|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-254 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 572.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPK 80
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VDTTLLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLC 160
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
250
....*....|....
gi 1391526133 241 QDKRTEDYITGRFG 254
Cdd:COG1117 245 KDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
8-253 |
3.39e-175 |
|
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: 481.79 E-value: 3.39e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAV 167
Cdd:TIGR00972 82 RRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTED 247
Cdd:TIGR00972 162 EPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTED 241
|
....*.
gi 1391526133 248 YITGRF 253
Cdd:TIGR00972 242 YISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-235 |
1.08e-150 |
|
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: 418.89 E-value: 1.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKksALGLSGGQQQRLCIARALAV 167
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQ 235
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-254 |
2.32e-143 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 401.46 E-value: 2.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAV 167
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTED 247
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 1391526133 248 YITGRFG 254
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-254 |
1.11e-138 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 390.30 E-value: 1.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPK 80
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VDTTLLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRsrVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLC 160
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYK--GDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLV---------GEMVEYN 231
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFD 241
|
250 260
....*....|....*....|...
gi 1391526133 232 DTEQMFSMPQDKRTEDYITGRFG 254
Cdd:PRK14243 242 RTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-254 |
3.80e-111 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 320.45 E-value: 3.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPK 80
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VDTTLLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLC 160
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGS--LKEKYTVAIVTHNMQQATRISDYTAFF-----LVGEMVEYNDT 233
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLT 240
|
250 260
....*....|....*....|.
gi 1391526133 234 EQMFSMPQDKRTEDYITGRFG 254
Cdd:PRK14258 241 KKIFNSPHDSRTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-254 |
5.20e-103 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 299.45 E-value: 5.20e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-IRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARAL 165
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRT 245
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 1391526133 246 EDYITGRFG 254
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-252 |
5.98e-93 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 273.71 E-value: 5.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYspKVDTTLLR 87
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGI-RSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARAL 165
Cdd:PRK14247 82 RRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRT 245
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*..
gi 1391526133 246 EDYITGR 252
Cdd:PRK14247 242 EKYVTGR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-254 |
2.25e-80 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 242.69 E-value: 2.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKvDTTLLRKKVG 91
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 92 MVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEV 171
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTEDYITG 251
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
...
gi 1391526133 252 RFG 254
Cdd:PRK14271 265 LSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-249 |
1.35e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 239.51 E-value: 1.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE--PD---SGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvklDEIVEKSLrdaAIFDEV--KDRLKKSALGLSGGQQQRLCIARA 164
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSK---AEAEERAM---ELLERVglADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDK 243
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
....*.
gi 1391526133 244 RTEDYI 249
Cdd:COG1126 231 RTRAFL 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-252 |
2.22e-78 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 237.25 E-value: 2.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPN-VKIEGKVLLDGEDIYspKVDTTLLR 87
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:PRK14246 90 KEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTE 246
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
....*.
gi 1391526133 247 DYITGR 252
Cdd:PRK14246 250 KYVIGR 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-226 |
5.46e-65 |
|
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: 200.11 E-value: 5.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpNVKIEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-----EEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYgprihgirsrvkldeivekslrdaaifdevkdrlkksalGLSGGQQQRLCIARALA 166
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIAL---------------------------------------GLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQATRISDYTAFFLVGE 226
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-222 |
1.76e-64 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 200.06 E-value: 1.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--PD---SGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFF 222
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-242 |
8.11e-63 |
|
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: 204.75 E-value: 8.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYS-PKV 81
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PT---SGSILFDGKDLTKlSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQP----NPFpMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRlkkSALGLSGGQQQ 157
Cdd:COG1123 336 SLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR---YPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQ 235
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....*..
gi 1391526133 236 MFSMPQD 242
Cdd:COG1123 492 VFANPQH 498
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-238 |
3.27e-62 |
|
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: 194.86 E-value: 3.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYspKVDTTLL 86
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDIT--KKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQqpNP----FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIA 162
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGL----EHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-237 |
1.22e-61 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 193.49 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIY--SPKvDTTL 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRPD---SGEVLIDGEDISglSEA-ELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPF-PMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLrDAAIFDEVKDRLKKSalgLSGGQQQRLCIARA 164
Cdd:cd03261 75 LRRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKL-EAVGLRGAEDLYPAE---LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-249 |
1.14e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 188.38 E-value: 1.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnvkIE---GKVLLDGEDIYSpkVDT 83
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL--------IEptsGRILIDGEDIRD--LDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVklDEIVEK-SLrDAAIFdevKDRLKKSalgLSGGQQ 156
Cdd:COG1125 72 VELRRRIGYVIQQIGLFPhMTVAENIATVPRLLGwdkerIRARV--DELLELvGL-DPEEY---RDRYPHE---LSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTE 234
Cdd:COG1125 143 QRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPE 222
|
250
....*....|....*
gi 1391526133 235 QMFSMPQDKRTEDYI 249
Cdd:COG1125 223 EILANPANDFVADFV 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-237 |
2.58e-58 |
|
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: 185.18 E-value: 2.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDT-TLL 86
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPD---SGEILVDGQDITGLSEKElYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPF-PMSVYDNIAYGPRIHGIRSRVKLDEIV-EK----SLRDAAifdevkdrlKKSALGLSGGQQQRLC 160
Cdd:COG1127 81 RRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVlEKlelvGLPGAA---------DKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-215 |
4.71e-58 |
|
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: 183.85 E-value: 4.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIY--SPKV 81
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVRVDGTDISklSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvkldeivEKSLRDAAIFDEV--KDRLKKSALGLSGGQQQR 158
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPLLLAGVPKK-------ERRERAEELLERVglGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQ---QATRI 215
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPElaeYADRI 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-221 |
1.97e-57 |
|
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: 181.95 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspkVDTTLLR 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL--ERPD---SGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGirsrVKLDEIVEKSLRDAAIFDeVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRG----VPKAEIRARVRELLELVG-LEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 167 VEPEVLLMDEPTSALDPISTskiEELMGSLKE-----KYTVAIVTHNMQQATRISDYTAF 221
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLR---EELREELKElqrelGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-231 |
1.15e-56 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 180.78 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY----GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYS-PKVD 82
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKlSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQP----NPFpMSVYDNIAYGPRIHGIRSrvKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQR 158
Cdd:cd03257 77 RKIRRKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLS--KKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYN 231
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-242 |
1.84e-56 |
|
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: 180.77 E-value: 1.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGT----NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPNVkiEGKVLLDGEDIysPKVDT 83
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAG---LERPW--SGEVTFDGRPV--TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQP----NPFpMSVYDNIAYGPRIHGIRSRvklDEIVEKSLRDAAIFDEVKDRLKKSalgLSGGQQQRL 159
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYPHQ---LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
....*
gi 1391526133 238 SMPQD 242
Cdd:COG1124 228 AGPKH 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-217 |
3.96e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.47 E-value: 3.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDI--YSPkvdtTL 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPLsaMPP----PE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIR-SRVKLDEIVEKSLRDAAIfdevkdrLKKSALGLSGGQQQRLCIARA 164
Cdd:COG4619 72 WRRQVAYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDI-------LDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISD 217
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVlwVSHDPEQIERVAD 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-218 |
1.43e-55 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 178.70 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDI--YSPKVdttl 85
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKP---SSGEVLLDGRDLasLSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPN-PFPMSVYDNIAYG--PRIHGIRSRVKLD-EIVEKSLRDAAIfDEVKDRlkkSALGLSGGQQQRLCI 161
Cdd:COG1120 73 LARRIAYVPQEPPaPFGLTVRELVALGryPHLGLFGRPSAEDrEAVEEALERTGL-EHLADR---PVDELSGGERQRVLI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISDY 218
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADR 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.45e-55 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 178.74 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHY----GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVkiEGKVLLDGEDI 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKPT--SGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 77 YSPkvdttllRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLrdaaifDEV--KDRLKKSALGLSG 153
Cdd:COG1116 76 TGP-------GPDRGVVFQEPALLPwLTVLDNVALGLELRGV-PKAERRERARELL------ELVglAGFEDAYPHQLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISD 217
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLAD 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-241 |
1.28e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 178.32 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVKIEGKVLLDGEDI--YSPKV 81
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLlkLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQP----NPFpMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIfDEVKDRLKKSALGLSGGQQQ 157
Cdd:COG0444 80 LRKIRGREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--THNMQQATRISDYTAFFLVGEMVEYNDTEQ 235
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILfiTHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*.
gi 1391526133 236 MFSMPQ 241
Cdd:COG0444 238 LFENPR 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-222 |
4.12e-54 |
|
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: 173.42 E-value: 4.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDIYSPKVDTtlLR 87
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGP---TSGEVLVDGKDLTKLSLKE--LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARAL 165
Cdd:cd03225 75 RKVGLVFQNPDDqfFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGL----EGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFF 222
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-249 |
4.20e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 177.58 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDIyspkvdT 83
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE--RPT---SGSVLVDGVDL------T 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TL-------LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVK-LDEIVEksLRDaaifdevkdrlKKSAL 149
Cdd:COG1135 71 ALserelraARRKIGMIFQHFNLLSsRTVAENVALPLEIAGvpkaeIRKRVAeLLELVG--LSD-----------KADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 150 --GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAfflV- 224
Cdd:COG1135 138 psQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVA---Vl 214
|
250 260
....*....|....*....|....*..
gi 1391526133 225 --GEMVEYNDTEQMFSMPQDKRTEDYI 249
Cdd:COG1135 215 enGRIVEQGPVLDVFANPQSELTRRFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-217 |
6.41e-54 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 173.43 E-value: 6.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLK---TLNRmndlvPNvkiEGKVLLDGEDIYSPk 80
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiaGLER-----PT---SGEVLVDGEPVTGP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 vdttllRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvKLDEIVEkslrdaAIFDEV--KDRLKKSALGLSGGQQQ 157
Cdd:cd03293 72 ------GPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKA-EARERAE------ELLELVglSGFENAYPHQLSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISD 217
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLAD 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-215 |
9.44e-54 |
|
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: 171.03 E-value: 9.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIysPKVDTTL 85
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PT---SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIaygprihgirsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARAL 165
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHN---MQQATRI 215
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRlstIRDADRI 164
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-249 |
3.50e-53 |
|
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: 172.10 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSpkVDTTLL 86
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--IEPT---SGEIFIDGEDIRE--QDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVK-LDEIVekSLRDAaifdEVKDRLKKSalgLSGGQQQRL 159
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIALVPKLLKwpkekIRERADeLLALV--GLDPA----EFADRYPHE---LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|..
gi 1391526133 238 SMPQDKRTEDYI 249
Cdd:cd03295 225 RSPANDFVAEFV 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-241 |
3.56e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 179.33 E-value: 3.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNVKIEGKVLLDGEDIYspKVDTTL 85
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLL--ELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQP--NPFPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIAR 163
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-214 |
2.47e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.45 E-value: 2.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIY--SPKV 81
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGL--DRPT---SGEVLIDGQDISslSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEkslrdaaIFDEV--KDRLKKSALGLSGGQQQR 158
Cdd:COG1136 80 LARLRRRHIGFVFQFFNLLPeLTALENVALPLLLAGVSRKERRERARE-------LLERVglGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATR 214
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-217 |
2.54e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.36 E-value: 2.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnRMndlvpnvkI-------EGKVLLDGEDIyspk 80
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RM--------IagfetpdSGRILLDGRDV---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 vdTTLL--RKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLrdaaifdevkDRLKKSALG------L 151
Cdd:COG3842 70 --TGLPpeKRNVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELL----------ELVGLEGLAdryphqL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPistsKI-----EELMGSLKE-KYTVAIVTHNMQQATRISD 217
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDA----KLreemrEELRRLQRElGITFIYVTHDQEEALALAD 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-236 |
3.73e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.47 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSpkvDTTLLR 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML--LGLLRPT---SGEVRVLGEDVAR---DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRLCIARALA 166
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-217 |
9.36e-52 |
|
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: 169.55 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYS-PKV 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITAkKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDRlkkSALGLSGGQQQRL 159
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGL-SEEEAEERVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYAD 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-249 |
3.04e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYSPKVDTTLLR 87
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRihgirsRVKldeivekSLRDAAIFDEVKDRLKKSALG---------LSGGQQQ 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPhLTALENVMFGPL------RVR-------GASKEEAEKQARELLAKVGLAerahhypseLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
250
....*....|...
gi 1391526133 237 FSMPQDKRTEDYI 249
Cdd:PRK09493 224 IKNPPSQRLQEFL 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-217 |
1.45e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 166.09 E-value: 1.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKT---LNRmndlvPNvkiEGKVLLDGEDIYSpkvDT 83
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET-----PD---SGRIVLNGRDLFT---NL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGiRSRVKLDEIVEKSLrdaaifdevkDRLKKSALG------LSGGQQ 156
Cdd:COG1118 71 PPRERRVGFVFQHYALFPhMTVAENIAFGLRVRP-PSKAEIRARVEELL----------ELVQLEGLAdrypsqLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELAD 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-241 |
1.61e-49 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 162.37 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYS-PKVD 82
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PT---SGSVLVDGTDLTLlSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNPF-PMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRdaaiFDEVKDRLKKSALGLSGGQQQRLCI 161
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLE----LVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSM 239
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 1391526133 240 PQ 241
Cdd:cd03258 232 PQ 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-215 |
2.25e-49 |
|
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: 172.33 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIysPKVDTTL 85
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL--YEPT---SGRILIDGIDL--RQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEIVEkSLRDAAIFDEVKD-------RLKKSALGLSGGQQQR 158
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLG------DPDATDEEIIE-AARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQR 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHN---MQQATRI 215
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRlstIRLADRI 679
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-249 |
3.08e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 162.10 E-value: 3.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDI-YSPKVDTT- 84
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLE--TPD---SGQLNIAGHQFdFSQKPSEKa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 --LLRKKVGMVFQQPNPFP-MSVYDNIAYGP-RIHGI---RSRVKLDEIVEKsLRdaaiFDEVKDRLkksALGLSGGQQQ 157
Cdd:COG4161 77 irLLRQKVGMVFQQYNLWPhLTVMENLIEAPcKVLGLskeQAREKAMKLLAR-LR----LTDKADRF---PLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEqM 236
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-H 227
|
250
....*....|...
gi 1391526133 237 FSMPQDKRTEDYI 249
Cdd:COG4161 228 FTQPQTEAFAHYL 240
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-179 |
4.28e-49 |
|
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: 158.58 E-value: 4.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDIYSPkvDTTLLRKKVGMVFQQPNPFP- 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSP---TEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 102 MSVYDNIAYGPRIHGIRSRVKLDEiVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-238 |
5.15e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.41 E-value: 5.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTlnrMNDLVPNVKieGKVLLDGEDIyspkvdtTLLR 87
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLPPTS--GTVRLFGKPP-------RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPN---PFPMSVYDNIAYG--PRIHGIRSRVKLD-EIVEKSLRDAAIFDevkdrLKKSALG-LSGGQQQRLC 160
Cdd:COG1121 75 RRIGYVPQRAEvdwDFPITVRDVVLMGryGRRGLFRRPSRADrEAVDEALERVGLED-----LADRPIGeLSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAfFLVGEMVEYNDTEQMFS 238
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEVLT 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-221 |
1.15e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 158.33 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSPKVDttlLR 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDIKKEPEE---VK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYgprihgirsrvkldeivekslrdaaifdevkdrlkksalglSGGQQQRLCIARALA 166
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENLKL-----------------------------------------SGGMKQRLALAQALL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY-TVAIVTHNMQQATRISDYTAF 221
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAI 167
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-217 |
1.27e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.91 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDI--YSPKvDTT 84
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE--PT---SGEILVDGQDVtaLRGR-ALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LLRKKVGMVFQQPNPFP-MSVYDNIAYG--PRIHGIRSRVKLdeiVEKSLRDAAI--FDEV--KDRLKKSALGLSGGQQQ 157
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPrLSVLTNVLAGrlGRTSTWRSLLGL---FPPEDRERALeaLERVglADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTskiEELMGSLKE-----KYTVAIVTHNMQQATRISD 217
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTA---RQVMDLLRRiaredGITVVVNLHQVDLARRYAD 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-250 |
8.74e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 155.94 E-value: 8.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVP---NVKIEGKVLlDGEDIYSPKvDT 83
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLE--MPrsgTLNIAGNHF-DFSKTPSDK-AI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFP-MSVYDNIAYGP-RIHGI---RSRVKLDEIVEKsLRdaaiFDEVKDRLkksALGLSGGQQQR 158
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNLIEAPcRVLGLskdQALARAEKLLER-LR----LKPYADRF---PLHLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE-KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQmF 237
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-F 228
|
250
....*....|...
gi 1391526133 238 SMPQDKRTEDYIT 250
Cdd:PRK11124 229 TQPQTEAFKNYLS 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-229 |
1.97e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYspKVDTTL 85
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD--PT---SGRILIDGVDIR--DLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEIVEkSLRDAAIFDEVkDRLKK---SALG-----LSGGQQQ 157
Cdd:COG1132 412 LRRQIGVVPQDTFLFSGTIRENIRYG------RPDATDEEVEE-AAKAAQAHEFI-EALPDgydTVVGergvnLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRIsdytaffLV---GEMVE 229
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLstiRNADRI-------LVlddGRIVE 554
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-249 |
2.30e-46 |
|
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: 154.42 E-value: 2.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGtNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPnvkIEGKVLLDGEDIyspkvdTTL-- 85
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKP---DSGKILLNGKDI------TNLpp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYGPRiHGIRSRVKLDEIVEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRLCIARA 164
Cdd:cd03299 69 EKRDISYVPQNYALFPhMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHLLNRKPET---LSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQD 242
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
....*..
gi 1391526133 243 KRTEDYI 249
Cdd:cd03299 224 EFVAEFL 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-228 |
2.59e-46 |
|
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: 153.74 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNdLVPnvKIEGKVLLDGEDIYSPKVDTtLLRKK 89
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MG-LLP--PRSGSIRFDGRDITGLPPHE-RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNPFP-MSVYDNI---AYGPRIHGIRSRvkLDEIVEkslrdaaIFDEVKDRLKKSALGLSGGQQQRLCIARAL 165
Cdd:cd03224 77 IGYVPEGRRIFPeLTVEENLllgAYARRRAKRKAR--LERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-217 |
5.08e-46 |
|
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: 153.88 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYS-PKVDTTL 85
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDINKlKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNI-----AYGPRIHGIRSRVKLDEIveksLRDAAIFDEV--KDRLKKSALGLSGGQQQ 157
Cdd:cd03256 76 LRRQIGMIFQQFNLIErLSVLENVlsgrlGRRSTWRSLFGLFPKEEK----QRALAALERVglLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTskiEELMGSLKEK-----YTVAIVTHNMQQATRISD 217
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRInreegITVIVSLHQVDLAREYAD 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-215 |
7.14e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.39 E-value: 7.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnRMndlvpnvkI-------EGKVLLDGEDIysp 79
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RM--------IagledptSGEILIGGRDV--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 kvdTTLLRKK--VGMVFQQPNPFP-MSVYDNIAYGPRIHGirsrVKLDEIVEKSLRDAAIFDeVKDRLKKSALGLSGGQQ 156
Cdd:COG3839 68 ---TDLPPKDrnIAMVFQSYALYPhMTVYENIAFPLKLRK----VPKAEIDRRVREAAELLG-LEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPistsKI-EELMGSLKE-----KYTVAIVTHN----MQQATRI 215
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDA----KLrVEMRAEIKRlhrrlGTTTIYVTHDqveaMTLADRI 204
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-251 |
2.63e-45 |
|
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: 155.40 E-value: 2.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnvkIE---GKVLLDGEDI--YSPKVDTTLLRKKVGM 92
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL--------IEptaGQIFIDGENImkQSPVELREVRRKKIGM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 93 VFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEkSLRDAAIfDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEV 171
Cdd:TIGR01186 76 VFQQFALFPhMTILQNTSLGPELLGWPEQERKEKALE-LLKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTEDYI 249
Cdd:TIGR01186 151 LLMDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
..
gi 1391526133 250 TG 251
Cdd:TIGR01186 231 GK 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-226 |
2.64e-45 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 149.32 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIysPKVDTTLLRK 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQqpnpfpmsvydniaygprihgirsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARALAVE 168
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 169 PEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGE 226
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-210 |
5.51e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 150.59 E-value: 5.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmnDLVPNvkiEGKVLLDGEDIYS-PKVDTTL 85
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPT---SGQVLVNGQDLSRlKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQ----PNpfpMSVYDNIAYGPRIHG-----IRSRVkldeivekslrdAAIFDEV--KDRLKKSALGLSGG 154
Cdd:COG2884 77 LRRRIGVVFQDfrllPD---RTVYENVALPLRVTGksrkeIRRRV------------REVLDLVglSDKAKALPHELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQ 210
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLE 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-213 |
9.23e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 148.73 E-value: 9.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKvDTTL 85
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEE-NLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQP-NPF-PMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAaifdEVKDRLKKSALGLSGGQQQRLCIAR 163
Cdd:TIGR04520 75 IRKKVGMVFQNPdNQFvGATVEDDVAFGLENLGV-PREEMRKRVDEALKLV----GMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQAT 213
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAV 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-251 |
1.64e-43 |
|
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: 148.18 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnvkIE---GKVLLDGEDI--YSPKVDTTLLRKKVGMVFQQ 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL--------IEptsGKVLIDGQDIaaMSRKELRELRRKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNPFP-MSVYDNIAYGPRIHGIRSRVKLdEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:cd03294 111 FALLPhRTVLENVAFGLEVQGVPRAERE-ERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 176 EPTSALDP-ISTSKIEELMG-SLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTEDYITG 251
Cdd:cd03294 186 EAFSALDPlIRREMQDELLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-218 |
2.99e-43 |
|
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: 146.43 E-value: 2.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspkvdTTLL--- 86
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPT---SGSVLFDGEDI------TGLPphe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 --RKKVGMVFQQPNPFP-MSVYDNI------AYGPRIHGIRSRVKLDEIVEKSLRdaaIFDEVK--DRLKKSALGLSGGQ 155
Cdd:cd03219 72 iaRLGIGRTFQIPRLFPeLTVLENVmvaaqaRTGSGLLLARARREEREARERAEE---LLERVGlaDLADRPAGELSYGQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDY 218
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADR 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-249 |
3.26e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 146.82 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSP-KVDTTL 85
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIhgirsrvkldeiVEKSLRDAAIfDEVKDRLKKSALG---------LSGGQ 155
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPhRTVLENIIEGPVI------------VKGEPKEEAT-ARARELLAKVGLAgketsyprrLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPistskieELMGSL--------KEKYTVAIVTHNMQQATRISDYTAFFLVGEM 227
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDP-------ELVGEVlntirqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
250 260
....*....|....*....|..
