGLNGQ------LTGIENIEL-----KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 170 AIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQQAARCSDSTAFMYLGELIEFSD 236
Cdd:PRK13545 159 HINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-211 |
2.26e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDI-AKNKVtAFIGPSGCGKSTLLRTFnkMYQLYPEQraeggilldGQNILTDNsdiall 90
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLeAGERL-AIIGENGVGKTTLLRTL--VGELEPDS---------GTVKWSEN------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 rAKVGMvfqkptpFPMSIYDNIAFGVRLFEKLSR----ADMDERVQWALTKAALwneTKDKLHQSGYSLSGGQQQRLCIA 166
Cdd:PRK15064 382 -ANIGY-------YAQDHAYDFENDLTLFDWMSQwrqeGDDEQAVRGTLGRLLF---SQDDIKKSVKVLSGGEKGRMLFG 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1875943321 167 RGIAIRPEVLLLDEPCSALDPIStgkIEELISELKaDY--TVVIVTH 211
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMES---IESLNMALE-KYegTLIFVSH 493
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-211 |
2.51e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNFYYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRtFNKMYQ----------LYPEQRAEGGILLDGQNIL 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR-YMAMHAidgipkncqiLHVEQEVVGDDTTALQCVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 82 tdNSDIA---LLRAKVGMVFQKPT-PFPMSI----------YDNIAFGVRL---FEKLSRADMDERVQWALTKAALWNET 144
Cdd:PLN03073 257 --NTDIErtqLLEEEAQLVAQQRElEFETETgkgkgankdgVDKDAVSQRLeeiYKRLELIDAYTAEARAASILAGLSFT 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 145 KDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELIseLKADYTVVIVTH 211
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
24-211 |
3.36e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.19 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 24 FHALKNITLDIAKnkVTAFIGPSGCGKST------LLRTFNKMY----QLYPEQRAEGGILLDGQNILTDNSDIALLRAK 93
Cdd:COG4938 9 FGPFKEAELELKP--LTLLIGPNGSGKSTliqallLLLQSNFIYlpaeRSGPARLYPSLVRELSDLGSRGEYTADFLAEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 94 VGMVFQKPTPFpmSIYDNIAfgvRLFEKLSRADMD---ERVQWALTKAALWNETKDKLHQSGYslsgGQQQRLCI---AR 167
Cdd:COG4938 87 ENLEILDDKSK--ELLEQVE---EWLEKIFPGKVEvdaSSDLVRLVFRPSGNGKRIPLSNVGS----GVSELLPIllaLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1875943321 168 GIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTH 211
Cdd:COG4938 158 SAAKPGSLLIIEEPEAHLHPKAQSALAELLAELaNSGVQVIIETH 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
155-213 |
5.34e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1875943321 155 LSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNM 213
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-211 |
1.09e-04 |
|
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: 42.21 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 39 VTAFIGPSGCGKSTLLRTFNkmYQLYPEQRAEGGILLDGQNILTDNSDiallRAKVGMVFQKPTPFPM------SIYDNI 112
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK--YALTGELPPNSKGGAHDPKLIREGEV----RAQVKLAFENANGKKYtitrslAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 113 AFgVRlfeklsradmDERVQWALTkaalwnETKDklhqsgySLSGGQQQ------RLCIARGIAIRPEVLLLDEPCSALD 186
Cdd:cd03240 98 IF-CH----------QGESNWPLL------DMRG-------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180
....*....|....*....|....*...
gi 1875943321 187 PIS-TGKIEELISELK--ADYTVVIVTH 211
Cdd:cd03240 154 EENiEESLAEIIEERKsqKNFQLIVITH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-200 |
1.24e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 12 IQVRDLNF-YYGKFHALKNITLDIAKNKVTAFIGPSGCGKSTLLRtfnkmyqlypeqraeggiLLDGQniLTDNSDIALL 90
Cdd:PLN03073 509 ISFSDASFgYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGE--LQPSSGTVFR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 91 RAKVGM-VFQK-----------PTPFPMSIYDNIAfgvrlfEKLSRADMDErvqwaltkaalWNETKDKLHQSGYSLSGG 158
Cdd:PLN03073 569 SAKVRMaVFSQhhvdgldlssnPLLYMMRCFPGVP------EQKLRAHLGS-----------FGVTGNLALQPMYTLSGG 631
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1875943321 159 QQQRLCIARGIAIRPEVLLLDEPCSALDpisTGKIEELISEL 200
Cdd:PLN03073 632 QKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGL 670
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-213 |
1.26e-04 |
|
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: 41.20 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 36 KNKVTAFIGPSGCGKSTLLRTFNKMYQlypeQRAEGGILLDGQNILTDNSDIALLrakvgmvfqkptpfpmsiydniafg 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELG----PPGGGVIYIDGEDILEEVLDQLLL------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 116 vrlfeklsradmdervqwaltkaalwnetkDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEE 195
Cdd:smart00382 52 ------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180
....*....|....*....|....