gi 1391526133 228 VEYNDTEQMFSMPQDKRTEDYI 249
Cdd:PRK11264 223 VEQGPAKALFADPQQPRTRQFL 244
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-215 |
4.47e-43 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 146.15 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGT---NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLvpnvkIEGKVLLDGEDIYSpkVDTT 84
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDIRD--LNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LLRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEiVEKSLRDAAIFDEVKD-------RLKKSALGLSGGQQQ 157
Cdd:cd03249 74 WLRSQIGLVSQEPVLFDGTIAENIRYG------KPDATDEE-VEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQKQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRI 215
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLstiRNADLI 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-217 |
7.44e-43 |
|
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: 145.52 E-value: 7.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYSPK-VDTTL 85
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDITKLRgKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNI-----AYGPRIHGIRSRVKLDEIVE--KSLRDAAIFDEVKDRLKKsalgLSGGQQQ 157
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVlhgrlGYKPTWRSLLGRFSEEDKERalSALERVGLADKAYQRADQ----LSGGQQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYAD 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-249 |
2.71e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.87 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYS-PKVD 82
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLER--PT---SGRVLVDGQDLTAlSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNPfpMS---VYDNIAYGPRIHG-----IRSRV-KLDEIVEKSlrdaaifdevkDRLKKSALGLSG 153
Cdd:PRK11153 77 LRKARRQIGMIFQHFNL--LSsrtVFDNVALPLELAGtpkaeIKARVtELLELVGLS-----------DKADRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--THNMQQATRISDYTAFFLVGEMVEYN 231
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVliTHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250
....*....|....*...
gi 1391526133 232 DTEQMFSMPQDKRTEDYI 249
Cdd:PRK11153 224 TVSEVFSHPKHPLTREFI 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-217 |
2.80e-42 |
|
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: 144.02 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIyspkVDTTLL 86
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER--PD---SGTILFGGEDA----TDVPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEK--SLRDAAIFDEVKDRLKKSalgLSGGQQQRLCIAR 163
Cdd:cd03296 73 ERNVGFVFQHYALFRhMTVFDNVAFGLRVKPRSERPPEAEIRAKvhELLKLVQLDWLADRYPAQ---LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 164 ALAVEPEVLLMDEPTSALDpistSKI-EELMGSLKEKY-----TVAIVTHNMQQATRISD 217
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALD----AKVrKELRRWLRRLHdelhvTTVFVTHDQEEALEVAD 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-220 |
3.37e-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: 143.06 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPnvKIEGKVLLDGEDIyspkvdtTLLRK 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLK--PTSGSIRVFGKPL-------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQQPN---PFPMSVYDNIA---YGPRIHGIRSRVKLDEIVEKSLRDAAIFDevkdrLKKSALG-LSGGQQQRLCI 161
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLmglYGHKGLFRRLSKADKAKVDEALERVGLSE-----LADRQIGeLSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTA 220
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-253 |
1.41e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 142.63 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 2 EKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDIYSPK- 80
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLE--TPD---SGEIRVGGEEIRLKPd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 -------VDT---TLLRKKVGMVFQQPNPFP-MSVYDNIAYGPrIHgirsrvkldeiVEKSLRDAAIfDEVKDRLKKSAL 149
Cdd:COG4598 78 rdgelvpADRrqlQRIRTRLGMVFQSFNLWShMTVLENVIEAP-VH-----------VLGRPKAEAI-ERAEALLAKVGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 150 G---------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistskieEL-------MGSL-KEKYTVAIVTHNMQQA 212
Cdd:COG4598 145 AdkrdaypahLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELvgevlkvMRDLaEEGRTMLVVTHEMGFA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1391526133 213 TRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTEDYITGRF 253
Cdd:COG4598 218 RDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-249 |
1.49e-41 |
|
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: 141.99 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIyspkVDTTLLR 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PT---SGEILLDGKDI----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRdaaiFDEVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:cd03300 72 RPVNTVFQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALD----LVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 167 VEPEVLLMDEPTSALD-PISTSKIEELMGSLKE-KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKR 244
Cdd:cd03300 147 NEPKVLLLDEPLGALDlKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
....*
gi 1391526133 245 TEDYI 249
Cdd:cd03300 227 VADFI 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-228 |
1.56e-41 |
|
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: 140.26 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLvpnvkIEGKVLLDGEDI--YSPKVdttlLR 87
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-----SSGEILLDGKDLasLSPKE----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQqpnpfpmsvydniaygprihgIRSRVKLDEIVEKSLRDaaifdevkdrlkksalgLSGGQQQRLCIARALAV 167
Cdd:cd03214 73 RKIAYVPQ---------------------ALELLGLAHLADRPFNE-----------------LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-215 |
8.35e-41 |
|
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: 147.21 E-value: 8.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpkVD 82
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP--PY---SGSILINGVDLSD--LD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNPFPMSVYDNIA-YGPRIhgirSrvklDEIVEKSLRDAAIFDEVKD-------RLKKSALGLSGG 154
Cdd:COG4988 406 PASWRRQIAWVPQNPYLFAGTIRENLRlGRPDA----S----DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGG 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH---NMQQATRI 215
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI 541
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-217 |
9.66e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.34 E-value: 9.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHY--GT---NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKV 81
Cdd:PRK13637 2 SIKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPT---SGKIIIDGVDITDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQP--NPFPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAI-FDEVKDrlkKSALGLSGGQQQR 158
Cdd:PRK13637 77 KLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGL-SEEEIENRVKRAMNIVGLdYEDYKD---KSPFELSGGQKRR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLAD 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-218 |
1.68e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 139.35 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNdLVPnvKIEGKVLLDGEDIYSPKVDTtLLRKK 89
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SG-LLP--PRSGSIRFDGEDITGLPPHR-IARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVK--LDEIVEkslrdaaIFDEVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:COG0410 80 IGYVPEGRRIFPsLTVEENLLLGAYARRDRAEVRadLERVYE-------LFPRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHNMQQATRISDY 218
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADR 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-251 |
2.10e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 139.72 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIY---------- 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSIVVNGQTINlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 78 -SPKVDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGP-RIHGIrSRVKLDEIVEKSLRDAAIFDEVKDrlkKSALGLSGG 154
Cdd:PRK10619 81 vADKNQLRLLRTRLTMVFQHFNLWShMTVLENVMEAPiQVLGL-SKQEARERAVKYLAKVGIDERAQG---KYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDT 233
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*...
gi 1391526133 234 EQMFSMPQDKRTEDYITG 251
Cdd:PRK10619 237 EQLFGNPQSPRLQQFLKG 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-215 |
2.86e-40 |
|
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: 138.16 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDI--YSPKvdttl 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIGGRDVtdLPPK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 lRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGirsrVKLDEIVEKSLRDAAIF--DEVKDRLKKSalgLSGGQQQRLCIA 162
Cdd:cd03301 71 -DRDIAMVFQNYALYPhMTVYDNIAFGLKLRK----VPKDEIDERVREVAELLqiEHLLDRKPKQ---LSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 163 RALAVEPEVLLMDEPTSALDpistSKI-EELMGSLKE-----KYTVAIVTHN----MQQATRI 215
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLD----AKLrVQMRAELKRlqqrlGTTTIYVTHDqveaMTMADRI 201
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-241 |
4.76e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 4.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHY-----------GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKV 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE--PT---SGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 70 LLDGEDIYS-PKVDTTLLRKKVGMVFQQP----NPfPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLrdaaifDEVkdRL 144
Cdd:COG4608 76 LFDGQDITGlSGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELL------ELV--GL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 145 KKSALG-----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-SKIEELMGSLKEKYTVAIV--THNMQQATRIS 216
Cdd:COG4608 147 RPEHADrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIqAQVLNLLEDLQDELGLTYLfiSHDLSVVRHIS 225
|
250 260
....*....|....*....|....*
gi 1391526133 217 DYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-228 |
1.36e-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: 136.48 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYG--TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVkieGKVLLDGEDIYSPKVDttl 85
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRPTS---GTAYINGYSIRTDRKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDeVKDRLKKSalgLSGGQQQRLCIARA 164
Cdd:cd03263 73 ARQSLGYCPQFDALFDeLTVREHLRFYARLKGL-PKSEIKEEVELLLRVLGLTD-KANKRART---LSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-217 |
5.92e-39 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 134.73 E-value: 5.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDI---FKNKITAFIGPSGCGKSTFLKTLNRMNDL-VPNVKIEGKVLLDGEDiyspKVDTTLLRKKVGMVFQQPN 98
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGTVLFDSRK----KINLPPQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 99 PFP-MSVYDNIAYGPRIHGIRS-RVKLDEIVekslrDAAIFDEVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDE 176
Cdd:cd03297 86 LFPhLNVRENLAFGLKRKRNREdRISVDELL-----DLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391526133 177 PTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLAD 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-218 |
2.25e-38 |
|
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: 134.40 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspkvdTTL---L 86
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPT---SGRILFDGRDI------TGLpphR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMV--FQQPNPFP-MSVYDNIAYGPRIHGIRS------RVKLDEIVEKSLRDAA--IFDEVK--DRLKKSALGLSG 153
Cdd:COG0411 76 IARLGIArtFQNPRLFPeLTVLENVLVAAHARLGRGllaallRLPRARREEREARERAeeLLERVGlaDRADEPAGNLSY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE--KYTVAIVTHNMQQATRISDY 218
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADR 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
3.83e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHVENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVd 82
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQ---SGEIKIDGITISKENL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 tTLLRKKVGMVFQQP-NPF-PMSVYDNIAYGPRIHGIrSRVKLDEIVEkslrDAAIFDEVKDRLKKSALGLSGGQQQRLC 160
Cdd:PRK13632 79 -KEIRKKIGIIFQNPdNQFiGATVEDDIAFGLENKKV-PPKKMKDIID----DLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQATrISDYTAFFLVGEMV 228
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-228 |
5.45e-38 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 133.60 E-value: 5.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDI--YSPKVdtt 84
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQ---SGTVFLGDKPIsmLSSRQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 lLRKKVGMVFQQ-PNPFPMSVYDNIAYG--PRI-HGIRSRVKLDEIVEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRLC 160
Cdd:PRK11231 74 -LARRLALLPQHhLTPEGITVRELVAYGrsPWLsLWGRLSAEDNARVNQAMEQTRI-NHLADRRLTD---LSGGQRQRAF 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-249 |
6.21e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.57 E-value: 6.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGtnHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnrmnDLV-----PnvkIEGKVLLDGEDIyspkvd 82
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLL-------NLIagflpP---DSGRILWNGQDL------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLL--RKKVGMVFQQPNPFP-MSVYDNIAYGprihgIRSRVKLDEIVEKSLRDAAI---FDEVKDRLKKSalgLSGGQQ 156
Cdd:COG3840 64 TALPpaERPVSMLFQENNLFPhLTVAQNIGLG-----LRPGLKLTAEQRAQVEQALErvgLAGLLDRLPGQ---LSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPistSKIEELMGSLKE-----KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYN 231
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDP---ALRQEMLDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
250
....*....|....*...
gi 1391526133 232 DTEQMFSMPQDKRTEDYI 249
Cdd:COG3840 213 PTAALLDGEPPPALAAYL 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-207 |
4.22e-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: 130.42 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpkVDTTLL 86
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQ---KGQILIDGIDIRD--ISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKlDEIVEKSLRDAAIFDEVKDR-------LKKSALGLSGGQQQRL 159
Cdd:cd03254 76 RSMIGVVLQDTFLFSGTIMENIRLG------RPNAT-DEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-212 |
4.28e-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: 129.08 E-value: 4.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTTLLRKKVGMVFQQPNP-- 99
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQ---SGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDDql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 FPMSVYDNIAYGPRIHGIRsrvklDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLS-----EAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 1391526133 180 ALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQA 212
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-215 |
4.53e-37 |
|
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: 137.20 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSpkV 81
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF--LDPQ---SGSITLGGVDLRD--L 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNPFPMSVYDNIAYGprihgirsrvkldeivekslRDAAIFDEVKDRLKKSALG----------- 150
Cdd:COG4987 403 DEDDLRRRIAVVPQRPHLFDTTLRENLRLA--------------------RPDATDEELWAALERVGLGdwlaalpdgld 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 151 ---------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI-EELMGSLKEKyTVAIVTHN---MQQATRI 215
Cdd:COG4987 463 twlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGR-TVLLITHRlagLERMDRI 539
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-241 |
7.58e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 135.97 E-value: 7.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKS-TFLKTLNrmndLVPN--VKIEGKVLLDGEDI--YSPK 80
Cdd:COG4172 9 VEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSILR----LLPDpaAHPSGSILFDGQDLlgLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VdttlLRK----KVGMVFQQP----NPFpMSVYDNIAYGPRIH-GIRSRVKLDEIVEkSLRDAAIfDEVKDRLKKSALGL 151
Cdd:COG4172 85 E----LRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHrGLSGAAARARALE-LLERVGI-PDPERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--THNMQQATRISDYTAFFLVGEMVE 229
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLliTHDLGVVRRFADRVAVMRQGEIVE 237
|
250
....*....|..
gi 1391526133 230 YNDTEQMFSMPQ 241
Cdd:COG4172 238 QGPTAELFAAPQ 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-228 |
1.42e-36 |
|
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: 128.64 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSpkvDTTLLR 87
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPT---SGRATVAGHDVVR---EPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFdEVKDRLKKSalgLSGGQQQRLCIARALA 166
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLYGV-PGAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-217 |
3.11e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 132.15 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPnvkIEGKVLLDGEDI--YSPKvdtTLL---RKKVGMVFQQ 96
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE--P---TAGEVLIDGEDItkLSKK---ELRelrRKKMSMVFQH 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 ----PNpfpMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLrdaaifDEV--KDRLKKSALGLSGGQQQRLCIARALAVEPE 170
Cdd:COG4175 114 fallPH---RTVLENVAFGLEIQGV-PKAERRERAREAL------ELVglAGWEDSYPDELSGGMQQRVGLARALATDPD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 171 VLLMDEPTSALDPIstskI-----EELMgSL--KEKYTVAIVTHNMQQATRISD 217
Cdd:COG4175 184 ILLMDEAFSALDPL----IrremqDELL-ELqaKLKKTIVFITHDLDEALRLGD 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-209 |
3.24e-36 |
|
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: 128.12 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIysPKVDTTLL 86
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD--VS---SGSILIDGQDI--REVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFPMSVYDNIAYGprihgirsRVKL-DEIVEKSLRDAAIFDEVKD-------RLKKSALGLSGGQQQR 158
Cdd:cd03253 74 RRAIGVVPQDTVLFNDTIGYNIRYG--------RPDAtDEEVIEAAKAAQIHDKIMRfpdgydtIVGERGLKLSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM 209
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-237 |
5.86e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 128.71 E-value: 5.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GT---NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDIYSPKV- 81
Cdd:PRK13649 3 INLQNVSYTYqaGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH--VPT---QGSVRVDDTLITSTSKn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 -DTTLLRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDrlkKSALGLSGGQQQR 158
Cdd:PRK13649 78 kDIKQIRKKVGLVFQFPESqlFEETVLKDVAFGPQNFGV-SQEEAEALAREKLALVGISESLFE---KNPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-212 |
1.07e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 127.67 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYG----TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlNRMNDLVPnvKIEGKVLLDGEDIYSPKVD 82
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGFLA--PSSGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 ttllRkkvGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLR--------DAAIFDevkdrlkksalgLSG 153
Cdd:COG4525 78 ----R---GVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLAlvgladfaRRRIWQ------------LSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQA 212
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-207 |
1.30e-35 |
|
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: 126.15 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMdIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVkiEGKVLLDGEDIyspKVDTTLLR 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRILA---TLTPPS--SGTIRIDGQDV---LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRLCIARALA 166
Cdd:cd03264 72 RRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSK-EVKARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
10-249 |
2.07e-35 |
|
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: 129.00 E-value: 2.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDI--YSPKvdttllR 87
Cdd:TIGR03265 7 IDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDItrLPPQ------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGprIHGirSRVKLDEIVEK--SLRDAAIFDEVKDrlkKSALGLSGGQQQRLCIARA 164
Cdd:TIGR03265 76 RDYGIVFQSYALFPnLTVADNIAYG--LKN--RGMGRAEVAERvaELLDLVGLPGSER---KYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 165 LAVEPEVLLMDEPTSALDpistSKI-EELMGSLKE-----KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR 224
|
250
....*....|.
gi 1391526133 239 MPQDKRTEDYI 249
Cdd:TIGR03265 225 HPATPFVADFV 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
2.47e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTTL--LRKKVGMVFQQPNP 99
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPT---SGTVTIGERVITAGKKNKKLkpLRKKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 --FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 177
Cdd:PRK13634 97 qlFEETVEKDICFGPMNFGV-SEEDAKQKAREMIELVGLPEEL---LARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 178 TSALDPISTSKIEELMGSL-KEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQD 242
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLhKEKgLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-215 |
5.26e-35 |
|
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: 125.04 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYG--TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYspkvDTTL 85
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDVR----DYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 --LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEiVEKSLRdAAIFDEVKDRLKK---SALG-----LSGGQ 155
Cdd:cd03251 72 asLRRQIGLVSQDVFLFNDTVAENIAYG------RPGATREE-VEEAAR-AANAHEFIMELPEgydTVIGergvkLSGGQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRI 215
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLstiENADRI 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-209 |
5.90e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 126.50 E-value: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHY--GTnHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDI-YSPK 80
Cdd:PRK13636 2 EDYILKVEELNYNYsdGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIdYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 vDTTLLRKKVGMVFQQPNP--FPMSVYDNIAYGPrihgIRSRVKLDEI---VEKSLRDAAIfDEVKDrlkKSALGLSGGQ 155
Cdd:PRK13636 76 -GLMKLRESVGMVFQDPDNqlFSASVYQDVSFGA----VNLKLPEDEVrkrVDNALKRTGI-EHLKD---KPTHCLSFGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNM 209
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDI 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-241 |
9.59e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 130.19 E-value: 9.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHY-----------GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPNvkiEGKVLLDGEDIys 78
Cdd:COG4172 278 ARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPS---EGEIRFDGQDL-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 79 pkvdTTL-------LRKKVGMVFQQP----NPfPMSVYDNIAYGPRIHGI-RSRVKLDEIVekslrdAAIFDEVkdRLKK 146
Cdd:COG4172 350 ----DGLsrralrpLRRRMQVVFQDPfgslSP-RMTVGQIIAEGLRVHGPgLSAAERRARV------AEALEEV--GLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 147 SALG-----LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTSK-IEELMGSLKEKYTVA--IVTHNMQQATRISDY 218
Cdd:COG4172 417 AARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHGLAylFISHDLAVVRALAHR 495
|
250 260
....*....|....*....|....*.
gi 1391526133 219 TaffLV---GEMVEYNDTEQMFSMPQ 241
Cdd:COG4172 496 V---MVmkdGKVVEQGPTEQVFDAPQ 518
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
8-210 |
1.71e-34 |
|
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: 123.13 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYS-PKVDTTL 85
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA--LTPS---RGQVRIAGEDVNRlRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVKldeivekslrdaAIFDEV--KDRLKKSALGLSGGQQQ 157
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPdRTVYENVALPLEVRGkkereIQRRVG------------AALRQVglEHKADAFPEQLSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTskiEELMGSLKEKY----TVAIVTHNMQ 210
Cdd:TIGR02673 145 RVAIARAIVNSPPLLLADEPTGNLDPDLS---ERILDLLKRLNkrgtTVIVATHDLS 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-217 |
2.33e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.37 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIySPKVdttlLR 87
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPI-KAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNP--FPMSVYDNIAYGPRIHGirsrvKLDEIVEKSLRDAAIFDEvKDRLKKSalgLSGGQQQRLCIARAL 165
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKELD-----AGNEQAETVLKDLDLYAL-KERHPLS---LSGGQKQRLAIAAAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISD 217
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCD 194
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-236 |
2.97e-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: 123.02 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNdLVPnVKiEGKVLLDGEDIyspkvdTTL---- 85
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MG-LLP-VK-SGSIRLDGEDI------TKLpphe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 -LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEkslrdaaIFDEVKDRLKKSALGLSGGQQQRLCIAR 163
Cdd:TIGR03410 72 rARAGIAYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAIllVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-217 |
5.47e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.22 E-value: 5.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKtlnrmndLVPNVK--IEGKVLLDGEDIyspkVDTTLLRKK 89
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDV----THRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVKldEIVEksLRDAAIFDevkDRLKKSalgLSGGQQQRLCIAR 163
Cdd:PRK11432 80 ICMVFQSYALFPhMSLGENVGYGLKMLGvpkeeRKQRVK--EALE--LVDLAGFE---DRYVDQ---ISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 164 ALAVEPEVLLMDEPTSALDP-ISTS---KIEELMGSLkeKYTVAIVTHNMQQATRISD 217
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDAnLRRSmreKIRELQQQF--NITSLYVTHDQSEAFAVSD 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-207 |
1.04e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 127.40 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTtl 85
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPT---EGSIAVNGVPLADADADS-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEIVEkSLRDAAIFDEVKDR-------LKKSALGLSGGQQQR 158
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIRLA------RPDASDAEIRE-ALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQR 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-234 |
5.77e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.00 E-value: 5.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTnHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDIYspKVDTTL 85
Cdd:PRK13647 5 IEVEDLHFRYkdGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY--LPQ---RGRVKVMGREVN--AENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIRsRVKLDEIVEKSLRDAAIFDeVKDrlkKSALGLSGGQQQRLCIAR 163
Cdd:PRK13647 77 VRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLD-KDEVERRVEEALKAVRMWD-FRD---KPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTE 234
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-240 |
6.83e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 120.68 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIysPKVDTTLL 86
Cdd:PRK13652 4 IETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPT---SGSVLIRGEPI--TKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIRSRVkLDEIVEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRLCIARA 164
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGLDEET-VAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-240 |
7.68e-33 |
|
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: 121.83 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 39 IGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIyspkVDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGI 117
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 118 rSRVKLDEIVEKSLRDAaifdEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistSKIEELMG--- 194
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLV----QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQlel 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391526133 195 -SLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:TIGR01187 144 kTIQEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-241 |
9.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.57 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHY----GTnHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTTL 85
Cdd:PRK13639 2 LETRDLKYsypdGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPT---SGEVLIKGEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIRsrvklDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIAR 163
Cdd:PRK13639 76 VRKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGLS-----KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-217 |
9.49e-33 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 118.47 E-value: 9.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIyspkVDTTLLR 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII--LGLIKPD---SGEITFDGKSY----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRsrvklDEIVEKSLRDAAIFDEVKDRLKKSALGLsggqQQRLCIARALA 166
Cdd:cd03268 72 RRIGALIEAPGFYPnLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGM----KQRLGIALALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISD 217
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVAD 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-208 |
1.52e-32 |
|
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: 118.28 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNvkiEGKVLLDGEDIYS-PKVDTTL 85
Cdd:cd03292 1 IEFINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPT---SGTIRVNGQDVSDlRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvkldEIVEkslRDAAIFDEVKDRLKKSAL--GLSGGQQQRLCIA 162
Cdd:cd03292 76 LRRKIGVVFQDFRLLPdRNVYENVAFALEVTGVPPR----EIRK---RVPAALELVGLSHKHRALpaELSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHN 208
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
7-217 |
2.78e-32 |
|
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: 120.98 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVeNLNLHYGtNHALkNVNMDIFKNKITAFIGPSGCGKSTFLKT---LNRmndlvPNvkiEGKVLLDGEDIYSPKVDT 83
Cdd:COG4148 2 MLEV-DFRLRRG-GFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER-----PD---SGRIRLGGEVLQDSARGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLL--RKKVGMVFQQPNPFP-MSVYDNIAYG-PRIHGIRSRVKLDEIVE----KSLrdaaifdevkdrLKKSALGLSGGQ 155
Cdd:COG4148 71 FLPphRRRIGYVFQEARLFPhLSVRGNLLYGrKRAPRAERRISFDEVVEllgiGHL------------LDRRPATLSGGE 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISD 217
Cdd:COG4148 139 RQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPIlyVSHSLDEVARLAD 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-217 |
4.18e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.57 E-value: 4.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKT---LNRMNdlvpnvkiEGKVLLDGEDiyspkVDT 83
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIiagLEHQT--------SGHIRFHGTD-----VSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLR-KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEK--SLRDAAIFDEVKDRLKKSalgLSGGQQQRL 159
Cdd:PRK10851 69 LHARdRKVGFVFQHYALFRhMTVFDNIAFGLTVLPRRERPNAAAIKAKvtQLLEMVQLAHLADRYPAQ---LSGGQKQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE--KYTVAIVTHNMQQATRISD 217
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVAD 205
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-220 |
5.30e-32 |
|
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: 119.03 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 16 HYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSpkvDTTLLRKKVGMVFQ 95
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDVVR---EPRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 96 QPNPFP-MSVYDNIAYGPRIHGI---RSRVKLDEIVEK-SLRDAAifdevkDRLKKsalGLSGGQQQRLCIARALAVEPE 170
Cdd:TIGR01188 74 YASVDEdLTGRENLEMMGRLYGLpkdEAEERAEELLELfELGEAA------DRPVG---TYSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 171 VLLMDEPTSALDPISTSKIEELMGSLKE-KYTVAIVTHNMQQATRISDYTA 220
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIA 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-217 |
6.66e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.83 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGE--DIYSPKvDTtlLR 87
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL--SGLYKPD---SGEILVDGKevSFASPR-DA--RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQqpnpfpmsvydniaygprihgirsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARALAV 167
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISD 217
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIAD 150
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-183 |
7.05e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.43 E-value: 7.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNVKIEGKVLLDGEDIyspkvdTTL--L 86
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRL------TALpaE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFP-MSVYDNIAYGprihgirsrvkLDEIVEKSLRDAAifdeVKDRLKKSALG---------LSGGQQ 156
Cdd:COG4136 75 QRRIGILFQDDLLFPhLSVGENLAFA-----------LPPTIGRAQRRAR----VEQALEEAGLAgfadrdpatLSGGQR 139
|
170 180
....*....|....*....|....*..
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDP 183
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-217 |
8.91e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 8.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGE--DIYSPKVDttlLR 87
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGV--YQPD---SGEILLDGEpvRFRSPRDA---QA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYG--PRIHGIRSRVKLdeiveksLRDA-AIFDEVKDRLKKSAL--GLSGGQQQRLCI 161
Cdd:COG1129 79 AGIAIIHQELNLVPnLSVAENIFLGrePRRGGLIDWRAM-------RRRArELLARLGLDIDPDTPvgDLSVAQQQLVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKyTVAI--VTHNMQQATRISD 217
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIiyISHRLDEVFEIAD 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-229 |
9.04e-32 |
|
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: 116.82 E-value: 9.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN--HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSpkVDTTL 85
Cdd:cd03252 1 ITFEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPE---NGRVLVDGHDLAL--ADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEIVE-KSLRDAAIF--------DEVkdrLKKSALGLSGGQQ 156
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALA------DPGMSMERVIEaAKLAGAHDFiselpegyDTI---VGEQGAGLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMqQATRISDYTAFFLVGEMVE 229
Cdd:cd03252 145 QRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVE 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-215 |
1.24e-31 |
|
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: 116.03 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIysPKVDTTLLRKKVGMVFQQPNPFPM 102
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPI--SQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 103 SVYDNIAYGprihgiRSRVKLDEIVEkslrdAAIFDEVKDRLKKSALG-----------LSGGQQQRLCIARALAVEPEV 171
Cdd:cd03248 103 SLQDNIAYG------LQSCSFECVKE-----AAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRI 215
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLstvERADQI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-242 |
3.00e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.65 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPN---VKIEGKVLlDGEDIYSpkvd 82
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPEagtITVGGMVL-SEETVWD---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 ttlLRKKVGMVFQQP-NPF-PMSVYDNIAYGPRIHGIrSRvklDEIVEKSlrDAAIfDEV--KDRLKKSALGLSGGQQQR 158
Cdd:PRK13635 79 ---VRRQVGMVFQNPdNQFvGATVQDDVAFGLENIGV-PR---EEMVERV--DQAL-RQVgmEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQATRiSDYTAFFLVGEMVEYNDTEQM 236
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
....*.
gi 1391526133 237 FSMPQD 242
Cdd:PRK13635 228 FKSGHM 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-228 |
3.53e-31 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 115.85 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 11 ENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDI--YSPKVdttlLRK 88
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIqhYASKE----VAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQQP-NPFPMSVYDNIAYGPRIHG---IRSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARA 164
Cdd:PRK10253 82 RIGLLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI----THLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEK-YTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKgYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
8-215 |
5.22e-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: 120.83 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndLVPNVKIEGKVLLDGEDIysPKVDTTL 85
Cdd:TIGR03797 452 IEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDL--AGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgirSRVKLDEIVEkSLRDAAIFDEVKDR-------LKKSALGLSGGQQQR 158
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIAGG-------APLTLDEAWE-AARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQR 596
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPIstskieelmgslkekyTVAIVTHNM--QQATRI 215
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNR----------------TQAIVSESLerLKVTRI 639
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-251 |
1.24e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.48 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiEGKVLLDGEDIysPKVDTTLL- 86
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPD---HGEILFDGENI--PAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 --RKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG------IRSRV--KLDEIvekSLRDAAifdevkdRLKKSALglSGGQ 155
Cdd:PRK11831 81 tvRKRMSMLFQSGALFTdMNVFDNVAYPLREHTqlpaplLHSTVmmKLEAV---GLRGAA-------KLMPSEL--SGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYtAFFLVGEMVEYNDT 233
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIADH-AYIVADKKIVAHGS 227
|
250
....*....|....*...
gi 1391526133 234 EQMFSMPQDKRTEDYITG 251
Cdd:PRK11831 228 AQALQANPDPRVRQFLDG 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-249 |
1.73e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.47 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIyspkVDTTLLR 87
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--PT---AGQIMLDGVDL----SHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRihgiRSRVKLDEIvekSLRDAAIFDEV--KDRLKKSALGLSGGQQQRLCIARA 164
Cdd:PRK11607 91 RPINMMFQSYALFPhMTVEQNIAFGLK----QDKLPKAEI---ASRVNEMLGLVhmQEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQD 242
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
....*..
gi 1391526133 243 KRTEDYI 249
Cdd:PRK11607 244 RYSAEFI 250
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-218 |
2.20e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIySPKVdttll 86
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGILAPD---SGEVLWDGEPL-DPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVG-MvfqqpnpfP--------MSVYDNIAYGPRIHGI---RSRVKLDEIVEKslrdaaiFdEVKDRLKKSALGLSGG 154
Cdd:COG4152 70 RRRIGyL--------PeerglypkMKVGEQLVYLARLKGLskaEAKRRADEWLER-------L-GLGDRANKKVEELSKG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDY 218
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDR 198
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-215 |
5.96e-30 |
|
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: 110.00 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHA--LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSpkVDTTL 85
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLI--LGLLRPT---SGRVRLDGADISQ--WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIaygprihgirsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARAL 165
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNM---QQATRI 215
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-241 |
6.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.39 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHVENLNLHY--GT---NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPK 80
Cdd:PRK13641 1 MSIKFENVDYIYspGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHITPET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VDTTL--LRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDrlkKSALGLSGGQQ 156
Cdd:PRK13641 76 GNKNLkkLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGF-SEDEAKEKALKWLKKVGLSEDLIS---KSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQatrISDYTAFFLV---GEMVEYND 232
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDD---VAEYADDVLVlehGKLIKHAS 228
|
....*....
gi 1391526133 233 TEQMFSMPQ 241
Cdd:PRK13641 229 PKEIFSDKE 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-215 |
7.18e-30 |
|
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: 111.14 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYspKVDTTL 85
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPT---SGSVLLDGTDIR--QLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGirsrvklDEIVEKSLRDAAIFDEVKDRLKKSAL-------GLSGGQQQR 158
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLGAPLAD-------DERILRAAELAGVTDFVNKHPNGLDLqigergrGLSGGQRQA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSK-IEELMGSLKEKyTVAIVTHNM---QQATRI 215
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERlKERLRQLLGDK-TLIIITHRPsllDLVDRI 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-217 |
8.58e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.66 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIyspkVDTTLLR 87
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI----THVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHgirsRVKLDEI---VEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRLCIAR 163
Cdd:PRK09452 86 RHVNTVFQSYALFPhMTVFENVAFGLRMQ----KTPAAEItprVMEALRMVQL-EEFAQRKPHQ---LSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 164 ALAVEPEVLLMDEPTSALDpistSKIEELMGS----LKEKY--TVAIVTHNMQQATRISD 217
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD----YKLRKQMQNelkaLQRKLgiTFVFVTHDQEEALTMSD 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-244 |
1.75e-29 |
|
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: 110.83 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTflkTLNRMNDLVPNVkiEGKVLLDGEDIYSPKVDttlL 86
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVRPD--AGKILIDGQDITHLPMH---E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVF--QQPNPF-PMSVYDNIaygprIHGIRSRVKLDEIVEKSLRDAAIFD-EVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:TIGR04406 73 RARLGIGYlpQEASIFrKLTVEENI-----MAVLEIRKDLDRAEREERLEALLEEfQISHLRDNKAMSLSGGERRRVEIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERgIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
...
gi 1391526133 242 DKR 244
Cdd:TIGR04406 228 VRR 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-217 |
2.27e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.02 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPnvkIEGKVLLDGEDI--YSPkvdt 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSP---DSGEVRLNGRPLadWSP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPN-PFPMSVYDNIAYGpRIHGIRSRVKLDEIVEKSLRDAAIfDEVKDRlkkSALGLSGGQQQRLCIA 162
Cdd:PRK13548 72 AELARRRAVLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDL-AHLAGR---DYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 163 RALA------VEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISD 217
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYAD 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-210 |
2.99e-29 |
|
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: 108.55 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN--HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmnDLVPNvkiEGKVLLDGEDIYSPKvdtTL 85
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLE---KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIaygprihGIRsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARAL 165
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL-------GRR--------------------------------FSGGERQRLALARIL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQ 210
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLT 158
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-233 |
3.47e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.72 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRM------------NDLVPNVKIEGKVLLDGEDIYSPKVDTTL---- 85
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifKDEKNKKKTKEKEKVLEKLVIQKTRFKKIkkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 -LRKKVGMVFQ--QPNPFPMSVYDNIAYGPRIHGirsrVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:PRK13651 102 eIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG----VSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDT 233
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-237 |
3.61e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.36 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEdiySPKVD 82
Cdd:PRK13643 2 IKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSST---SKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNP--FPMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfdeVKDRLKKSALGLSGGQQQRLC 160
Cdd:PRK13643 79 IKPVRKKVGVVFQFPESqlFEETVLKDVAFGPQNFGI-PKEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-251 |
4.19e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.20 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIysPKVDTTLLR----KKVGMV 93
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDI--AKISDAELRevrrKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 94 FQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEkSLRDAAifdevkdrLKKSALG----LSGGQQQRLCIARALAVE 168
Cdd:PRK10070 112 FQSFALMPhMTVLDNTAFGMELAGINAEERREKALD-ALRQVG--------LENYAHSypdeLSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 169 PEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRTE 246
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
....*
gi 1391526133 247 DYITG 251
Cdd:PRK10070 263 TFFRG 267
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-208 |
6.20e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 113.99 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIYSpkVD 82
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVSS--LD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKlDEIVEKSLRDAAIFDEVKDR-------LKKSALGLSGGQ 155
Cdd:TIGR02868 404 QDEVRRRVSVCAQDAHLFDTTVRENLRLA------RPDAT-DEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHN 208
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
10-215 |
7.08e-29 |
|
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: 108.47 E-value: 7.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDI--YSPKVDTTLLR 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEK-----FDSGQVYLNGQETppLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQpnpFPM----SVYDNIAYGpRIHGIRSRVKLDEIVEKSLRDAAIFDevkdRLKKSALGLSGGQQQRLCIAR 163
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLG-LKYKKLSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNM---QQATRI 215
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
32-228 |
7.58e-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: 108.35 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 32 KNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDI-YSPKVDttllrKKVGMVFQQPNPFP-MSVYDNIA 109
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGF--ETPQ---SGRVLINGVDVtAAPPAD-----RPVSMLFQENNLFAhLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 110 YGpRIHGIRSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI 189
Cdd:cd03298 93 LG-LSPGLKLTAEDRQAIEVALARVGL----AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391526133 190 EELMGSL--KEKYTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03298 168 LDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-217 |
1.28e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 111.27 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTL---------------NRMNDLVPNvkiegkvlldgedi 76
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigeKRMNDVPPA-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 77 yspkvdttllRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHG-----IRSRVkldEIVEKSLRDAAIFDevkdRLKKSalg 150
Cdd:PRK11000 74 ----------ERGVGMVFQSYALYPhLSVAENMSFGLKLAGakkeeINQRV---NQVAEVLQLAHLLD----RKPKA--- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 151 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDP-------ISTSKIEELMGSlkekyTVAIVTHNMQQATRISD 217
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmrIEISRLHKRLGR-----TMIYVTHDQVEAMTLAD 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-217 |
2.11e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.59 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 20 NHALKnVNMDIFKNKITAFIGPSGCGKSTFLktlNRMNDLV-PNvkiEGKVLLDGEDIYSP--KVDTTLLRKKVGMVFQQ 96
Cdd:TIGR02142 11 DFSLD-ADFTLPGQGVTAIFGRSGSGKTTLI---RLIAGLTrPD---EGEIVLNGRTLFDSrkGIFLPPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNPFP-MSVYDNIAYGPRihgiRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:TIGR02142 84 ARLFPhLSVRGNLRYGMK----RARPSERRISFERVIELLGIGHLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391526133 176 EPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISD 217
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPIlyVSHSLQEVLRLAD 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-237 |
2.51e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.55 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLN-----RMNDL-VPNVKIEGKVLLDGEDIY--SPKV-DTTLLRKKVGM 92
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIqVGDIYIGDKKNNHELITNpySKKIkNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 93 VFQQP--NPFPMSVYDNIAYGP---RIHGIRSRVKLDEIVEK-SLRDaaifdevkDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPvalGVKKSEAKKLAKFYLNKmGLDD--------SYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEEL-MGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMF 237
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-207 |
3.00e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.42 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 2 EKEQVTIHVENLNLHY-GTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYsp 79
Cdd:PRK11176 336 ERAKGDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDLR-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 kvDTTL--LRKKVGMVFQQPNPFPMSVYDNIAYGPRihGIRSRvkldEIVEKSLRDAAIFDEVKdRLKK---SALG---- 150
Cdd:PRK11176 409 --DYTLasLRNQVALVSQNVHLFNDTIANNIAYART--EQYSR----EQIEEAARMAYAMDFIN-KMDNgldTVIGengv 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 151 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:PRK11176 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-236 |
3.59e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 112.51 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIysPKVDTTLLRKKVGMVFQQPNPFPM 102
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQPT---GGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 103 SVYDNIAYGprihgirsrvkLDEIVEKSLRDAAIFDEVKDRLKKSALG-----------LSGGQQQRLCIARALAVEPEV 171
Cdd:TIGR00958 570 SVRENIAYG-----------LTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 172 LLMDEPTSALDpistSKIEELMGSLKEKY--TVAIVTHNMQQATRiSDYTAFFLVGEMVEYNDTEQM 236
Cdd:TIGR00958 639 LILDEATSALD----AECEQLLQESRSRAsrTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
4.19e-28 |
|
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: 107.17 E-value: 4.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSPKVDTTLlrkkvgmVFQQPNPFP- 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQ--PT---SGGVILEGKQITEPGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MSVYDNIAYG-PRIHGIRSRVKLDEIVEKS-----LRDAAifdevkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:TIGR01184 69 LTVRENIALAvDRVLPDLSKSERRAIVEEHialvgLTEAA---------DKRPGQLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391526133 176 EPTSALDPISTSKI-EELMGSLKE-KYTVAIVTHNMQQATRISD 217
Cdd:TIGR01184 140 EPFGALDALTRGNLqEELMQIWEEhRVTVLMVTHDVDEALLLSD 183
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-215 |
5.38e-28 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 111.73 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 2 EKEQVT--IHVENLNLHYGTNH--ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIy 77
Cdd:TIGR02203 323 AIERARgdVEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDL- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 78 spkVDTTL--LRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVkldeivEKSLRDAAIFDEVkDRLKK--------S 147
Cdd:TIGR02203 397 ---ADYTLasLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEI------ERALAAAYAQDFV-DKLPLgldtpigeN 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 148 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRI 215
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKADRI 537
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-210 |
6.62e-28 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.88 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYspKVDTTL 85
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL--LGLYQPT---EGSVLLDGVDIR--QIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYG-PRIHgirsrvklDEIVEKSLRDAAIFDEVKD-------RLKKSALGLSGGQQQ 157
Cdd:TIGR03375 537 LRRNIGYVPQDPRLFYGTLRDNIALGaPYAD--------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQRQ 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSK-IEELMGSLKEKyTVAIVTHNMQ 210
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERfKDRLKRWLAGK-TLVLVTHRTS 661
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-215 |
8.44e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 105.24 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNH-----ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVpnvKIEGKVLLDGediyspkvd 82
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 ttllrkKVGMVFQQPNPFPMSVYDNIAYGPRIHgirsRVKLDEIVEKS--LRDAAIFD-----EVKDRlkksALGLSGGQ 155
Cdd:cd03250 67 ------SIAYVSQEPWIQNGTIRENILFGKPFD----EERYEKVIKACalEPDLEILPdgdltEIGEK----GINLSGGQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEE--LMGSLKEKYTVAIVTHNMQ---QATRI 215
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQllpHADQI 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-230 |
1.24e-27 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 105.19 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN--HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIysPKVDTTL 85
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDI--STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVydniaygprihgirsRVKLDEIVEKSlrDAAIFDEVkdRLKKSALGLSGGQQQRLCIARAL 165
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTI---------------RSNLDPFDEYS--DEEIYGAL--RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQatrISDYTAFFLV--GEMVEY 230
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRT---IIDYDKILVMdaGEVKEY 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-248 |
1.24e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNVkieGKVLLDGEDIYSPKVDTTL--LRKKVGMVFQQPNP 99
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKPTT---GTVTVDDITITHKTKDKYIrpVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 --FPMSVYDNIAYGPRIHGIrsrvKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 177
Cdd:PRK13646 97 qlFEDTVEREIIFGPKNFKM----NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 178 TSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSmpQDKRTEDY 248
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADW 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-228 |
1.38e-27 |
|
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: 105.14 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY----GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDT 83
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPD---AGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 tllRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSR---VKLDEIVEKSlrdaaifdEVKDRLKKSALGLSGGQQQRL 159
Cdd:cd03266 77 ---RRRLGFVSDSTGLYDrLTARENLEYFAGLYGLKGDeltARLEELADRL--------GMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMV 228
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-245 |
1.54e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.32 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTflkTLNRMNDLV-PNvkiEGKVLLDGEDIYSPKVDTtllRK 88
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLVkPD---SGKILLDGQDITKLPMHK---RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVF--QQPNPF-PMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfDEVKDRLkksALGLSGGQQQRLCIARAL 165
Cdd:cd03218 74 RLGIGYlpQEASIFrKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDyTAFFLV-GEMVEYNDTEQMFSMPQDK 243
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITD-RAYIIYeGKVLAEGTPEEIAANELVR 227
|
..