gi 1875943321 196 ------LISELKADYTVVIVTHNM 213
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTND 125
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-213 |
1.66e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1875943321 153 YSLSGGQQQRLCIARGI---AIRPEVLLLDEPCSALdpiSTGKIEELISELKA----DYTVVIVTHNM 213
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQSlthqGHTVVIIEHNM 872
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-213 |
2.06e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 147 KLHQSGYSLSGGQQQRLCIARGIAIR---PEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNM 213
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVIEHNL 892
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-226 |
4.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 148 LHQSGYSLSGGQQQRLCIARGIAIRPE--VLLLDEPCSALDPISTGKIEELISELKADYTVVIVTHNMQQAARCSDSTAF 225
Cdd:PRK00635 1381 LGQEQDTLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIH 1460
|
.
gi 1875943321 226 M 226
Cdd:PRK00635 1461 L 1461
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-234 |
5.46e-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: 39.65 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 155 LSGGQQQR--LCIARGIA-IRPEVL-LLDEPCSALDPISTGKIEELISE-LKADYTVVIVTHNMQQAARcsdSTAFMYLG 229
Cdd:cd03227 78 LSGGEKELsaLALILALAsLKPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL---ADKLIHIK 154
|
....*
gi 1875943321 230 ELIEF 234
Cdd:cd03227 155 KVITG 159
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-186 |
5.80e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 27 LKNITLDIAKNKVTAFIGPSGCGKSTLLRTfnkmyqLYPEQRAEGGILLDGQNiltdnsdiallrAKVGMVFQKPTPFPM 106
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLAL------LKNEISADGGSYTFPGN------------WQLAWVNQETPALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 107 SIYDNIAFGVRLFEKLSRA------------------DMDERVQWALTK--AALWNE---TKDKLHQSGYSLSGGQQQRL 163
Cdd:PRK10636 79 PALEYVIDGDREYRQLEAQlhdanerndghaiatihgKLDAIDAWTIRSraASLLHGlgfSNEQLERPVSDFSGGWRMRL 158
|
170 180
....*....|....*....|...
gi 1875943321 164 CIARGIAIRPEVLLLDEPCSALD 186
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
154-227 |
6.61e-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: 40.04 E-value: 6.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNMQQAARCSDSTAFMY 227
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
36-54 |
7.68e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 7.68e-04
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
36-70 |
9.20e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.80 E-value: 9.20e-04
10 20 30
....*....|....*....|....*....|....*
gi 1875943321 36 KNKVTAFIGPSGCGKSTLLrtfNKmyqLYPEQRAE 70
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLL---NA---LAPDLELK 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-54 |
1.06e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTLL 54
Cdd:TIGR00630 622 NNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
154-229 |
1.10e-03 |
|
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: 40.38 E-value: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKI-EELISELKADYTVVIVTHNMQQAARCSDSTAFMYLG 229
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
24-57 |
1.16e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|....
gi 1875943321 24 FHALKNITLDIAKnkVTAFIGPSGCGKSTLLRTF 57
Cdd:COG4637 10 FKSLRDLELPLGP--LTVLIGANGSGKSNLLDAL 41
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
36-54 |
1.20e-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: 38.68 E-value: 1.20e-03
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
24-60 |
1.26e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 39.50 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1875943321 24 FHALKNITLDIaKNKVTAFIGPSGCGKSTLLRTFNKM 60
Cdd:pfam13175 11 FRCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-209 |
1.26e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYTVVIV 209
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV 459
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
154-213 |
1.69e-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: 39.38 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL-KADYTVVIVTHNM 213
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDL 272
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
25-53 |
2.24e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 2.24e-03
10 20
....*....|....*....|....*....
gi 1875943321 25 HALKNITLDIAKNKVTAFIGPSGCGKSTL 53
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-69 |
3.06e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 3.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1875943321 22 GKFHALkniTLDIAKNKVTAFIGPSGCGKSTLLRTFnkMYQLYPEQRA 69
Cdd:pfam13555 10 GTFDGH---TIPIDPRGNTLLTGPSGSGKSTLLDAI--QTLLVPAKRA 52
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-180 |
5.90e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.77 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 39 VTAFIGPSGCGKSTLLRTFNKMyqlypEQRAEGGILLDGQNIltdNSDIALLRAKVGmvFQKPTPFPMSIYDNIAFGVRL 118
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGI-----MQPSSGNIYYKNCNI---NNIAKPYCTYIG--HNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1875943321 119 FeklsraDMDERVQWALTKAALwnetKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDE 180
Cdd:PRK13541 98 Y------NSAETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
73-212 |
6.24e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 73 ILLDGQNILTDNSDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVqwaltKAALWNETKDKLHQSG 152
Cdd:pfam13304 160 GLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRE-----RGLILLENGGGGELPA 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 153 YSLSGGQQQRLCIA---RGIAIRPEVLLLDEPCSALDPISTGKIEELISELKADYT-VVIVTHN 212
Cdd:pfam13304 235 FELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-214 |
7.83e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 7.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1875943321 154 SLSGGQQQRLCIAR--GIAIRPEVLLLDEPCSALDPISTGKIEELISELKAD-YTVVIVTHNMQ 214
Cdd:PRK00635 476 TLSGGEQERTALAKhlGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQ 539
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-221 |
9.70e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 36.01 E-value: 9.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1875943321 154 SLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGKIEELISEL--KADYTVVIVTHNMQQAARCSD 221
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYLSD 140
|
|
| |