gi 1391526133 244 RT 245
Cdd:cd03218 228 KV 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-208 |
1.66e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.18 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDI--YS 78
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPT---SGTLLFEGEDIstLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 79 PKVdttlLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKldeiveKSLRDAAIFDEVKDRLKKSALGLSGGQQQR 158
Cdd:PRK10247 76 PEI----YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPA------IFLDDLERFALPDTILTKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHN 208
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-183 |
2.09e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.58 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmnDLVPNvkiEGKVLLDGEDI--YSPKVdttl 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPLaaWSPWE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPN-PFPMSVYDNIAYGpRIHGIRSRVKLDEIVEKSLR--DAAIFdevKDRlkkSALGLSGGQQQRLCIA 162
Cdd:COG4559 73 LARRRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALAlvGLAHL---AGR---SYQTLSGGEQQRVQLA 145
|
170 180
....*....|....*....|....*...
gi 1391526133 163 RALA-------VEPEVLLMDEPTSALDP 183
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-212 |
2.84e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNVKIEGKVLLDGEDIYSPKVDTtlLRKKVGMVFQQP-NPF 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKTVWD--IREKVGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 -PMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:PRK13640 98 vGATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYIDSEPAN----LSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1391526133 180 ALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQA 212
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEA 207
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-213 |
5.00e-27 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 103.65 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDI----YSPKVdtTLLRKKVGMVFQQP 97
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLD-----SGSLTLAGKEVtnlsYSQKI--ILRRELIGYIFQSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 NPFP-MSVYDNIAYGPRIHGIRSRvkldEIVEKSLRDAAIFDeVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDE 176
Cdd:NF038007 93 NLIPhLSIFDNVALPLKYRGVAKK----ERIERVNQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1391526133 177 PTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQAT 213
Cdd:NF038007 168 PTGNLDSKNARAVLQQLKYINQKgTTIIMVTHSDEAST 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-212 |
1.01e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIySPKVDTTLLRKKVGMVFQQPNPFP 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPS---EGKVYVDGLDT-SDEENLWDIRNKAGMVFQNPDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MS--VYDNIAYGPRIHGIRSrvklDEI---VEKSLRDAAIFDevkdrLKKSALG-LSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:PRK13633 99 VAtiVEEDVAFGPENLGIPP----EEIrerVDESLKKVGMYE-----YRRHAPHlLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391526133 176 EPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQA 212
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-242 |
1.35e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.40 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN---HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIYSPKVDTt 84
Cdd:PRK13642 5 LEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAENVWN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 lLRKKVGMVFQQP-NPF-PMSVYDNIAYGPRIHGIRSrvklDEIVeKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:PRK13642 79 -LRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPR----EEMI-KRVDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRiSDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
..
gi 1391526133 241 QD 242
Cdd:PRK13642 232 ED 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-230 |
1.39e-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: 102.36 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspkvdTTLLR 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGKPL------DIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGirsrVKLDEIVEKSLRDAAIFdEVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:cd03269 70 NRIGYLPEERGLYPkMKVIDQLVYLAQLKG----LKKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEY 230
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-242 |
1.70e-26 |
|
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: 103.73 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN---------HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKIE----GKVLLDGE 74
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL---------LGLEkpaqGTVSFRGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 75 DIYspKVDTT---LLRKKVGMVFQQP----NPfPMSVYDNIAygpriHGIRSRVKLDEiVEKSLRDAAIFDEVK---DRL 144
Cdd:TIGR02769 74 DLY--QLDRKqrrAFRRDVQLVFQDSpsavNP-RMTVRQIIG-----EPLRHLTSLDE-SEQKARIAELLDMVGlrsEDA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 145 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVA--IVTHNMQQATRISDYTAFF 222
Cdd:TIGR02769 145 DKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAylFITHDLRLVQSFCQRVAVM 224
|
250 260
....*....|....*....|
gi 1391526133 223 LVGEMVEYNDTEQMFSMPQD 242
Cdd:TIGR02769 225 DKGQIVEECDVAQLLSFKHP 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-214 |
3.37e-26 |
|
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: 102.13 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVD- 82
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL--DRPT---SGTVRLAGQDLFALDEDa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 -TTLLRKKVGMVFQQ----PNpfpMSVYDNIAygprihgirsrVKLDEiveKSLRDAaiFDEVKDRLKKSALG------- 150
Cdd:COG4181 84 rARLRARHVGFVFQSfqllPT---LTALENVM-----------LPLEL---AGRRDA--RARARALLERVGLGhrldhyp 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 151 --LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATR 214
Cdd:COG4181 145 aqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-228 |
4.20e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlNRMNDLVPnvKIEGKVLLDGEDIYSPKVDTtllr 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVP--YQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 kkvGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLR--DAAIFDevkdrlKKSALGLSGGQQQRLCIARA 164
Cdd:PRK11248 73 ---GVVFQNEGLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKkvGLEGAE------KRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATrisdytafFLVGEMV 228
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEAV--------FMATELV 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-217 |
6.05e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGE--DIYSPKVdttL 85
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGL--YQPD---SGEILIDGKpvRIRSPRD---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFP-MSVYDNIAYG--PRIHGIRSRVKL-DEIVEKSLR-------DAAIFDevkdrlkksalgLSGG 154
Cdd:COG3845 78 IALGIGMVHQHFMLVPnLTVAENIVLGlePTKGGRLDRKAArARIRELSERygldvdpDAKVED------------LSVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALDPistSKIEELMGSLK----EKYTVAIVTHNMQQATRISD 217
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIAD 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-207 |
6.62e-26 |
|
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: 100.63 E-value: 6.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSPKVDttlLR 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPPS---AGEVLWNGEPIRDARED---YR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIR-SRVKLDEIVEK-SLRDAAifdevkDRLkksALGLSGGQQQRLCIARA 164
Cdd:COG4133 75 RRLAYLGHADGLKPeLTVRENLRFWAALYGLRaDREAIDEALEAvGLAGLA------DLP---VRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGS-LKEKYTVAIVTH 207
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-217 |
1.07e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTflkTLNRMNDLV-PNvkiEGKVLLDGEDIyspkvdTTL 85
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGLVkPD---SGRIFLDGEDI------THL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 ---LRKKVGM--------VFQQpnpfpMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIfdevkDRLKKS-ALGLSG 153
Cdd:COG1137 71 pmhKRARLGIgylpqeasIFRK-----LTVEDNILAVLELRKL-SKKEREERLEELLEEFGI-----THLRKSkAYSLSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISD 217
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICD 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
12-241 |
1.26e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHY----------GTNHALKNVNMDIFKNKITAFIGPSGCGKSTflktLNRMNDLV--PNvkiEGKVLLDGEDIYSP 79
Cdd:PRK11308 10 DLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIetPT---GGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 -KVDTTLLRKKVGMVFQQP----NPfpmsvydniaygprihgirsRVKLDEIVEKSLR-----DAAifdEVKDRLKK--S 147
Cdd:PRK11308 83 dPEAQKLLRQKIQIVFQNPygslNP--------------------RKKVGQILEEPLLintslSAA---ERREKALAmmA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 148 ALGL------------SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--THNMQQAT 213
Cdd:PRK11308 140 KVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVfiSHDLSVVE 219
|
250 260
....*....|....*....|....*...
gi 1391526133 214 RISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK11308 220 HIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-218 |
1.41e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.93 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPnvKIEGKVLLDGEDIYSPKVDTtlLR 87
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---LLP--PDSGEVLVDGLDVATTPSRE--LA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGmVFQQPNPFPM--SVYDNIAYG--PriHgirSRVKLDEivekslRDAAIFDEVKDRLKKSALG------LSGGQQQ 157
Cdd:COG4604 75 KRLA-ILRQENHINSrlTVRELVAFGrfP--Y---SKGRLTA------EDREIIDEAIAYLDLEDLAdryldeLSGGQRQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDpISTSKieELMGSLKE-----KYTVAIVTHNMQQATRISDY 218
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLD-MKHSV--QMMKLLRRladelGKTVVIVLHDINFASCYADH 205
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-230 |
1.76e-25 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.88 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIysPKVDTTL 85
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDI--SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAygP-------RIHGIRSRVKLDEIVEKSLrdaaifDEVKDRLKKSALGLSGGQQQR 158
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLD--PfgeysdeELWQALERVGLKEFVESLP------GGLDTVVEEGGENLSVGQRQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELmgsLKEKY---TVAIVTHnmqqatRIS---DYtAFFLV---GEMVE 229
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkdcTVLTIAH------RLDtiiDS-DRILVldkGRVVE 217
|
.
gi 1391526133 230 Y 230
Cdd:cd03244 218 F 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
8-207 |
5.42e-25 |
|
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: 99.00 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmnDLVP----NVKIEGKVLlDGEDIYSpkvdt 83
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPtygnDVRLFGERR-GGEDVWE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 tlLRKKVGMV---FQQPNPFPMSVYDNI---AYGprIHGIRSRVKlDEIVEKSLRDAAIFDeVKDRLKKSALGLSGGQQQ 157
Cdd:COG1119 76 --LRKRIGLVspaLQLRFPRDETVLDVVlsgFFD--SIGLYREPT-DEQRERARELLELLG-LAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTH 207
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLvlVTH 201
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
9-207 |
7.21e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 103.10 E-value: 7.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 9 HVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDG---EDIysPKv 81
Cdd:TIGR03796 477 YVELRNITFGYSplepPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ-----PWSGEILFDGiprEEI--PR- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 dtTLLRKKVGMVFQQPNPFPMSVYDNIA-YGPRIhgirsrvkLDEIVEKSLRDAAIFDEVKDR-------LKKSALGLSG 153
Cdd:TIGR03796 549 --EVLANSVAMVDQDIFLFEGTVRDNLTlWDPTI--------PDADLVRACKDAAIHDVITSRpggydaeLAEGGANLSG 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPIsTSKIeeLMGSLKEK-YTVAIVTH 207
Cdd:TIGR03796 619 GQRQRLEIARALVRNPSILILDEATSALDPE-TEKI--IDDNLRRRgCTCIIVAH 670
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-206 |
1.42e-24 |
|
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: 97.73 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlVPNVKI-EGKVLLDGEdiyspKVDTTLLRKKVGMVFQQPNPFP 101
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTtSGQILFNGQ-----PRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 -MSVYDNIAY-----GPRIHGIRSRVKLDEIVekSLRDAAIFDEVKDRLKksalGLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:cd03234 95 gLTVRETLTYtailrLPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLVK----GISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|.
gi 1391526133 176 EPTSALDPISTSKIEELMGSLKEKYTVAIVT 206
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-240 |
1.86e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.41 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNH----ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVKIEGKVLLDGEDI 76
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 77 YS-PKVDTTLLR-KKVGMVFQQP----NPFpMSVYDNIAYGPRIHgirSRVKLDEIVEKSLR--DAAIFDEVKDRLKKSA 148
Cdd:PRK09473 84 LNlPEKELNKLRaEQISMIFQDPmtslNPY-MRVGEQLMEVLMLH---KGMSKAEAFEESVRmlDAVKMPEARKRMKMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 149 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISDYTAFFLVGE 226
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGICDKVLVMYAGR 239
|
250
....*....|....
gi 1391526133 227 MVEYNDTEQMFSMP 240
Cdd:PRK09473 240 TMEYGNARDVFYQP 253
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-217 |
3.03e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.87 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvPNVKiEGKVLLDGEDIYSPKVdT 83
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD----PRAT-SGRIVFDGKDITDWQT-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIhgirsrVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSrMTVEENLAMGGFF------AERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISD 217
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLAD 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-207 |
3.45e-24 |
|
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: 95.70 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVKIEGKVLLDGEDIYSPKvdttlLRKKVGMVFQqpnpfpm 102
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---GRRTGLGVSGEVLINGRPLDKRS-----FRKIIGYVPQ------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 103 svyDNIAYGprihgirsrvklDEIVEKSLRDAAifdevkdRLKksalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:cd03213 90 ---DDILHP------------TLTVRETLMFAA-------KLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 1391526133 183 PISTSKIEELMGSL-KEKYTVAIVTH 207
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIH 169
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-212 |
3.47e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNL--HYGT---NHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiEGKVLLDGEDIyspkvd 82
Cdd:COG1101 2 LELKNLSKtfNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA--GSLPPD---SGSILIDGKDV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 tTLLR-----KKVGMVFQQP--NPFP-MSVYDN--IAY--GPRiHGIRSRVKldeiveKSLRDaaifdEVKDRLKKSALG 150
Cdd:COG1101 71 -TKLPeykraKYIGRVFQDPmmGTAPsMTIEENlaLAYrrGKR-RGLRRGLT------KKRRE-----LFRELLATLGLG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 151 -----------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQA 212
Cdd:COG1101 138 lenrldtkvglLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQA 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-245 |
5.01e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 5.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIEGKVLLDGEDIYSPKVDTTL-LRKKVGMVFQQ 96
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNRRQLLpVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 P----NPfPMSVYDNIAYGPRIH-GIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEV 171
Cdd:PRK15134 371 PnsslNP-RLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE---FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKYTVA--IVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRT 245
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAylFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-214 |
7.09e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 100.20 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN-HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIysPKVDTTLL 86
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPFPMSVYDNIaygprIHGIRSRVKLDEIVEkSLRDAAIFDEVKD-------RLKKSALGLSGGQQQRL 159
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENL-----LLGAKENVSQDEIWA-ACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRI 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKyTVAIVTHNMQQATR 214
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ 674
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
7.46e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.74 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHA--LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYS 78
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM--IGIEKVK---SGEIFYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 79 PkvDTTLLRKKVGMVFQQP-NPFPMSV--YDnIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDRLKksalGLSGGQ 155
Cdd:PRK13648 76 D--NFEKLRKHIGIVFQNPdNQFVGSIvkYD-VAFGLENHAV-PYDEMHRRVSEALKQVDMLERADYEPN----ALSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRiSDYTAFFLVGEMVEYNDT 233
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
....*
gi 1391526133 234 EQMFS 238
Cdd:PRK13648 227 TEIFD 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-229 |
7.50e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.04 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 11 ENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpkVDTTLLRKK 89
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--PQ---SGRILIDGTDIRT--VTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNPFPMSVYDNIaygprihgirsRVKLDEIVEKSLRDAAIFDEVKDRLKKSALG-----------LSGGQQQR 158
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNI-----------RVGRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrqLSGGERQR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNM---QQATRIsdytAFFLVGEMVE 229
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLstvRNADRI----LVFDNGRVVE 549
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-241 |
8.38e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.85 E-value: 8.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYG-------------TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPNVkiEG 67
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKAT--DG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 68 KVLLDGEDIYS-PKVDTTLLRKKVGMVFQQP----NPfPMSVYDNIAYGPRIHgirsRVKLDEivekslrdaaifDEVKD 142
Cdd:PRK15079 77 EVAWLGKDLLGmKDDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTY----HPKLSR------------QEVKD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 143 RLKKSAL--GL------------SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--T 206
Cdd:PRK15079 140 RVKAMMLkvGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIfiA 219
|
250 260 270
....*....|....*....|....*....|....*
gi 1391526133 207 HNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK15079 220 HDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-233 |
8.41e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 95.31 E-value: 8.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 14 NLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGEDIyspkVDTTLLRKKVGMV 93
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSH----TGLAPYQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 94 FQQPNPFP-MSVYDNIAYGprihgIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVL 172
Cdd:TIGR01277 76 FQENNLFAhLTVRQNIGLG-----LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 173 LMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDT 233
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-198 |
1.21e-23 |
|
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: 99.12 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHA-LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpkVDTTL 85
Cdd:COG5265 357 EVRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD--VT---SGRILIDGQDIRD--VTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEiVEKSLRDAAIFD-----------EVKDR-LKksalgLSG 153
Cdd:COG5265 430 LRAAIGIVPQDTVLFNDTIAYNIAYG------RPDASEEE-VEAAARAAQIHDfieslpdgydtRVGERgLK-----LSG 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDpistSKIE-ELMGSLKE 198
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALD----SRTErAIQAALRE 539
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-238 |
1.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.62 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRM------NDLVPNVKIEGKVlldgediysPKV-DTTLLRKKVGMVF 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIVGDYAIPANL---------KKIkEVKRLRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 95 QQP--NPFPMSVYDNIAYGPrihgIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVL 172
Cdd:PRK13645 97 QFPeyQLFQETIEKDIAFGP----VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 173 LMDEPTSALDPISTSKIEELMGSLKEKYT--VAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-245 |
2.69e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIYS-PKVDTTLLRKKVGMVFQQP-- 97
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPya 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 --NPfPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:PRK10261 413 slDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 176 EPTSALDPISTSKIEELMGSLKEKYTVA--IVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQDKRT 245
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAylFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-240 |
2.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNhALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKvDTTL 85
Cdd:PRK13644 2 IRLENVSYSYpdGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQ---KGKVLVSGIDTGDFS-KLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNP--FPMSVYDNIAYGPRiHGIRSRVKLDEIVEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRLCIAR 163
Cdd:PRK13644 75 IRKLVGIVFQNPETqfVGRTVEEDLAFGPE-NLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKT---LSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQaTRISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
10-227 |
4.00e-23 |
|
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: 93.62 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspkvdTTLLRKK 89
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRPT---SGEIIFDGHPW------TRKDLHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSlrdaaifdEVKDRLKKSALGLSGGQQQRLCIARALAVE 168
Cdd:TIGR03740 72 IGSLIESPPLYEnLTARENLKVHTTLLGL-PDSRIDEVLNIV--------DLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 169 PEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEM 227
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-217 |
1.54e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.82 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSPKVDTTLLrkk 89
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET--PS---AGELLAGTAPLAEAREDTRLM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 vgmvFQQPNPFP-MSVYDNIAYGPRIHgirsrvkldeiveksLRDAAI--FDEV--KDRLKKSALGLSGGQQQRLCIARA 164
Cdd:PRK11247 87 ----FQDARLLPwKKVIDNVGLGLKGQ---------------WRDAALqaLAAVglADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMAD 202
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-238 |
2.53e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTTLLRKKVG 91
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 92 MVFQQPNP--FPMSVYDNIAYGPRIHGIRSrvklDEIVEKsLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEP 169
Cdd:PRK13638 81 TVFQDPEQqiFYTDIDSDIAFSLRNLGVPE----AEITRR-VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 170 EVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-249 |
3.53e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.48 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYgtnhaLKNVNMDIFKN--------KITAFIGPSGCGKSTFLKTLNRMNDL-------------------- 59
Cdd:PTZ00265 1166 IEIMDVNFRY-----ISRPNVPIYKDltfscdskKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 60 -----------VPNV------------------KIEGKVLLDGEDIyspkVDTTL--LRKKVGMVFQQPNPFPMSVYDNI 108
Cdd:PTZ00265 1241 dyqgdeeqnvgMKNVnefsltkeggsgedstvfKNSGKILLDGVDI----CDYNLkdLRNLFSIVSQEPMLFNMSIYENI 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 109 AYGpRIHGIRSRVK-------LDEIVEkSLRDAaiFDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMDEPTSAL 181
Cdd:PTZ00265 1317 KFG-KEDATREDVKrackfaaIDEFIE-SLPNK--YDTNVGPYGKS---LSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 182 DPISTSKIEELMGSLKEKYTVAIVT--HNMQQATRiSDYTAFF----LVGEMVEYNDTEQMFSMPQDKRTEDYI 249
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDKADKTIITiaHRIASIKR-SDKIVVFnnpdRTGSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-241 |
6.55e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLhYGTNHALKNVNMDIFKNKITAFIGPSGCGKStfLKTLNRMNDLVPNV-KIEGKVLLDGEdiysPKVDTTL 85
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVrQTAGRVLLDGK----PVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPfpmsvydniAYGP----RIHGI-----RSRVKLDEIVEKSLRDAAIfDEVKDRLKKSALGLSGGQQ 156
Cdd:PRK10418 77 RGRKIATIMQNPRS---------AFNPlhtmHTHARetclaLGKPADDATLTAALEAVGL-ENAARVLKLYPFEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYT--VAIVTHNMQQATRISDYTAFFLVGEMVEYNDTE 234
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
....*..
gi 1391526133 235 QMFSMPQ 241
Cdd:PRK10418 227 TLFNAPK 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-217 |
6.62e-22 |
|
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: 90.85 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDttlLRKKVGMVFQQPNP-- 99
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPT---SGEVRVAGLVPWKRRKK---FLRRIGVVFGQKTQlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 FPMSVYDNIAYGPRIHGI---RSRVKLDEIVEkslrdaaiFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDE 176
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLppaRFKKRLDELSE--------LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391526133 177 PTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALAR 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-219 |
7.76e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 37 AFIGPSGCGKSTFLktlNRMNDLVPNVKieGKVLLDGEDiyspKVDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGprIH 115
Cdd:PRK10771 29 AILGPSGAGKSTLL---NLIAGFLTPAS--GSLTLNGQD----HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLG--LN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 116 -GIR----SRVKLDEIVEK-SLrdaaifDEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI 189
Cdd:PRK10771 98 pGLKlnaaQREKLHAIARQmGI------EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190
....*....|....*....|....*....|..
gi 1391526133 190 EELMGSL--KEKYTVAIVTHNMQQATRISDYT 219
Cdd:PRK10771 169 LTLVSQVcqERQLTLLMVSHSLEDAARIAPRS 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-235 |
8.47e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 16 HYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPN---VKIEGKV--LLDgediyspkvdttllrkkV 90
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LEPTsgrVEVNGRVsaLLE-----------------L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 91 GMVFqQPNpfpMSVYDNIAYGPRIHGIRS---RVKLDEIVEKS-LRDAaiFDE-VKDrlkksalgLSGGQQQRLCIARAL 165
Cdd:COG1134 96 GAGF-HPE---LTGRENIYLNGRLLGLSRkeiDEKFDEIVEFAeLGDF--IDQpVKT--------YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 166 AVEPEVLLMDEPTSALDPI----STSKIEELMGSLKekyTVAIVTHNMQQATRISDYtAFFLV-GEMVEYNDTEQ 235
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR---TVIFVSHSMGAVRRLCDR-AIWLEkGRLVMDGDPEE 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
1.07e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 2 EKEQVTIHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIysP 79
Cdd:PRK11160 333 AADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQ---QGEILLNGQPI--A 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 KVDTTLLRKKVGMVFQQPNPFPMSVYDNIAYG------PRIHGIRSRVKLDEIVE--KSLrDAAIFDevkdrlkksaLG- 150
Cdd:PRK11160 406 DYSEAALRQAISVVSQRVHLFSATLRDNLLLAapnasdEALIEVLQQVGLEKLLEddKGL-NAWLGE----------GGr 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 151 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHN---MQQATRI 215
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRltgLEQFDRI 543
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-214 |
1.22e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 17 YGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPnvkIEGKVLLDGediyspkvdttllRKKVGMVFQQ 96
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV--LRP---TSGTVRRAG-------------GARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 ---PNPFPMSVYDNIAYG--PRIHGIRSRVKLDE-IVEKSLRDAAIfdevkDRLKKSALG-LSGGQQQRLCIARALAVEP 169
Cdd:NF040873 64 sevPDSLPLTVRDLVAMGrwARRGLWRRLTRDDRaAVDDALERVGL-----ADLAGRQLGeLSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391526133 170 EVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATR 214
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRR 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-244 |
1.22e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.95 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTflkTLNRMNDLVPnvKIEGKVLLDGEDIyspkvdtTLL 86
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDI-------SLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 ------RKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIfDEVKDRLKKSalgLSGGQQQRL 159
Cdd:PRK10895 71 plharaRRGIGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQS---LSGGERRRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
....*.
gi 1391526133 239 MPQDKR 244
Cdd:PRK10895 227 DEHVKR 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-241 |
1.26e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 37 AFIGPSGCGKS-TFLKTLnRMNDLVPNVKIEGKVLLDGEDIYspKVDTTLLRK----KVGMVFQQP----NPFpMSVYDN 107
Cdd:PRK15134 39 ALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESLL--HASEQTLRGvrgnKIAMIFQEPmvslNPL-HTLEKQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 108 IAYGPRIH-GIRSRVKLDEIVE----KSLRDAAifdevkDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:PRK15134 115 LYEVLSLHrGMRREAARGEILNcldrVGIRQAA------KRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 183 PISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK15134 189 VSVQAQILQLLRELQQELNMGLlfITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-246 |
2.70e-21 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 89.50 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNVKIEGKVLLDGE--DIYS-PKVDTT-L 85
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPDHGTATYIMRSGAelELYQlSEAERRrL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQP-NPFPMSVY--DNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIfdeVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:TIGR02323 84 MRTEWGFVHQNPrDGLRMRVSagANIGERLMAIGARHYGNIRATAQDWLEEVEI---DPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVA--IVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAviIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....*.
gi 1391526133 241 QDKRTE 246
Cdd:TIGR02323 241 QHPYTQ 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-182 |
2.85e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.06 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnRMndlvpnvkI-------EGKVLLDGEDI--YSPKvdttllRK 88
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL----RM--------VagleritSGEIWIGGRVVneLEPA------DR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQQPNPFP-MSVYDNIAYGPRIHGirsrVKLDEIvEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAV 167
Cdd:PRK11650 77 DIAMVFQNYALYPhMSVRENMAYGLKIRG----MPKAEI-EERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 1391526133 168 EPEVLLMDEPTSALD 182
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-209 |
3.96e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY-GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKIE----GKVLLDGEDIYSPK-V 81
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLI---------CGIErpsaGKIWFSGHDITRLKnR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNPF-PMSVYDNIAYGPRIHG-----IRSRVkldeivekslrdAAIFDEVK--DRLKKSALGLSG 153
Cdd:PRK10908 73 EVPFLRRQIGMIFQDHHLLmDRTVYDNVAIPLIIAGasgddIRRRV------------SAALDKVGllDKAKNFPIQLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE-KYTVAIVTHNM 209
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDI 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-227 |
4.34e-21 |
|
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: 92.38 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTflkTLNRMNDLVPnvKIEGKVLLDGEDIyspKVDTTLLRKKVGMVFQQPNPFP 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLP--PTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 -MSVYDNIAYGPRIHGiRSRVKLDEIVEKSLRDAAIfdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 180
Cdd:TIGR01257 1017 hLTVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391526133 181 LDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVGEM 227
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-242 |
5.67e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 5.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN---HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDTt 84
Cdd:PRK13650 5 IEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAE---SGQIIIDGDLLTEENVWD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 lLRKKVGMVFQQP-NPF-PMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDeVKDRlkkSALGLSGGQQQRLCIA 162
Cdd:PRK13650 79 -IRHKIGMVFQNPdNQFvGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKER---EPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATrISDYTAFFLVGEMVEYNDTEQMFSMP 240
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRG 231
|
..
gi 1391526133 241 QD 242
Cdd:PRK13650 232 ND 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-207 |
5.96e-21 |
|
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: 91.35 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKI----EGKVLLDGEDIYSpkV 81
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL---------VGVwpptAGSVRLDGADLSQ--W 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQPNPFPMSVYDNIAygpRIHGIRSrvklDEIVEkslrdAAIFDEVKD---RLKK--------SALG 150
Cdd:COG4618 400 DREELGRHIGYLPQDVELFDGTIAENIA---RFGDADP----EKVVA-----AAKLAGVHEmilRLPDgydtrigeGGAR 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 151 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE-KYTVAIVTH 207
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITH 525
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-211 |
6.14e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.44 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHVENLNL--HYGTNhALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnrmNDLVPNVKIEGKVLLDGEDIYSpkVDT 83
Cdd:PRK11174 348 VTIEAEDLEIlsPDGKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIELRE--LDP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFPMSVYDNIAYG-PRIHgirsrvklDEIVEKSLRDAAIFD-----------EVKDRlkksALGL 151
Cdd:PRK11174 419 ESWRKHLSWVGQNPQLPHGTLRDNVLLGnPDAS--------DEQLQQALENAWVSEflpllpqgldtPIGDQ----AAGL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQ 211
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-230 |
1.79e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.43 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 17 YGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEdiyspkvDTTLLRKKVGMvfqQ 96
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPD---SGTVTVRGR-------VSSLLGLGGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNpfpMSVYDNIAYGPRIHGIR---SRVKLDEIVEkslrdaaiFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 173
Cdd:cd03220 97 PE---LTGRENIYLNGRLLGLSrkeIDEKIDEIIE--------FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 174 MDEPTSALDPISTSKIEELMGSLKEKY-TVAIVTHNMQQATRISDYTAFFLVGEMVEY 230
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-246 |
1.82e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHY----GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLL---DGEDIYSPKVD 82
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVG----MVFQQP----NP-FPmsVYDNIAYGPRIHGIRSRvkldeivEKSLRDAA-IFDEVKDRLKKSALG-- 150
Cdd:PRK10261 95 AAQMRHVRGadmaMIFQEPmtslNPvFT--VGEQIAESIRLHQGASR-------EEAMVEAKrMLDQVRIPEAQTILSry 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 151 ---LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYT--VAIVTHNMQQATRISDYTAFFLVG 225
Cdd:PRK10261 166 phqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260
....*....|....*....|.
gi 1391526133 226 EMVEYNDTEQMFSMPQDKRTE 246
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTR 266
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-208 |
2.39e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 85.66 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDlvPNVKI-EGKVLLDGEDIYSPKVDTTlLRK 88
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGH--PKYEVtEGEILFKGEDITDLPPEER-ARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQQPnpfpmsvydniaygPRIHGIRsrvkldeiVEKSLRDaaiFDEvkdrlkksalGLSGGQQQRLCIARALAVE 168
Cdd:cd03217 78 GIFLAFQYP--------------PEIPGVK--------NADFLRY---VNE----------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391526133 169 PEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHN 208
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-207 |
6.82e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.17 E-value: 6.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNL-HYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKI----EGKVLLDGEDIYspK 80
Cdd:TIGR01842 316 HLSVENVTIvPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLI---------VGIwpptSGSVRLDGADLK--Q 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VDTTLLRKKVGMVFQQPNPFPMSVYDNIAYgprihgIRSRVKLDEIVEKSlrDAAIFDEVKDRLKK---SALG-----LS 152
Cdd:TIGR01842 385 WDRETFGKHIGYLPQDVELFPGTVAENIAR------FGENADPEKIIEAA--KLAGVHELILRLPDgydTVIGpggatLS 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 153 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTH 207
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITH 512
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-218 |
8.02e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNdlVPNVkieGKVLLDGEDIYSpkvDTTLLR 87
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT--HPDA---GSISLCGEPVPS---RARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRdaaiFDEVKDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:PRK13537 80 QRVGVVPQFDNLDPdFTVRENLLVFGRYFGL-SAAAARALVPPLLE----FAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 167 VEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDY 218
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLCDR 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-210 |
9.81e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 84.69 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHA-LKNVNMDIFKNKITAFIGPSGCGKSTFL-KTLNRMNdlvpnvKIEGKVLLDGEDIYSPKVDTTL 85
Cdd:cd03290 1 VQVTNGYFSWGSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVHWSNKNESEPSFEATR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKK--VGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEvKDRLKKSALGLSGGQQQRLCIAR 163
Cdd:cd03290 75 SRNRysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGD-QTEIGERGINLSGGQRQRICVAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 164 ALAVEPEVLLMDEPTSALDpISTSkiEELM--GSLK----EKYTVAIVTHNMQ 210
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALD-IHLS--DHLMqeGILKflqdDKRTLVLVTHKLQ 203
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-221 |
1.31e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.41 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENL-------NLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmNDLVPnvkiEGKVLLDGE----DI 76
Cdd:COG4778 5 LEVENLsktftlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPD----SGSILVRHDggwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 77 YS-PKVDTTLLRKK-VGMVFQQPNPFPmsvydniaygprihgirsRVKLDEIVEKSLRDAAIFDEV-KDRLKK--SALGL 151
Cdd:COG4778 80 AQaSPREILALRRRtIGYVSQFLRVIP------------------RVSALDVVAEPLLERGVDREEaRARAREllARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 ------------SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTvAIVT--HN---MQQ-AT 213
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGT-AIIGifHDeevREAvAD 220
|
....*...
gi 1391526133 214 RISDYTAF 221
Cdd:COG4778 221 RVVDVTPF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-217 |
1.50e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNVkieGKVLLDGEDIYSpkVDTTLL 86
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTPTA---GTVLVAGDDVEA--LSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPN-PFPMSVYDNIAYGPRIHgiRSRV-KLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARA 164
Cdd:PRK09536 76 SRRVASVPQDTSlSFEFDVRQVVEMGRTPH--RSRFdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE--KYTVAIVtHNMQQATRISD 217
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdgKTAVAAI-HDLDLAARYCD 207
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-216 |
1.51e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.48 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDI--YSPKVDTTLLRKKVGMVFQQPNPF 100
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT-----PTSGDVIFNGQPMskLSSAAKAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 P-MSVYDNIAYGPRIHGirsrVKLDEIVEKSLRD-AAIFDEVKDRLKKSALglSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:PRK11629 100 PdFTALENVAMPLLIGK----KKPAEINSRALEMlAAVGLEHRANHRPSEL--SGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1391526133 179 SALDPISTSKIEELMGSLKEKYTVA--IVTHNMQQATRIS 216
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAflVVTHDLQLAKRMS 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-209 |
2.06e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGT-----NHA----LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKIE----GKVLLDGE 74
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgKHQhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLL---------VGLEspsqGNVSWRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 75 DIysPKVDTT---LLRKKVGMVFQqpnpfpmsvyDNI-AYGPRiHGIRSRVK--------LDEI-----VEKSLRDAAIF 137
Cdd:PRK10419 75 PL--AKLNRAqrkAFRRDIQMVFQ----------DSIsAVNPR-KTVREIIReplrhllsLDKAerlarASEMLRAVDLD 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 138 DEVKDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVA--IVTHNM 209
Cdd:PRK10419 142 DSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAclFITHDL 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-207 |
2.47e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFK-NKItAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGediyspkvdttllRK 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDRI-GLVGRNGAGKSTLLKIL--AGELEPD---SGEVSIPK-------------GL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMVFQQPNPFP-MSVYDNIAYG-PRIHGIRSR-----VKLDEIVEKSLRDAAIFDEVKD--------RLKK--SALG- 150
Cdd:COG0488 62 RIGYLPQEPPLDDdLTVLDTVLDGdAELRALEAEleeleAKLAEPDEDLERLAELQEEFEAlggweaeaRAEEilSGLGf 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 151 -----------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTskIEELMGSLKE-KYTVAIVTH 207
Cdd:COG0488 142 peedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWLEEFLKNyPGTVLVVSH 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-218 |
2.75e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDlvPNVKI-EGKVLLDGEDIyspkvdTTLL-- 86
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGH--PKYEVtSGSILLDGEDI------LELSpd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 ---RKKVGMVFQQPNPFP-MSVYD--NIAYGPRIhgiRSRVKLDEiVEKSLRDAAifDEVKdrLKKSAL------GLSGG 154
Cdd:COG0396 73 eraRAGIFLAFQYPVEIPgVSVSNflRTALNARR---GEELSARE-FLKLLKEKM--KELG--LDEDFLdryvneGFSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 155 QQQRLCIARALAVEPEVLLMDEPTSALD----PISTSKIEELmgsLKEKYTVAIVTHNmqqaTRISDY 218
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDidalRIVAEGVNKL---RSPDRGILIITHY----QRILDY 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-207 |
2.88e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVlldgediyspKVDTTLlr 87
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPD---SGTV----------KLGETV-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 kKVGMVFQQPNPFP--MSVYDNIAYGprihgirsrvkLDEIVEKSLRD-AAIFDEVKDRLKKSALGLSGGQQQRLCIARA 164
Cdd:COG0488 379 -KIGYFDQHQEELDpdKTVLDELRDG-----------APGGTEQEVRGyLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391526133 165 LAVEPEVLLMDEPTSALDPIStskIEELMGSLKEkY--TVAIVTH 207
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET---LEALEEALDD-FpgTVLLVSH 487
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-207 |
3.13e-19 |
|
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: 81.34 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPnvkIEGKVLLDGediyspkvdttllR 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEP---DEGIVTWGS-------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGmVFQQpnpfpmsvydniaygprihgirsrvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLCIARALAV 167
Cdd:cd03221 63 VKIG-YFEQ------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELmgsLKEKY-TVAIVTH 207
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEA---LKEYPgTVILVSH 125
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-241 |
3.20e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.82 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmnDLVPNvkiEGKVLLDGEDiySPKVDT------ 83
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRD--GQLRDLyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 ---TLLRKKVGMVFQQP-NPFPMSVY--DNI-----AYGPRIHG-IR-------SRVKLDEivekslrdaaifdevkDRL 144
Cdd:PRK11701 82 errRLLRTEWGFVHQHPrDGLRMQVSagGNIgerlmAVGARHYGdIRatagdwlERVEIDA----------------ARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 145 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISDYTAFF 222
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVM 225
|
250
....*....|....*....
gi 1391526133 223 LVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQ 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-238 |
9.10e-19 |
|
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: 84.85 E-value: 9.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPnvkIEGKVLLD--------------- 72
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 73 --------GEDIYSPKVD--------TTLLRKKVGMVFQQPnpFPM----SVYDNIaygprihgIRSRVKLDEIVEKSLR 132
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDfwnlsdklRRRIRKRIAIMLQRT--FALygddTVLDNV--------LEALEEIGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 133 DAA-IFDEVK--DRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELM--GSLKEKYTVAIVTH 207
Cdd:TIGR03269 148 RAVdLIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeAVKASGISMVLTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 1391526133 208 NMQQATRISDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-214 |
1.16e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVtIHVENLNLHYGTNHA----LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDI 76
Cdd:PRK10584 1 MPAENI-VEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 77 YspKVD----TTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvkldeiveKSLRDAAIFDE---VKDRLKKSA 148
Cdd:PRK10584 75 H--QMDeearAKLRAKHVGFVFQSFMLIPtLNALENVELPALLRGESSR--------QSRNGAKALLEqlgLGKRLDHLP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 149 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATR 214
Cdd:PRK10584 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-209 |
1.59e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHAL---KNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDgeDIYSPK-VDT 83
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIIN--DSHNLKdINL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFPMSVYDNIAY------------------------------------GPRIHGIRSRVKLDEIV 127
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqenknkrnscrakcAGDLNDMSNTTDSNELI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 128 E-----KSLRDAAIFDEVKDRL----------------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 186
Cdd:PTZ00265 536 EmrknyQTIKDSEVVDVSKKVLihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260
....*....|....*....|....*
gi 1391526133 187 SKIEELMGSLK--EKYTVAIVTHNM 209
Cdd:PTZ00265 616 YLVQKTINNLKgnENRITIIIAHRL 640
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-217 |
1.69e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpk 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PD---AGKITVLGVPVPA-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 vDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGIRSRvKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRL 159
Cdd:PRK13536 108 -RARLARARIGVVPQFDNLDLeFTVRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSD----LSGGMKRRL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDPISTSKI-EELMGSLKEKYTVAIVTHNMQQATRISD 217
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCD 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-237 |
1.98e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRM--NDLVPNVKIEgkvlLDGEDIYSP--- 79
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIE----LLGRTVQREgrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 KVDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGP--RIHGIRSRVKLDEIVEK-----SLRDAAIFDEVKDRLKKsalgL 151
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNrLSVLENVLIGAlgSTPFWRTCFSWFTREQKqralqALTRVGMVHFAHQRVST----L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQATRISDYTAFFLVGEmVE 229
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGH-VF 232
|
....*...
gi 1391526133 230 YNDTEQMF 237
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-238 |
2.24e-18 |
|
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: 83.70 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHY-----GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKV-LLDGE 74
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--AGVLEPT---SGEVnVRVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 75 DIyspkVDTTLLR--------KKVGMVFQQPNPFP-MSVYDNIAygprihgirSRVKLDEIVEKSLRDAAI------FDE 139
Cdd:TIGR03269 348 EW----VDMTKPGpdgrgrakRYIGILHQEYDLYPhRTVLDNLT---------EAIGLELPDELARMKAVItlkmvgFDE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 140 VKDR--LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI-EELMGSLKE-KYTVAIVTHNMQQATRI 215
Cdd:TIGR03269 415 EKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEmEQTFIIVSHDMDFVLDV 494
|
250 260
....*....|....*....|...
gi 1391526133 216 SDYTAFFLVGEMVEYNDTEQMFS 238
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEIVE 517
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-218 |
2.84e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 20 NHALkNVNMDIFKNKITAFIGPSGCGKSTFLktlNRMNDLV-P---NVKIEGKVLLDGE-DIYSPKVdttllRKKVGMVF 94
Cdd:PRK11144 12 DLCL-TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTrPqkgRIVLNGRVLFDAEkGICLPPE-----KRRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 95 QQPNPFP-MSVYDNIAYGprihgirsrvkldeiVEKSlrDAAIFDEV------KDRLKKSALGLSGGQQQRLCIARALAV 167
Cdd:PRK11144 83 QDARLFPhYKVRGNLRYG---------------MAKS--MVAQFDKIvallgiEPLLDRYPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 168 EPEVLLMDEPTSALD-PistsKIEELM---GSLKEKYTVAI--VTHNMQQATRISDY 218
Cdd:PRK11144 146 APELLLMDEPLASLDlP----RKRELLpylERLAREINIPIlyVSHSLDEILRLADR 198
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-215 |
2.87e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSPKVD--TTLLRKKVGMVFQQPNPF 100
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDK--PT---SGTYRVAGQDVATLDADalAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 P-MSVYDNIAYgPRIH-GIRSRVKLDEIVEKSLRDAaifdeVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:PRK10535 99 ShLTAAQNVEV-PAVYaGLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391526133 179 SALDPISTskiEELMGSLKE----KYTVAIVTHNMQ---QATRI 215
Cdd:PRK10535 173 GALDSHSG---EEVMAILHQlrdrGHTVIIVTHDPQvaaQAERV 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-207 |
1.08e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSpkVDTTL 85
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLT---EGEIRLDGRPLSS--LSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNIAYG-----PRIHGIRSRVKLDEIVeKSLRDAaifdeVKDRLKKSALGLSGGQQQRLC 160
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANVTLGrdiseEQVWQALETVQLAELA-RSLPDG-----LYTPLGEQGNNLSVGQKQLLA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-217 |
1.17e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.68 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHvenlNLHY-GTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYSPKVD 82
Cdd:PRK10789 315 DVNIR----QFTYpQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TtlLRKKVGMVFQQPNPFPMSVYDNIAYGprihgiRSRVKLDEIvEKSLRDAAIFD-----------EVKDRlkksALGL 151
Cdd:PRK10789 386 S--WRSRLAVVSQTPFLFSDTVANNIALG------RPDATQQEI-EHVARLASVHDdilrlpqgydtEVGER----GVML 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISD 217
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASE 518
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-236 |
1.90e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 34 KITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIYSpkVDTTLLRKKVGMVFQQ-PNPFPMSVYDNIAYG- 111
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQP--PS---EGEILLDAQPLES--WSSKAFARKVAYLPQQlPAAEGMTVRELVAIGr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 112 -PrIHG------IRSRVKLDE-IVEKSLRDAAifdevkDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 183
Cdd:PRK10575 111 yP-WHGalgrfgAADREKVEEaISLVGLKPLA------HRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 184 ISTSKIEELMGSLKEK--YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:PRK10575 181 AHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-206 |
2.53e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVKIEGKVLLDGEdiyspKVDTTLLRKKVGMVFQQP 97
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGM-----PIDAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 NPFPM-SVYDNIAYgprihgiRSRVKLDEIVEKSLRDAAIfDEVKDR--LKKSA----------LGLSGGQQQRLCIARA 164
Cdd:TIGR00955 109 LFIPTlTVREHLMF-------QAHLRMPRRVTKKEKRERV-DEVLQAlgLRKCAntrigvpgrvKGLSGGERKRLAFASE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1391526133 165 LAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVT 206
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-254 |
3.13e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPkvDTTLLRKKVGMVFQQP---- 97
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPT---SGELLIDDHPLHFG--DYSYRSQRIRMIFQDPstsl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 NPfpmsvydniaygprihgiRSRV--------KLDEIVEKSLRDAAIFDEVK------DRLKKSALGLSGGQQQRLCIAR 163
Cdd:PRK15112 101 NP------------------RQRIsqildfplRLNTDLEPEQREKQIIETLRqvgllpDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 164 ALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSMPQ 241
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYiyVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
250
....*....|...
gi 1391526133 242 DKRTEDYITGRFG 254
Cdd:PRK15112 243 HELTKRLIAGHFG 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-254 |
8.83e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 8.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDL----VPN-VKIEGKVLLDGEDIYSpkVDTTLLRKKVGMVFQQP 97
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLtgggAPRgARVTGDVTLNGEPLAA--IDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 NP-FPMSVYDNIAYGPRIHGIRSRvkldeivEKSLRDAAIFDEVKDRLKKSALG------LSGGQQQRLCIARALA---- 166
Cdd:PRK13547 93 QPaFAFSAREIVLLGRYPHARRAG-------ALTHRDGEIAWQALALAGATALVgrdvttLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 167 -----VEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVT--HNMQQATRISDYTAFFLVGEMVEYndteqmfSM 239
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLADGAIVAH-------GA 238
|
250
....*....|....*
gi 1391526133 240 PQDKRTEDYITGRFG 254
Cdd:PRK13547 239 PADVLTPAHIARCYG 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-217 |
1.10e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIY---SPKVdttlL 86
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYK--PT---GGTILLRGQHIEglpGHQI----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 RKKVGMVFQQPNPF-PMSVYDNIAYGPR-------IHGIRSRVKLDEIVEKSLRDAAIFDEV---KDRLKKSALGLSGGQ 155
Cdd:PRK11300 79 RMGVVRTFQHVRLFrEMTVIENLLVAQHqqlktglFSGLLKTPAFRRAESEALDRAATWLERvglLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 156 QQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAI--VTHNMQQATRISD 217
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVllIEHDMKLVMGISD 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-182 |
5.10e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFlktLNRMNDLVPNvkiEGKVLLDGEDI--YSPkvdTTLLRKKVGMVFQQPNPF 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPLsdWSA---AELARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 PMSVYDNIA-YGPRIHGirsrvklDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARA-LAVEPEV------L 172
Cdd:COG4138 83 AMPVFQYLAlHQPAGAS-------SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlL 155
|
170
....*....|
gi 1391526133 173 LMDEPTSALD 182
Cdd:COG4138 156 LLDEPMNSLD 165
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-217 |
1.35e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 17 YGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIYSPKVDttlLRKKVGMVFQQ 96
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPT---SGEVRVLGYVPFKRRKE---FARRIGVVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNP--FPMSVYDNIAYGPRIHGI---RSRVKLDEIVEkslrdaaIFDeVKDRLKKSALGLSGGQQQRLCIARALAVEPEV 171
Cdd:COG4586 104 RSQlwWDLPAIDSFRLLKAIYRIpdaEYKKRLDELVE-------LLD-LGELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKY--TVAIVTHNMQQATRISD 217
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCD 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-238 |
1.43e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEdiyspKVDT 83
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-----SGKISILGQ-----PTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPN---PFPMSVYDNIAYGPRIH-GIRSRVKLdeivekslRDAAIFDEVKDR-----LKKSALG-LSG 153
Cdd:PRK15056 74 ALQKNLVAYVPQSEEvdwSFPVLVEDVVMMGRYGHmGWLRRAKK--------RDRQIVTAALARvdmveFRHRQIGeLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 154 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHNMQQATRISDYTAfFLVGEMVEYND 232
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGP 224
|
....*.
gi 1391526133 233 TEQMFS 238
Cdd:PRK15056 225 TETTFT 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-246 |
4.28e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.62 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN----HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEgKVLLDGEDI--YSPKV 81
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAE-KLEFNGQDLqrISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DTTLLRKKVGMVFQQP----NPfPMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEvKDRLKKSALGLSGGQQQ 157
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPmtslNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIV--THNMQQATRISDYTAFFLVGEMVEYNDTEQ 235
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVliTHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|.
gi 1391526133 236 MFSMPQDKRTE 246
Cdd:PRK11022 241 IFRAPRHPYTQ 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-219 |
7.92e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNvkiEGKVLLDGEDIysPKVDTTLLR 87
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PT---KGTITINNINY--NKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 K-KVGMVFQQPNPF-PMSVYDNIAYGPriHGIRSRVKLDEIVEKSLRDAA--IFDEV--KDRLKKSALGLSGGQQQRLCI 161
Cdd:PRK09700 79 QlGIGIIYQELSVIdELTVLENLYIGR--HLTKKVCGVNIIDWREMRVRAamMLLRVglKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISD-YT 219
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDrYT 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-208 |
8.04e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPNVkiEGKVLLDGEDIYSPKV--DTTLLR 87
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG---LLPPA--AGTIKLDGGDIDDPDVaeACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMvfqqpNPFpMSVYDNIAYGPRIHGIRsrvkldeivEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAV 167
Cdd:PRK13539 80 HRNAM-----KPA-LTVAENLEFWAAFLGGE---------ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKIEELM-GSLKEKYTVAIVTHN 208
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATHI 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-236 |
8.06e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.32 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 17 YGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVKIEGKVLLDGEDIYSPKVDTTLlRKKVGMVFQQ 96
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS---GVYPHGTWDGEIYWSGSPLKASNIRDTE-RAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNPFP-MSVYDNIAYGPRIHGIRSRVKLDEIVeksLRDAAIFDEVK---DRLKKSALGLSGGQQQRLCIARALAVEPEVL 172
Cdd:TIGR02633 87 LTLVPeLSVAENIFLGNEITLPGGRMAYNAMY---LRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 173 LMDEPTSALDPISTSKIEELMGSLKEKYTVAI-VTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVACVyISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-216 |
1.16e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.24 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 4 EQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmNDLVPnvKIEGKVLLDGEDIYSPKVDT 83
Cdd:NF033858 263 DEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKML---TGLLP--ASEGEAWLFGQPVDAGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 tllRKKVGMvfqqpnpfpMS----------VYDNIAYGPRIHG-----IRSRVklDEIVEKslrdaaiFD--EVKDRLkK 146
Cdd:NF033858 338 ---RRRVGY---------MSqafslygeltVRQNLELHARLFHlpaaeIAARV--AEMLER-------FDlaDVADAL-P 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 147 SALGLsgGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL--KEKYTVAIVTHNMQQAT---RIS 216
Cdd:NF033858 396 DSLPL--GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAErcdRIS 468
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-217 |
1.37e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHveNLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmndlvpnvkieGKVLLD-GEDIYSPKVDTT 84
Cdd:PRK11147 4 ISIH--GAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDdGRIIYEQDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LLrkkvgmvfQQ--PNPFPMSVYDNIAYG--------PRIHGIRSRVKLDEiVEKSLRDAAIFDEV-------------K 141
Cdd:PRK11147 70 RL--------QQdpPRNVEGTVYDFVAEGieeqaeylKRYHDISHLVETDP-SEKNLNELAKLQEQldhhnlwqlenriN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 142 DRLKKSAL-------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTskIEELMGSLKEkYTVAIV--TH----- 207
Cdd:PRK11147 141 EVLAQLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKT-FQGSIIfiSHdrsfi 216
|
250
....*....|.
gi 1391526133 208 -NMqqATRISD 217
Cdd:PRK11147 217 rNM--ATRIVD 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-178 |
1.65e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNlhygTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTL---NRmndlvpnvKIEGKVLLDGE--DIYSPKvdtT 84
Cdd:COG1129 259 VEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgaDP--------ADSGEIRLDGKpvRIRSPR---D 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LLRKKVGMV---------FQqpnpfPMSVYDNIAYG--PRI--HGIRSRVKLDEIVEKSLRDAAIfdevK-DRLKKSALG 150
Cdd:COG1129 324 AIRAGIAYVpedrkgeglVL-----DLSIRENITLAslDRLsrGGLLDRRRERALAEEYIKRLRI----KtPSPEQPVGN 394
|
170 180
....*....|....*....|....*...
gi 1391526133 151 LSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-199 |
3.08e-14 |
|
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: 68.61 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHygtnHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIySPKVDTTLLRKK 89
Cdd:cd03215 7 VRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL--FGLRPPA---SGEITLDGKPV-TRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMV---------FQQpnpfpMSVYDNIAygprihgIRSRvkldeivekslrdaaifdevkdrlkksalgLSGGQQQRLC 160
Cdd:cd03215 77 IAYVpedrkreglVLD-----LSVAENIA-------LSSL------------------------------LSGGNQQKVV 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK 199
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA 153
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-183 |
4.35e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNHAL-KNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNvkIEGKVLLdgediysPKVDTTL 85
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWPY--GSGRIAR-------PAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 lrkkvgmvF--QQPNpFPM-SVYDNIAYgPRIHGIRSrvklDEIVEKSLRDAAIfDEVKDRLKKSAL---GLSGGQQQRL 159
Cdd:COG4178 430 --------FlpQRPY-LPLgTLREALLY-PATAEAFS----DAELREALEAVGL-GHLAERLDEEADwdqVLSLGEQQRL 494
|
170 180
....*....|....*....|....
gi 1391526133 160 CIARALAVEPEVLLMDEPTSALDP 183
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDE 518
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-182 |
9.75e-14 |
|
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: 67.65 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTL-NRMNDLVpnvkIEGKVLLDGediySPKVDTtlLRKKVGMVFQQPNPFP 101
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGV----ITGEILING----RPLDKN--FQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MSVydniaygprihgirsrvkldeiVEKSLRdaaiFdevkdrlkkSAL--GLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:cd03232 93 NLT----------------------VREALR----F---------SALlrGLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
...
gi 1391526133 180 ALD 182
Cdd:cd03232 138 GLD 140
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-214 |
1.42e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKtlnrmndLVPNVKI--EGKVLLDGEDIYSPKVDTTL 85
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS-------LIAGARKiqQGRVEVLGGDMADARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMvfqqP-----NPFP-MSVYDNIAYGPRIHGirsrvkLDeiveKSLRDAAIfdevkDRLKKS----------AL 149
Cdd:NF033858 75 CPRIAYM----PqglgkNLYPtLSVFENLDFFGRLFG------QD----AAERRRRI-----DELLRAtglapfadrpAG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 150 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK---YTVAIVTHNMQQATR 214
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-238 |
1.57e-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: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN--HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLvpnvkIEGKVLLDGEDIysPKVDTTL 85
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVydniaygprihgirsRVKLD---EIVEKSLRDAAIFDEVKDRLKKSALGL----------- 151
Cdd:cd03288 93 LRSRLSIILQDPILFSGSI---------------RFNLDpecKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRiSDYTAFFLVGEMVEYN 231
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECD 236
|
....*..
gi 1391526133 232 DTEQMFS 238
Cdd:cd03288 237 TPENLLA 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-239 |
2.36e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIySPKVDTTLLRKKVGMVFQQPNPF- 100
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEI-DFKSSKEALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 PMSVYDNIAYGprihgiRSRVK---LDEivEKSLRDA-AIFDE----VKDRLKKSALGLSggQQQRLCIARALAVEPEVL 172
Cdd:PRK10982 87 QRSVMDNMWLG------RYPTKgmfVDQ--DKMYRDTkAIFDEldidIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 173 LMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYN-----DTEQMFSM 239
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIATQplaglTMDKIIAM 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-228 |
3.01e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiEGKVLLDGEDIYSPKVdTTLLRKKVGMVFQQPNPFP 101
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILS--GNYQPD---AGSILIDGQEMRFAST-TAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 -MSVYDNIAYG--PRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:PRK11288 93 eMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 179 SALdpiSTSKIEELMG---SLKEKYTVAI-VTHNMQQATRISD---------YTAFF----------LVGEMV 228
Cdd:PRK11288 169 SSL---SAREIEQLFRvirELRAEGRVILyVSHRMEEIFALCDaitvfkdgrYVATFddmaqvdrdqLVQAMV 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-214 |
3.11e-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: 69.17 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHygTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSPkvdttllrkkvg 91
Cdd:TIGR01271 433 NFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSGRISFSP------------ 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 92 mvfQQPNPFPMSVYDNIAYGPRIHGIR--SRVKLDEIVEkslrDAAIFDEvKDR--LKKSALGLSGGQQQRLCIARALAV 167
Cdd:TIGR01271 494 ---QTSWIMPGTIKDNIIFGLSYDEYRytSVIKACQLEE----DIALFPE-KDKtvLGEGGITLSGGQRARISLARAVYK 565
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391526133 168 EPEVLLMDEPTSALDPISTSKI-EELMGSLKEKYTVAIVTHNMQQATR 214
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-209 |
4.76e-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: 68.43 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndLVPNVKIEGKVLLDGEDIYSPK---VD 82
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKGSVAYVPQqawIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKlDEIVEKslrdaaifdevkdrlkksALGLSGGQQQRLCIA 162
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDR-TEIGEK------------------GVNLSGGQKQRVSLA 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEEL----MGSLKEKyTVAIVTHNM 209
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIFEHvigpEGVLKNK-TRILVTHGI 822
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-183 |
4.78e-13 |
|
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: 65.25 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHAL-KNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVKieGKvlldgedIYSPKVDTTLl 86
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLWPWGS--GR-------IGMPEGEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 87 rkkvgMVFQQPnpfpmsvydniaYGPRihGirsrvkldeivekSLRDAAIF--DEVkdrlkksalgLSGGQQQRLCIARA 164
Cdd:cd03223 68 -----FLPQRP------------YLPL--G-------------TLREQLIYpwDDV----------LSGGEQQRLAFARL 105
|
170
....*....|....*....
gi 1391526133 165 LAVEPEVLLMDEPTSALDP 183
Cdd:cd03223 106 LLHKPKFVFLDEATSALDE 124
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-240 |
2.16e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 18 GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVKIEG-KVLLDGEDI--YSPKVDTTLLRKKVGMVF 94
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTAdRFRWNGIDLlkLSPRERRKIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 95 QQPNPF--P--------MSVYDNIAYGPRI---HGIRSRvkldeIVEKSLRDAAIFDEvKDRLKKSALGLSGGQQQRLCI 161
Cdd:COG4170 96 QEPSSCldPsakigdqlIEAIPSWTFKGKWwqrFKWRKK-----RAIELLHRVGIKDH-KDIMNSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKE--KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMFSM 239
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 1391526133 240 P 240
Cdd:COG4170 250 P 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-217 |
3.86e-12 |
|
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: 63.97 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 29 DIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDI-YSPkvdttllrkkvgmvfQQPNP-FPMSVYD 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML--AGVLKPD---EGDIEIELDTVsYKP---------------QYIKAdYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 107 NIAYGPRIHGIRSRVKLDeiVEKSLRDAAIFD-EVKDrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP-- 183
Cdd:cd03237 81 LLSSITKDFYTHPYFKTE--IAKPLQIEQILDrEVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeq 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1391526133 184 --ISTSKIEELMgsLKEKYTVAIVTHNMQQATRISD 217
Cdd:cd03237 151 rlMASKVIRRFA--ENNEKTAFVVEHDIIMIDYLAD 184
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-249 |
5.13e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.44 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNH----ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvPNVKIEG-KVLLDGEDIY--SPKVD 82
Cdd:PRK15093 6 IRNLTIEFKTSDgwvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--DNWRVTAdRMRFDDIDLLrlSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLLRKKVGMVFQQP----NP-----------FPMSVYDNiAYGPRIHGIRSR-VKLdeiveksLRDAAIFDEvKDRLKK 146
Cdd:PRK15093 84 RKLVGHNVSMIFQEPqsclDPservgrqlmqnIPGWTYKG-RWWQRFGWRKRRaIEL-------LHRVGIKDH-KDAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 147 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNMQQATRISDYTAFFLV 224
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYC 234
|
250 260
....*....|....*....|....*
gi 1391526133 225 GEMVEYNDTEQMFSMPQDKRTEDYI 249
Cdd:PRK15093 235 GQTVETAPSKELVTTPHHPYTQALI 259
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-214 |
6.27e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRmndLVPNVKIEGKVLLDGEDIYSpkvDTTLLRKkvgmvFQQPNPF 100
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGR---EASLIDA-----IGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 PMSVYdniaygprihgIRSRVKLDEIVekSLRdaAIFDEvkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSA 180
Cdd:COG2401 113 KDAVE-----------LLNAVGLSDAV--LWL--RRFKE-----------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....
gi 1391526133 181 LDPiSTSKieelmgslkekytvaIVTHNMQQATR 214
Cdd:COG2401 167 LDR-QTAK---------------RVARNLQKLAR 184
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
34-215 |
6.92e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 34 KITAFIGPSGCGKSTFLktlNRMNDLVPNVKIEGKVLLDGEDIYSPkvdttlLRKKVGMVFQQPNPFP-MSVYDNIAYGP 112
Cdd:PLN03211 95 EILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQ------ILKRTGFVTQDDILYPhLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 113 RIHGIRSRVKLDEIvekSLRDAAIFDEVKDRLKKSALG------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 186
Cdd:PLN03211 166 LLRLPKSLTKQEKI---LVAESVISELGLTKCENTIIGnsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....*....
gi 1391526133 187 SKIEELMGSLKEKYTvAIVTHNMQQATRI 215
Cdd:PLN03211 243 YRLVLTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-214 |
7.56e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.72 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 12 NLNLHygTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGEDIYSPKVDTTLlrkkvg 91
Cdd:cd03291 44 NLCLV--GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSGRISFSSQFSWIM------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 92 mvfqqpnpfPMSVYDNIAYGprihgirsrVKLDEIVEKSL-------RDAAIFDEvKDR--LKKSALGLSGGQQQRLCIA 162
Cdd:cd03291 111 ---------PGTIKENIIFG---------VSYDEYRYKSVvkacqleEDITKFPE-KDNtvLGEGGITLSGGQRARISLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKI-EELMGSLKEKYTVAIVTHNMQQATR 214
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-207 |
8.68e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvPNVKI-EGKVLLDGEDIYSP 79
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH----PAYKIlEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 KVDttlLRKKVG--MVFQQPNPFP-MSVYD--NIAYGPRihgiRSRVKLDEIvekslrDAAIFDEV-KDRLKKSAL---- 149
Cdd:CHL00131 77 EPE---ERAHLGifLAFQYPIEIPgVSNADflRLAYNSK----RKFQGLPEL------DPLEFLEIiNEKLKLVGMdpsf 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391526133 150 -------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD----PISTSKIEELMGSLKekyTVAIVTH 207
Cdd:CHL00131 144 lsrnvneGFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSEN---SIILITH 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-238 |
1.05e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTN--HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIE-GKVLLDGEDIysPKVDTT 84
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI------VELErGRILIDGCDI--SKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LLRKKVGMVFQQPNPFPMSVydniaygprihgirsRVKLDEIVEKSlrDAAIFD-----EVKDRLKKSALGL-------- 151
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLFSGTV---------------RFNLDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseag 1372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 ---SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEElmgSLKEKY---TVAIVTHNMQqaTRI-SDYTAFFLV 224
Cdd:PLN03130 1373 enfSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQK---TIREEFkscTMLIIAHRLN--TIIdCDRILVLDA 1447
|
250
....*....|....
gi 1391526133 225 GEMVEYNDTEQMFS 238
Cdd:PLN03130 1448 GRVVEFDTPENLLS 1461
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-238 |
1.23e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIE-GKVLLDGEDIysPKVDT 83
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI------VELEkGRIMIDDCDV--AKFGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 84 TLLRKKVGMVFQQPNPFPMSVydniaygprihgirsRVKLDEIVEKSlrDAAIFD-----EVKDRLKKSALGL------- 151
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLFSGTV---------------RFNIDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevseg 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 ----SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEElmgSLKEKY---TVAIVTHNMQqaTRIS-DYTAFFL 223
Cdd:PLN03232 1369 genfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR---TIREEFkscTMLVIAHRLN--TIIDcDKILVLS 1443
|
250
....*....|....*
gi 1391526133 224 VGEMVEYNDTEQMFS 238
Cdd:PLN03232 1444 SGQVLEYDSPQELLS 1458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-242 |
2.46e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.43 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDIysPKVDTTL 85
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI--AKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVydniaygprihgirsRVKLDEIVEKSLRD--------------AAIFDEVKDRLKKSALGL 151
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSL---------------RMNLDPFSQYSDEEvwwalelahlktfvSALPDKLDHECAEGGENL 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQatrISDYTAFFLV--GEMVE 229
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTRVIVLdkGEVAE 1499
|
250 260
....*....|....*....|
gi 1391526133 230 YNDTEQM-------FSMPQD 242
Cdd:TIGR00957 1500 FGAPSNLlqqrgifYSMAKD 1519
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
40-186 |
3.95e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 40 GPSGCGKSTFLKTLNrmNDLVPNVKIEGKVLLDGediYSPKVDTTLLRKKVGMVFQQPNPFP-MSVYDNIAYGPRIHGir 118
Cdd:cd03233 40 GRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNG---IPYKEFAEKYPGEIIYVSEEDVHFPtLTVRETLDFALRCKG-- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 119 srvklDEIVEkslrdaaifdevkdrlkksalGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 186
Cdd:cd03233 113 -----NEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-182 |
4.43e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 35 ITAFIGPSGCGKSTFLKtlnRMNDLVPNvkiEGKVLLDGEDI--YSPkvdTTLLRKKVGMVFQQPNPFPMSVYDNIA-YG 111
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLA---RMAGLLPG---SGSIQFAGQPLeaWSA---AELARHRAYLSQQQTPPFAMPVFQYLTlHQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 112 PrihgirSRVKLDEiVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARA-LAVEPEV------LLMDEPTSALD 182
Cdd:PRK03695 95 P------DKTRTEA-VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
10-220 |
5.86e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLldgediYSPKVdttllrkK 89
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVK------WSENA-------N 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 90 VGMVFQQPNP-FP--MSVYDNIAYgprihgiRSRVKLDEIVEKSLRDAAIFDEvkDRLKKSALGLSGGQQQRLCIARALA 166
Cdd:PRK15064 384 IGYYAQDHAYdFEndLTLFDWMSQ-------WRQEGDDEQAVRGTLGRLLFSQ--DDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 167 VEPEVLLMDEPTSALDPIStskIEELMGSLkEKY--TVAIVTHNMQ----QATRISDYTA 220
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMES---IESLNMAL-EKYegTLIFVSHDREfvssLATRIIEITP 510
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-229 |
9.18e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 24 KNVNMDIFKNKITAFIGPSGCGKSTFlktlnrMNDLV-PNVKIEGKVLLDGEDIySPKVDTTLLRKKVGMVFQQPNP--- 99
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTEL------MNCLFgVDKRAGGEIRLNGKDI-SPRSPLDAVKKGMAYITESRRDngf 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 FP-MSVYDNIAYGPRIH--GIRSRVKL-DEIVEKSLRDAAifdEVKDRLKKSALG-----LSGGQQQRLCIARALAVEPE 170
Cdd:PRK09700 353 FPnFSIAQNMAISRSLKdgGYKGAMGLfHEVDEQRTAENQ---RELLALKCHSVNqniteLSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 171 VLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVE 229
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-210 |
1.11e-10 |
|
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: 60.25 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIEGKVLLDGedIYSPKVDTTL 85
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDG--VSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFPMSVYDNI-AYG----PRIHGIRSRVKLDEIVEKslrdaaIFDEVKDRLKKSALGLSGGQQQRLC 160
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLdPYGkwsdEEIWKVAEEVGLKSVIEQ------FPGQLDFVLVDGGCVLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQ 210
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-217 |
1.39e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVKIEGKVLLDGEDIYSPKV-DTTllRKKVGMVFQQ---- 96
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFEGEELQASNIrDTE--RAGIAIIHQElalv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNpfpMSVYDNIAYGPRI--HGIRSRVKLDEIVEKSLRDAAIfdEVKDRLKKSALGlsGGQQQRLCIARALAVEPEVLLM 174
Cdd:PRK13549 95 KE---LSVLENIFLGNEItpGGIMDYDAMYLRAQKLLAQLKL--DINPATPVGNLG--LGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391526133 175 DEPTSALDPISTSKIEELMGSLKEKYTVAI-VTHNMQQATRISD 217
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKAHGIACIyISHKLNEVKAISD 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
10-218 |
1.52e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNvkiEGKVLLDGEDI--YSPKVDTTllr 87
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT---GGTVEFKGKDLleLSPEDRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFPmSVYDNIAYGPRIHGIRS--------RVKLDEIVEKSLRdaaIFDEVKDRLKKSA-LGLSGGQQQR 158
Cdd:PRK09580 78 EGIFMAFQYPVEIP-GVSNQFFLQTALNAVRSyrgqepldRFDFQDLMEEKIA---LLKMPEDLLTRSVnVGFSGGEKKR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHnmqqATRISDY 218
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTH----YQRILDY 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-234 |
1.54e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTlnrMNDLVP----NVKIEGKVLLDGediyspkvdTTLLRKKVG--MVFQQ 96
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKI---IAGIVPpdsgTLEIGGNPCARL---------TPAKAHQLGiyLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 97 PNPFP-MSVYDNIAYG-PRIHGIRSRVK--LDEI-VEKSLRDAAIFDEVKDrlkksalglsggqQQRLCIARALAVEPEV 171
Cdd:PRK15439 95 PLLFPnLSVKENILFGlPKRQASMQKMKqlLAALgCQLDLDSSAGSLEVAD-------------RQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 172 LLMDEPTSALDPISTSKIEELMGSLKEKyTVAIV--THNM----QQATRIS----DYTAFFlvGEMVEYNDTE 234
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQ-GVGIVfiSHKLpeirQLADRISvmrdGTIALS--GKTADLSTDD 231
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-205 |
2.51e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 26 VNMDIFKNKITAFIGPSGCGKSTFLKTL---NRMndlvpnvkIEGKVLLDGE--DIYSPK--VDTTLL-----RKKVGMV 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRR--------TAGQVYLDGKpiDIRSPRdaIRAGIMlcpedRKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 94 fqqpnpfPM-SVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFD-EVKDRLKKSALG-LSGGQQQRLCIARALAVEPE 170
Cdd:PRK11288 344 -------PVhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSlNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMK 416
|
170 180 190
....*....|....*....|....*....|....*
gi 1391526133 171 VLLMDEPTSALDPISTSKIEELMGSLKEKyTVAIV 205
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVL 450
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-210 |
4.03e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTNHALKNVNMDIFK-NKItAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVlldgediyspKVDTTLlrk 88
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRgDKI-ALIGPNGCGKTTLLKLM--LGQLQAD---SGRI----------HCGTKL--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 89 KVGMvFQQ------PNPfpmSVYDNIAYGprihgirsrvKLDeiVEKSLRDAAIFDEVKDRL--KKSAL----GLSGGQQ 156
Cdd:PRK11147 383 EVAY-FDQhraeldPEK---TVMDNLAEG----------KQE--VMVNGRPRHVLGYLQDFLfhPKRAMtpvkALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 157 QRLCIARALAVEPEVLLMDEPTSALDpistskIE--ELMGSLKEKY--TVAIVTHNMQ 210
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLD------VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
40-195 |
4.87e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.50 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 40 GPSGCGKSTFLKTLNrmnDLVPnvKIEGKVLLDGEdiyspkvdttllrkkvGMVFQQPnpfpmSVYDNIAYGPRIHGIRS 119
Cdd:cd03231 33 GPNGSGKTTLLRILA---GLSP--PLAGRVLLNGG----------------PLDFQRD-----SIARGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 120 RVKldeiVEKSLR-------DAAIFDEVkDRLKKSALG------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 186
Cdd:cd03231 87 TLS----VLENLRfwhadhsDEQVEEAL-ARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*....
gi 1391526133 187 SKIEELMGS 195
Cdd:cd03231 162 ARFAEAMAG 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-205 |
8.62e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLnlhygTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPnvKIEGKVLLDGEDIyspKVDTTLLR 87
Cdd:PRK15439 269 LTVEDL-----TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLY---GLRP--ARGGRIMLNGKEI---NALSTAQR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVF-----QQPNPF---PMSvYDNIAYGPRIHGIRSRVKldeivekslRDAAIFDEVKDRL-------KKSALGLS 152
Cdd:PRK15439 336 LARGLVYlpedrQSSGLYldaPLA-WNVCALTHNRRGFWIKPA---------RENAVLERYRRALnikfnhaEQAARTLS 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 153 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKyTVAIV 205
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVL 457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-207 |
1.20e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlVPNVKI-EGKVLLDGEDIYSPkvdttllrkkvgmvfQQPNPFP 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSL------LSQFEIsEGRVWAERSIAYVP---------------QQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MSVYDNIAYgprihgirsrvkLDEIVEKSLRDAAIFDEVKDRLKKSALG-----------LSGGQQQRLCIARALAVEPE 170
Cdd:PTZ00243 735 ATVRGNILF------------FDEEDAARLADAVRVSQLEADLAQLGGGleteigekgvnLSGGQKARVSLARAVYANRD 802
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391526133 171 VLLMDEPTSALDPISTSKIEE--LMGSLKEKyTVAIVTH 207
Cdd:PTZ00243 803 VYLLDDPLSALDAHVGERVVEecFLGALAGK-TRVLATH 840
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
40-193 |
1.22e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.21 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 40 GPSGCGKSTFLKTLNrmnDLVPNVKieGKVLLDGEDI---------------YSPKVDTTLlrkkvgmvfqqpnpfpmSV 104
Cdd:TIGR01189 33 GPNGIGKTTLLRILA---GLLRPDS--GEVRWNGTPLaeqrdephenilylgHLPGLKPEL-----------------SA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 105 YDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAifdevkDRLkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 184
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVGLTGFE------DLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
....*....
gi 1391526133 185 STSKIEELM 193
Cdd:TIGR01189 162 GVALLAGLL 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-210 |
1.29e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHY--GTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIEGKVLLDGEDIYSPKVDTtlLR 87
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDGVSWNSVTLQT--WR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQPNPFPMSVYDNIAYGPR-----IHGIRSRVKLDEIVEKslrdaaIFDEVKDRLKKSALGLSGGQQQRLCIA 162
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNLDPYEQwsdeeIWKVAEEVGLKSVIEQ------FPDKLDFVLVDGGYVLSNGHKQLMCLA 1365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 163 RALAVEPEVLLMDEPTSALDPISTSKIEElmgSLKEKY---TVAIVTHNMQ 210
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRK---TLKQSFsncTVILSEHRVE 1413
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-207 |
1.37e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLK--TLNRMNDLVPNVKI---EGKVLLDGEDIYSPKVD 82
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQIlhvEQEVVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 -----TTLLRKKVGMVFQQPN-PFPMSV----------YDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAIFDEVK---DR 143
Cdd:PLN03073 258 tdierTQLLEEEAQLVAQQRElEFETETgkgkgankdgVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSftpEM 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391526133 144 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMgsLKEKYTVAIVTH 207
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-217 |
2.68e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDlvpnvKIEGKVLLDGEDI--YSPKVDTTllrKKVGMVFQQPNP 99
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSILYLGKEVtfNGPKSSQE---AGIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 FP-MSVYDNIAYGPRIHGIRSRVKLDEIVEKSlrdaaifDEVKDRLK-----KSALG-LSGGQQQRLCIARALAVEPEVL 172
Cdd:PRK10762 91 IPqLTIAENIFLGREFVNRFGRIDWKKMYAEA-------DKLLARLNlrfssDKLVGeLSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391526133 173 LMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHNMQQATRISD 217
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICD 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-217 |
3.38e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 6 VTIHVENLNLHYGTNHALK---NVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNvKIEGKVLLDGE--DIYSP- 79
Cdd:TIGR02633 256 VILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALF---GAYPG-KFEGNVFINGKpvDIRNPa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 ---KVDTTLL---RKKVGMVFQqpnpfpMSVYDNIAYGPrIHGIRSRVKLDEIVEKSLRDAAIfdevkDRLKKSAL---- 149
Cdd:TIGR02633 332 qaiRAGIAMVpedRKRHGIVPI------LGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAI-----QRLKVKTAspfl 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 150 ---GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISD 217
Cdd:TIGR02633 400 pigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSD 471
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-182 |
3.56e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 30 IFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiEGKVLLDGEDIYSP---KVDttllrkkvgmvfqqpnpFPMSVYD 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLA--GVLKPD---EGEVDPELKISYKPqyiKPD-----------------YDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 107 NIA-YGPRIHG------IRSRVKLDEIVEKSLRDaaifdevkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:PRK13409 420 LLRsITDDLGSsyykseIIKPLQLERLLDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
...
gi 1391526133 180 ALD 182
Cdd:PRK13409 483 HLD 485
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-217 |
3.67e-09 |
|
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: 55.34 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKST-------------FLKTL-----NRMNDL-VPNV-KIEGkvlldgediYSP- 79
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrrYVESLsayarQFLGQMdKPDVdSIEG---------LSPa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 80 -KVDTTLL----RKKVGMVfqqpnpfpMSVYDNIA--YGpRIhGIRSRVK-LDEIVEKSLrdaaifdevkdRLKKSALGL 151
Cdd:cd03270 80 iAIDQKTTsrnpRSTVGTV--------TEIYDYLRllFA-RV-GIRERLGfLVDVGLGYL-----------TLSRSAPTL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 152 SGGQQQRLCIARALAVE-PEVL-LMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHN---MQQATRISD 217
Cdd:cd03270 139 SGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDedtIRAADHVID 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-209 |
4.65e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 32 KNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiegkvLLDGEDIYSPKvdtTLLRKKVGMVFQqpNPFPMsVYDN---I 108
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILS--GELIPN-------LGDYEEEPSWD---EVLKRFRGTELQ--NYFKK-LYNGeikV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 109 AYGPR-IHGIRSRVK--LDEIVEKsLRDAAIFDEVKDRLKKSAL------GLSGGQQQRLCIARALAVEPEVLLMDEPTS 179
Cdd:PRK13409 163 VHKPQyVDLIPKVFKgkVRELLKK-VDERGKLDEVVERLGLENIldrdisELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....
gi 1391526133 180 ALD---PISTSK-IEELmgsLKEKYtVAIVTHNM 209
Cdd:PRK13409 242 YLDirqRLNVARlIREL---AEGKY-VLVVEHDL 271
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-207 |
7.02e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYSPKVDTtlLRKKVGMVFQQPNPFPM 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVC-----GGEIRVNGREIGAYGLRE--LRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 103 SVYDNIayGPRIHGIRSRV-KLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPE-VLLMDEPTSA 180
Cdd:PTZ00243 1399 TVRQNV--DPFLEASSAEVwAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATAN 1476
|
170 180
....*....|....*....|....*..
gi 1391526133 181 LDPISTSKIEELMGSLKEKYTVAIVTH 207
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAYTVITIAH 1503
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-217 |
1.31e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHVENLnlhygTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPnvKIEGKVLLDGEDIY--SPK-- 80
Cdd:PRK10762 255 EVRLKVDNL-----SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLY---GALP--RTSGYVTLDGHEVVtrSPQdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 -----VDTTLLRKKVGMVFQqpnpfpMSVYDNIAYGPRIHGIRSRVKLDEIVEKSLRDAAI--FDeVKDRLKKSALG-LS 152
Cdd:PRK10762 325 langiVYISEDRKRDGLVLG------MSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIrlFN-IKTPSMEQAIGlLS 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391526133 153 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLK-EKYTVAIVTHNMQQATRISD 217
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGMSD 463
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-217 |
1.47e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnVKIEGKVLLDgediyspKVDTTLLRKKVGMVFQQPNPF 100
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---------LYASGKARLI-------SFLPKFSRNKLIFIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 PMsvydNIAYGPrihgirsrvkldeivekslrdaaifdevkdrLKKSALGLSGGQQQRLCIARALAVEPE--VLLMDEPT 178
Cdd:cd03238 73 DV----GLGYLT-------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391526133 179 SALDPISTSK-IEELMGSLKEKYTVAIVTHN---MQQATRISD 217
Cdd:cd03238 118 TGLHQQDINQlLEVIKGLIDLGNTVILIEHNldvLSSADWIID 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-182 |
1.56e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLH-YGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndlvpnVKIE-GKVLLDGEDI--YSPKV---- 81
Cdd:COG3845 260 VENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL------RPPAsGSIRLDGEDItgLSPRErrrl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 -------DttllRKKVGMVfqqPNpfpMSVYDNIA----YGPRIHGiRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALG 150
Cdd:COG3845 334 gvayipeD----RLGRGLV---PD---MSVAENLIlgryRRPPFSR-GGFLDRKAIRAFAEELIEEFDVRTPGPDTPARS 402
|
170 180 190
....*....|....*....|....*....|..
gi 1391526133 151 LSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-216 |
1.70e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 119 SRVKLDEIVEK-SLRDAAifdevkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI-EELMGSL 196
Cdd:NF000106 121 ARARADELLERfSLTEAA---------GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMV 191
|
90 100
....*....|....*....|
gi 1391526133 197 KEKYTVAIVTHNMQQATRIS 216
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQLA 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-209 |
2.01e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLVPNvkiEGKVLLDGE-DI-YSPK---VD 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAPD---EGVIKRNGKlRIgYVPQklyLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 83 TTLlrkkvgmvfqqpnpfPMSVydniaygPRIHGIRSRVKLDEIVE--KSLRDAAIFDEvkdRLKKsalgLSGGQQQRLC 160
Cdd:PRK09544 80 TTL---------------PLTV-------NRFLRLRPGTKKEDILPalKRVQAGHLIDA---PMQK----LSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 161 IARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK--YTVAIVTHNM 209
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-207 |
2.97e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKSTFLKtlnrmndLVPNVKIEgkvlLDGEDIYSPKVdttllrkKVGMVFQQPNPF 100
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAGVDKD----FNGEARPQPGI-------KVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 P-MSVYDNIAYGprIHGIRSRVK-LDEIVEKSLRDAAIFDEVKDRLKK---------------------SAL-------- 149
Cdd:TIGR03719 81 PtKTVRENVEEG--VAEIKDALDrFNEISAKYAEPDADFDKLAAEQAElqeiidaadawdldsqleiamDALrcppwdad 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 150 --GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELmgsLKE-KYTVAIVTH 207
Cdd:TIGR03719 159 vtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH---LQEyPGTVVAVTH 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-182 |
2.97e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHY---GTNHALKNVNMDIFKNKITAFIGPSGCGK----STFLKTLNRMNDlvPNVKIEGKVlldg 73
Cdd:PLN03130 608 LEPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKtsliSAMLGELPPRSD--ASVVIRGTV---- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 74 edIYSPKVDTTllrkkvgmvfqqpnpFPMSVYDNIAYGPRIHGIRSRVKLDeiVEKSLRDAAIF-----DEVKDRlkksA 148
Cdd:PLN03130 682 --AYVPQVSWI---------------FNATVRDNILFGSPFDPERYERAID--VTALQHDLDLLpggdlTEIGER----G 738
|
170 180 190
....*....|....*....|....*....|....
gi 1391526133 149 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-182 |
6.13e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYG---TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrMNDLvpnvkiegkvlldgediySPKVDTT 84
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGEL------------------SHAETSS 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 L-LRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKLDeiVEKSLRDAAIF-----DEVKDRlkksALGLSGGQQQR 158
Cdd:PLN03232 675 VvIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAID--VTALQHDLDLLpgrdlTEIGER----GVNISGGQKQR 748
|
170 180
....*....|....*....|....
gi 1391526133 159 LCIARALAVEPEVLLMDEPTSALD 182
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALD 772
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-182 |
9.99e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 29 DIFKNKITAFIGPSGCGKSTFLKTLNrmNDLVPNvkiEGKVLLDGEDIY-----SPKVDTT---LLRKKVGmvfqqpNPF 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILA--GVLKPD---EGEVDEDLKISYkpqyiSPDYDGTveeFLRSANT------DDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 101 PMSVYDniaygpriHGIRSRVKLDEIVEKSLRDaaifdevkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSA 180
Cdd:COG1245 431 GSSYYK--------TEIIKPLGLEKLLDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
..
gi 1391526133 181 LD 182
Cdd:COG1245 486 LD 487
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-217 |
1.08e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 22 ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNrmnDLVPNVKIEGKVLLDGE-----DIYSpkvdttllRKKVGMVF-- 94
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS---GVYPHGSYEGEILFDGEvcrfkDIRD--------SEALGIVIih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 95 QQPNPFP-MSVYDNIAYGprihgirsrvklDEIVEKSLRD-AAIFDEVKDRLKK-----------SALGLsgGQQQRLCI 161
Cdd:NF040905 85 QELALIPyLSIAENIFLG------------NERAKRGVIDwNETNRRARELLAKvgldespdtlvTDIGV--GKQQLVEI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 162 ARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISD 217
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVAD 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-209 |
1.52e-07 |
|
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: 51.71 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 32 KNKITAFIGPSGCGKSTFLKTLNrmNDLVPNV-KIEGKVllDGEDIyspkvdttlLRKKVGMVFQQpnpFPMSVYDN--- 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILS--GELKPNLgDYDEEP--SWDEV---------LKRFRGTELQD---YFKKLANGeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 108 IAYGPR-IHGIRSRVK--LDEIVEKsLRDAAIFDEVKDRLK-KSALG-----LSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:COG1245 162 VAHKPQyVDLIPKVFKgtVRELLEK-VDERGKLDELAEKLGlENILDrdiseLSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*
gi 1391526133 179 SALD---PISTSK-IEELmgsLKEKYTVAIVTHNM 209
Cdd:COG1245 241 SYLDiyqRLNVARlIREL---AEEGKYVLVVEHDL 272
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-196 |
1.87e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTL-NRMNDlvpNVKIEGKVLLDGediysPKVDTTLLRKkVGMVFQQPNPFP 101
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTT---GVITGGDRLVNG-----RPLDSSFQRS-IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MS-VYDNIAYGPRIhgiR-----SRVKLDEIVEK--------SLRDAAIfdevkdrlKKSALGLSGGQQQRLCIARALAV 167
Cdd:TIGR00956 850 TStVRESLRFSAYL---RqpksvSKSEKMEYVEEvikllemeSYADAVV--------GVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190
....*....|....*....|....*....|
gi 1391526133 168 EPEVLL-MDEPTSALDPISTSKIEELMGSL 196
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-184 |
2.33e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 39 IGPSGCGKSTFLKTLN------RMNDLVpnvkIEGKVLLDGEDIYSPKvdttllrKKVGMVfqqpnpfpmsvydniaygp 112
Cdd:PRK10938 292 VGPNGAGKSTLLSLITgdhpqgYSNDLT----LFGRRRGSGETIWDIK-------KHIGYV------------------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 113 rihgiRSRVKLDEIVEKSLRDAAI---FD------EVKDRLKKSA------LG------------LSGGQQQRLCIARAL 165
Cdd:PRK10938 342 -----SSSLHLDYRVSTSVRNVILsgfFDsigiyqAVSDRQQKLAqqwldiLGidkrtadapfhsLSWGQQRLALIVRAL 416
|
170
....*....|....*....
gi 1391526133 166 AVEPEVLLMDEPTSALDPI 184
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPL 435
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-218 |
2.41e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 50.31 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKSTFL-----KTLNRMNDLV-----PNVKIEGKVLLDgediyspkvdttllrkKV 90
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKkeqpgNHDRIEGLEHID----------------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 91 GMVFQQP-------NPFP-MSVYDNI--AYGPRIHG---------IRSRVK-LDEIVEKSLRDAAIFDE----VKDRLK- 145
Cdd:cd03271 73 IVIDQSPigrtprsNPATyTGVFDEIreLFCEVCKGkrynretleVRYKGKsIADVLDMTVEEALEFFEnipkIARKLQt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 146 ------------KSALGLSGGQQQRLCIARAL---AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNM 209
Cdd:cd03271 153 lcdvglgyiklgQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNL 232
|
....*....
gi 1391526133 210 QQAtRISDY 218
Cdd:cd03271 233 DVI-KCADW 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-218 |
2.69e-07 |
|
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: 50.06 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 34 KITAFIGPSGCGKSTFLKTLNrmNDLVPNV-KIEGKVLLDG--------------EDIYSPKVDTTllrKKVGMVFQQPN 98
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILA--GKLKPNLgKFDDPPDWDEildefrgselqnyfTKLLEGDVKVI---VKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 99 PFPMSVYDNIAygpRIHgirSRVKLDEIVEKSlrdaaifdEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 178
Cdd:cd03236 102 AVKGKVGELLK---KKD---ERGKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391526133 179 SALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISDY 218
Cdd:cd03236 168 SYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDY 208
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-182 |
3.32e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpNVKIEGKVLLDGediYSPKVDTTLLRKKVGMVFQQPNPFP- 101
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGF-HIGVEGVITYDG---ITPEEIKKHYRGDVVYNAETDVHFPh 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 102 MSVYDNIAYGPRIHGIRSRVKL--DEIVEKSLRD--AAIF--DEVKDRLKKSAL--GLSGGQQQRLCIARALAVEPEVLL 173
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPDGvsREEYAKHIADvyMATYglSHTRNTKVGNDFvrGVSGGERKRVSIAEASLGGAKIQC 232
|
....*....
gi 1391526133 174 MDEPTSALD 182
Cdd:TIGR00956 233 WDNATRGLD 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-183 |
5.77e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENLNLHYGTNH-ALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVpnvkiEGKVLLDGEDIYSPKVDTtl 85
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-----SGEILLDGKPVTAEQPED-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 86 LRKKVGMVFQQPNPFpmsvydniaygPRIHGIRSRVKLDEIVEKSLRDAAIFDEVK-DRLKKSALGLSGGQQQRLCIARA 164
Cdd:PRK10522 395 YRKLFSAVFTDFHLF-----------DQLLGPEGKPANPALVEKWLERLKMAHKLElEDGRISNLKLSKGQKKRLALLLA 463
|
170
....*....|....*....
gi 1391526133 165 LAVEPEVLLMDEPTSALDP 183
Cdd:PRK10522 464 LAEERDILLLDEWAADQDP 482
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
66-205 |
6.80e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 66 EGKVLLDGE--DIYSP----KVDTTLL---RKKVGMVFQqpnpfpMSVYDNIAYgprihgirsrVKLDEIVEKSLRDAA- 135
Cdd:PRK13549 317 EGEIFIDGKpvKIRNPqqaiAQGIAMVpedRKRDGIVPV------MGVGKNITL----------AALDRFTGGSRIDDAa 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 136 ----IFDEVKdRLK-KSA------LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKyTVAI 204
Cdd:PRK13549 381 elktILESIQ-RLKvKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAI 458
|
.
gi 1391526133 205 V 205
Cdd:PRK13549 459 I 459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
140-235 |
7.84e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 140 VKDRLKKSALG-LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMGSL-KEKYTVAIVTHNMQQATRISD 217
Cdd:PRK10982 380 VKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITD 459
|
90 100
....*....|....*....|.
gi 1391526133 218 YTAFF---LVGEMVEYNDTEQ 235
Cdd:PRK10982 460 RILVMsngLVAGIVDTKTTTQ 480
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-236 |
2.84e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 20 NHALKNVNMDIFKNKITAFIGPSGCGKSTflktlnrMNDLVPNVKI--EGKVlldgeDIyspKVDTTLLRKKVGMVFQqp 97
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKST-------LSNLIAGVTMpnKGTV-----DI---KGSAALIAISSGLNGQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 npfpMSVYDNIAYGPRIHGIrSRVKLDEIVEKSLRDAAIFDEVKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEP 177
Cdd:PRK13545 100 ----LTGIENIELKGLMMGL-TKEKIKEIIPEIIEFADIGKFIYQPVKT----YSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 178 TSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQM 236
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-182 |
3.17e-06 |
|
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: 47.62 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlnRMndlvpnvkIEGKVLLDGEDIyspKVDTTLlr 87
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLF----RM--------ITGQEQPDSGTI---EIGETV-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 kKVGMVFQQ-----PNPfpmSVYDNIAYGPRI-----HGIRSRVKLDEIVEKSlrdaaifdevKDRLKKSALgLSGGQQQ 157
Cdd:TIGR03719 386 -KLAYVDQSrdaldPNK---TVWEEISGGLDIiklgkREIPSRAYVGRFNFKG----------SDQQKKVGQ-LSGGERN 450
|
170 180
....*....|....*....|....*
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALD 182
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-209 |
3.63e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 32 KNKITAFIGPSGCGKSTFLKTLnrMNDLVPNVKieGKVLLDGEDIyspkvdttllrkkvgmvfqqpnpfpmsvydniayg 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--ARELGPPGG--GVIYIDGEDI----------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 112 prihgirsrvkldeivekslRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEE 191
Cdd:smart00382 42 --------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180
....*....|....*....|....
gi 1391526133 192 ------LMGSLKEKYTVAIVTHNM 209
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTND 125
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-182 |
4.46e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 35 ITAFIGPSGCGKSTFLktlnrmnDLVPNVK----IEGKVLLDGediySPKVDTTLLRkkVGMVFQQPNpfpmsvydniay 110
Cdd:PLN03140 908 LTALMGVSGAGKTTLM-------DVLAGRKtggyIEGDIRISG----FPKKQETFAR--ISGYCEQND------------ 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 111 gprIHGIRSRVKLDEIVEKSLR--------DAAIF-DEVK-----DRLKKSALGLSG------GQQQRLCIARALAVEPE 170
Cdd:PLN03140 963 ---IHSPQVTVRESLIYSAFLRlpkevskeEKMMFvDEVMelvelDNLKDAIVGLPGvtglstEQRKRLTIAVELVANPS 1039
|
170
....*....|..
gi 1391526133 171 VLLMDEPTSALD 182
Cdd:PLN03140 1040 IIFMDEPTSGLD 1051
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-208 |
4.88e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHalknVNmdiFKNKITAFIGPSGCGKSTFL------------KTLNRMNDLVPNVKIEGKVLL---- 71
Cdd:COG0419 5 LRLENFRSYRDTET----ID---FDDGLNLIVGPNGAGKSTILeairyalygkarSRSKLRSDLINVGSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 72 ----------DGEDIYSPKVDTTLLRKKVGMVFQqpnpfpMSVYDNIaygprihgIRSRVKLDEIVEKSLRDAAIFDEVK 141
Cdd:COG0419 78 ggkryrierrQGEFAEFLEAKPSERKEALKRLLG------LEIYEEL--------KERLKELEEALESALEELAELQKLK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 142 DRL--KKSALG----LSGGQQQRLCIARALAvepevLLMDepTSALDPIStskIEELMGSLKEkytVAIVTHN 208
Cdd:COG0419 144 QEIlaQLSGLDpietLSGGERLRLALADLLS-----LILD--FGSLDEER---LERLLDALEE---LAIITHV 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-182 |
8.40e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 10 VENLNLHYGTN---HALKNVNMDIFKNKITAFIGPSGCGK-----STFLKTLNRmndlvpnvKIEGKVLLDGEDIYSPKV 81
Cdd:NF040905 260 VKNWTVYHPLHperKVVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSYGR--------NISGTVFKDGKEVDVSTV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 82 DT---------TLLRKKVGMVFQQpnpfpmSVYDNIAyGPRIHGIRSRVKLDEIVEkslrdAAIFDEVKDRLK-KS---- 147
Cdd:NF040905 332 SDaidaglayvTEDRKGYGLNLID------DIKRNIT-LANLGKVSRRGVIDENEE-----IKVAEEYRKKMNiKTpsvf 399
|
170 180 190
....*....|....*....|....*....|....*..
gi 1391526133 148 --ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:NF040905 400 qkVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-182 |
1.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 5 QVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTlnrmndlvpnvkIEGKVLLDGEDIyspKVDTT 84
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM------------ITGQEQPDSGTI---KIGET 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 85 LlrkKVGMVFQQ-----PNPfpmSVYDNIAYGprihgirsrvkLDEI-VEKSlrdaaifdEVKDRLKKSALG-------- 150
Cdd:PRK11819 387 V---KLAYVDQSrdaldPNK---TVWEEISGG-----------LDIIkVGNR--------EIPSRAYVGRFNfkggdqqk 441
|
170 180 190
....*....|....*....|....*....|....*.
gi 1391526133 151 ----LSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:PRK11819 442 kvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
152-225 |
1.38e-05 |
|
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: 46.16 E-value: 1.38e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 152 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKI-EELMGSLKEKYTVAIVTHNMQQATRISDYTAFFLVG 225
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
39-206 |
1.39e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.90 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 39 IGPSGCGKSTFLKTLNrmnDLVPnvkIEGKVLL---DGEDIYSPK---VDTTLLRKKVgmvfqqpnPFPMSVYDNIAYGP 112
Cdd:TIGR00954 484 CGPNGCGKSSLFRILG---ELWP---VYGGRLTkpaKGKLFYVPQrpyMTLGTLRDQI--------IYPDSSEDMKRRGL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 113 R---IHGIRSRVKLDEIVEKSLRdaaiFDEVKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistsKI 189
Cdd:TIGR00954 550 SdkdLEQILDNVQLTHILEREGG----WSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DV 617
|
170
....*....|....*..
gi 1391526133 190 EELMGSLKEKYTVAIVT 206
Cdd:TIGR00954 618 EGYMYRLCREFGITLFS 634
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-223 |
3.51e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.40 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 8 IHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMndLVPNvkiEGKVLLDGEDIyspKVDTTLLR 87
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--LNPE---KGEILFERQSI---KKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 88 KKVGMVFQQP--NPFpMSVYDNIAYGprIHGIRSRVKLDEIVEkslrdaaIFdEVKDRLKKSALGLSGGQQQRLCIARAL 165
Cdd:PRK13540 74 KQLCFVGHRSgiNPY-LTLRENCLYD--IHFSPGAVGITELCR-------LF-SLEHLIDYPCGLLSSGQKRQVALLRLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391526133 166 AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYTVAIVTHNMQQATRISDYTAFFL 223
Cdd:PRK13540 143 MSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-207 |
3.94e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDIFKN-KItAFIGPSGCGKSTFLKTlnrMNDLVPNvkiegkvlLDGEDIYSPKVdttllrkKVGMVFQQP--NP 99
Cdd:PRK11819 23 LKDISLSFFPGaKI-GVLGLNGAGKSTLLRI---MAGVDKE--------FEGEARPAPGI-------KVGYLPQEPqlDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 100 fPMSVYDNIAYGprIHGIRSRVK-LDEIVEKSLRDAAIFDEVKDRLKK---------------------SALG------- 150
Cdd:PRK11819 84 -EKTVRENVEEG--VAEVKAALDrFNEIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiamDALRcppwdak 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 151 ---LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTSKIEELMgslkEKY--TVAIVTH 207
Cdd:PRK11819 161 vtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-249 |
6.12e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 151 LSGGQQQRLCIARALAVEPE--VLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMQQ---ATRISDY--TAFF 222
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIIDIgpGAGI 556
|
90 100
....*....|....*....|....*..
gi 1391526133 223 LVGEMVeYNDTEQMFSMPQDKRTEDYI 249
Cdd:PRK00635 557 FGGEVL-FNGSPREFLAKSDSLTAKYL 582
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
37-205 |
7.46e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 37 AFIGPSGCGKSTFLKTLNrmNDLVpnvkiegkvLLDGEDIYSPKVDTTL----LRKKVGMVFQQPNPfpmsvyDNIAYGP 112
Cdd:PRK10938 33 AFVGANGSGKSALARALA--GELP---------LLSGERQSQFSHITRLsfeqLQKLVSDEWQRNNT------DMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 113 RIHGIRSRvkldEIVEKSLRDAAIFDEVKDRLKKSAL------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST 186
Cdd:PRK10938 96 DDTGRTTA----EIIQDEVKDPARCEQLAQQFGITALldrrfkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|
gi 1391526133 187 SKIEELMGSL-KEKYTVAIV 205
Cdd:PRK10938 172 QQLAELLASLhQSGITLVLV 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-209 |
1.02e-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: 43.08 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 143 RLKKSALGLSGGQQQRLCIARAL---AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNM 209
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL 892
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
149-208 |
1.17e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 1.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391526133 149 LGLSGGQQQRLCIARALA---VEPEVL-LMDEPTSALDPISTSKIEE-LMGSLKEKYTVAIVTHN 208
Cdd:cd03227 76 LQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEaILEHLVKGAQVIVITHL 140
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
111-217 |
1.22e-04 |
|
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: 41.79 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 111 GPRIHGIRSRVKLDEIVEKSLRDAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP---ISTS 187
Cdd:cd03222 32 GPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAA 111
|
90 100 110
....*....|....*....|....*....|.
gi 1391526133 188 K-IEELmgSLKEKYTVAIVTHNMQQATRISD 217
Cdd:cd03222 112 RaIRRL--SEEGKKTALVVEHDLAVLDYLSD 140
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-53 |
1.78e-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: 41.61 E-value: 1.78e-04
10 20
....*....|....*....|....*
gi 1391526133 29 DIFKNKITAFIGPSGCGKSTFLKTL 53
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNAL 105
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-218 |
2.02e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391526133 151 LSGGQQQRLCIARAL---AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNMqQATRISDY 218
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQgHTVVIIEHNM-HVVKVADY 880
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-182 |
2.26e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 24 KNVNMDIFKNKITAFIGPSGCGKSTFLKtlnrmndlvpnvkiegkvLLDGEdiYSPKVDTTLLRKKVGM-VFQQPNPFPM 102
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILK------------------LISGE--LQPSSGTVFRSAKVRMaVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 103 SVYDNiaygPRIHGIRSrvkLDEIVEKSLR-DAAIFDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSAL 181
Cdd:PLN03073 586 DLSSN----PLLYMMRC---FPGVPEQKLRaHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
.
gi 1391526133 182 D 182
Cdd:PLN03073 659 D 659
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-48 |
2.93e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.93e-04
10 20
....*....|....*....|....*...
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKST 48
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-207 |
3.66e-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: 40.28 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 31 FKNKITAFIGPSGCGKSTFLKTL-----------NRMNDLVPNVKIEGKVLLDGEDIYS--PKVDTTLLRKkvgmvfqqp 97
Cdd:cd03240 20 FFSPLTLIVGQNGAGKTTIIEALkyaltgelppnSKGGAHDPKLIREGEVRAQVKLAFEnaNGKKYTITRS--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 98 npfpMSVYDNIAYgprihgirsrVKLDEIvekslrDAAIFDEVKDrlkksalgLSGGQQQ------RLCIARALAVEPEV 171
Cdd:cd03240 91 ----LAILENVIF----------CHQGES------NWPLLDMRGR--------CSGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391526133 172 LLMDEPTSALDPIS-TSKIEELMGSLKEKYT--VAIVTH 207
Cdd:cd03240 143 LALDEPTTNLDEENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
31-66 |
4.02e-04 |
|
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: 39.83 E-value: 4.02e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1391526133 31 FKNKITAFIGPSGCGKSTFLktlnrmNDLVPNVKIE 66
Cdd:pfam03193 104 LKGKTTVLAGQSGVGKSTLL------NALLPELDLR 133
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1-208 |
4.38e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 1 MEKEQVTIHVENLNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPK 80
Cdd:pfam13304 99 LLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 81 VD-TTLLRKKVGMVFQQPNPFPMSVYDNIAYGPRIHGIRSRVKldeivekslrdaaIFDEVKDRLKKSALGLSGGQQQRL 159
Cdd:pfam13304 179 PDlKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGL-------------ILLENGGGGELPAFELSDGTKRLL 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391526133 160 CIARAL---AVEPEVLLMDEPTSALDPISTSKIEELMGSLKEKYT-VAIVTHN 208
Cdd:pfam13304 246 ALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-48 |
4.44e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.44e-04
10 20
....*....|....*....|....*...
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKST 48
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
28-66 |
5.07e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.57 E-value: 5.07e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1391526133 28 MDIFKNKITAFIGPSGCGKSTFLktlnrmNDLVPNVKIE 66
Cdd:PRK00098 159 KPLLAGKVTVLAGQSGVGKSTLL------NALAPDLELK 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
21-48 |
1.03e-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: 1.03e-03
10 20
....*....|....*....|....*...
gi 1391526133 21 HALKNVNMDIFKNKITAFIGPSGCGKST 48
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSS 37
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-241 |
1.27e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 19 TNHALKNVNMDIFKNKITAFIGPSGCGKSTFLktlNRMNDLVPNVkiEGKVLLDGEdiyspkvdTTLLRKKVGMVFQqpn 98
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLS---NIIGGSLSPT--VGKVDRNGE--------VSVIAISAGLSGQ--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 99 pfpMSVYDNIAYGPRIHGI-RSRVK--LDEIVEKSLRDAAIFDEVKDrlkksalgLSGGQQQRLCIARALAVEPEVLLMD 175
Cdd:PRK13546 100 ---LTGIENIEFKMLCMGFkRKEIKamTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391526133 176 EPTSALDPISTSKIEELMGSLKE-KYTVAIVTHNMQQATRISDYTAFFLVGEMVEYNDTEQMfsMPQ 241
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV--LPK 233
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
35-145 |
2.50e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 35 ITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIEGKVLLDGEDIYSPKVDTTLLRKKVGMVFQqpnpFPMSVYDNIAYGPRI 114
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFE----ISEFLEDGVRYRYGL 76
|
90 100 110
....*....|....*....|....*....|.
gi 1391526133 115 HGIRSRVKLDEIVEKSLRDAAIFDEVKDRLK 145
Cdd:pfam13304 77 DLEREDVEEKLSSKPTLLEKRLLLREDSEER 107
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-182 |
2.85e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 13 LNLHYGTNHALKNVNMDIFKNKITAFIGPSGCGKSTFLKTLnrmndlvpnvkiEGKVLLDGEDIYSPKvdttllRKKVGM 92
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL------------KNEISADGGSYTFPG------NWQLAW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 93 VFQQPNPFPMSVYDNIAYGPR-----------------------IHGirsrvKLDEIVEKSLRDAAI-------FDEvkD 142
Cdd:PRK10636 69 VNQETPALPQPALEYVIDGDReyrqleaqlhdanerndghaiatIHG-----KLDAIDAWTIRSRAAsllhglgFSN--E 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1391526133 143 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 182
Cdd:PRK10636 142 QLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
158-207 |
2.89e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 2.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 158 RLCIARALAVEPEVLLMDEPTSALDpISTskIEELMGSLKE-KYTVAIVTH 207
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INT--IRWLEDVLNErNSTMIIISH 210
|
|
| PRK12289 |
PRK12289 |
small ribosomal subunit biogenesis GTPase RsgA; |
32-69 |
6.21e-03 |
|
small ribosomal subunit biogenesis GTPase RsgA;
Pssm-ID: 237040 [Multi-domain] Cd Length: 352 Bit Score: 37.30 E-value: 6.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1391526133 32 KNKITAFIGPSGCGKSTFLktlnrmNDLVPNVKIE-GKV 69
Cdd:PRK12289 171 RNKITVVAGPSGVGKSSLI------NRLIPDVELRvGKV 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-218 |
6.41e-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: 37.69 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 113 RIHGIrsrvKLDEIVEKSLRDAAIFD------------------EVKDRLK-------------KSALGLSGGQQQRLCI 161
Cdd:TIGR00630 424 TVGGK----SIADVSELSIREAHEFFnqltltpeekkiaeevlkEIRERLGflidvgldylslsRAAGTLSGGEAQRIRL 499
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 162 ARALAVE-PEVL-LMDEPTSALDPISTSKIEELMGSLKEK-YTVAIVTHNmQQATRISDY 218
Cdd:TIGR00630 500 ATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLgNTLIVVEHD-EDTIRAADY 558
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
7-94 |
9.47e-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: 36.81 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 7 TIHVENlnlhYGtnhALKNVNMDiFKNKITAFIGPSGCGKSTFLKTLNRM--------NDLVPNVKIEGKVLLDGEDIYS 78
Cdd:pfam13175 5 SIIIKN----FR---CLKDTEID-LDEDLTVLIGKNNSGKSSILEALDIFlnnkekffEDDFLVLYLKDVIKIDKEDLNI 76
|
90
....*....|....*.
gi 1391526133 79 PKVDTTLLRKKVGMVF 94
Cdd:pfam13175 77 FENISFSIDIEIDVEF 92
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-152 |
9.57e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 36.90 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391526133 23 LKNVNMDiFKNKITAFIGPSGCGKSTFLKTLNRMNDLVPNVKIegkvllDGEDIYSPKvDTTLLRKKVGMVFQQPnpfPM 102
Cdd:COG3593 14 IKDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKF------DEEDFYLGD-DPDLPEIEIELTFGSL---LS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1391526133 103 SVYDNIAYGPRIHGIRSRV-KLDEIVEKSLRdaAIFDEVKDRLKKSALGLS 152
Cdd:COG3593 83 RLLRLLLKEEDKEELEEALeELNEELKEALK--ALNELLSEYLKELLDGLD 131
|
|
| |
