|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-260 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 515.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIY 83
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQ 163
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|....*..
gi 224511529 244 FNPKNTKTEEYISGKFG 260
Cdd:COG1117 242 TNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
13-259 |
1.06e-171 |
|
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: 473.32 E-value: 1.06e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVLEL 92
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLA 172
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTE 252
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 224511529 253 EYISGKF 259
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-242 |
3.39e-147 |
|
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: 410.42 E-value: 3.39e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVLELR 93
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLntNALSLSGGQQQRLCIARTLAI 173
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRL--HALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 174 EPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-260 |
3.40e-133 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 376.04 E-value: 3.40e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVL 90
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIART 170
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTK 250
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
250
....*....|
gi 224511529 251 TEEYISGKFG 260
Cdd:PRK14239 243 TEDYISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-260 |
3.01e-131 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 371.81 E-value: 3.01e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVL 90
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKktLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIART 170
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFF---------LNGCIEEESPTDE 241
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....*....
gi 224511529 242 LFFNPKNTKTEEYISGKFG 260
Cdd:PRK14243 246 IFNSPQQQATRDYVSGRFG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-260 |
1.25e-97 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 285.97 E-value: 1.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVLELR 93
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPF-LMSIYDNISYGPKIHG-TKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:PRK14267 85 REVGMVFQYPNPFpHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKT 251
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 224511529 252 EEYISGKFG 260
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-260 |
1.95e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 273.07 E-value: 1.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDVLELR 93
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLAI 173
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 174 EPNVILMDEPTSALDPISTGKIEELIIN--LKESYTIIIVTHNMQQAGRISDRTAFFLN-----GCIEEESPTDELFFNP 246
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 224511529 247 KNTKTEEYISGKFG 260
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-258 |
3.98e-91 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 269.48 E-value: 3.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYsnNFDVLELR 93
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPF-LMSIYDNISYGPKIHG-TKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:PRK14247 82 RRVQMVFQIPNPIpNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKT 251
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*..
gi 224511529 252 EEYISGK 258
Cdd:PRK14247 242 EKYVTGR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-260 |
4.65e-84 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 252.32 E-value: 4.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 18 NLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYsNNFDVLELRRKIG 97
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIF-NYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 98 MVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNV 177
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 178 ILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYISG 257
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
...
gi 224511529 258 KFG 260
Cdd:PRK14271 265 LSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-258 |
6.69e-77 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 233.79 E-value: 6.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYsnNFDV 89
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIA 168
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKN 248
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
250
....*....|
gi 224511529 249 TKTEEYISGK 258
Cdd:PRK14246 246 ELTEKYVIGR 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-256 |
8.53e-77 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 232.58 E-value: 8.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvEGIKiEGNVIYEGKNIYSNNFDVLEL 92
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTITVDGEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTK 250
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
....*.
gi 224511529 251 TEEYIS 256
Cdd:COG1126 232 TRAFLS 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-231 |
1.08e-62 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 194.33 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIYSNNFDVLELR 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG---LEE--PDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPF-LMSIYDNISYGpkihgtkdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIARTLA 172
Cdd:cd03229 76 RRIGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINLKES--YTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-233 |
1.12e-62 |
|
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: 195.83 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvEGIKiEGNVIYEGKNIYSNNFDVLELR 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFL-MSIYDNISYGP-KIHGtKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPiKVKG-MSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-243 |
1.51e-61 |
|
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: 193.32 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGIKI--EGNVIYEGKNIysNNFDVL 90
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-------GLLKptSGEVLVDGKDI--TKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQtpNP----FLMSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLC 166
Cdd:COG1122 72 ELRRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLG-LPREEIRERVEEALELVGLE----HLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-247 |
2.87e-60 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 198.20 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 2 VKEKDKPKNEIIIETKNLNLFYT-----DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVI 76
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG-----SIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 77 YEGKNIYS-NNFDVLELRRKIGMVFQTP----NPFlMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLn 151
Cdd:COG1123 324 FDGKDLTKlSRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRY- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 152 tnALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFL 229
Cdd:COG1123 402 --PHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMY 479
|
250
....*....|....*...
gi 224511529 230 NGCIEEESPTDELFFNPK 247
Cdd:COG1123 480 DGRIVEDGPTEEVFANPQ 497
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-243 |
5.19e-59 |
|
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: 186.94 E-value: 5.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTlnrMNDLVEgiKIEGNVIYEGKNIYSNNFDVL-EL 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLR--PDSGEVLIDGEDISGLSEAELyRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwNEVKDKLNTNalsLSGGQQQRLCIARTL 171
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAE---LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-236 |
8.63e-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: 178.47 E-value: 8.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD----FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNNFD 88
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG-----SIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLELRRK-IGMVFQTP----NPfLMSIYDNISYGPKIHGTKDKKT-LDEIVEQSLIKSALWNEVKDKLntnALSLSGGQQ 162
Cdd:cd03257 76 LRKIRRKeIQMVFQDPmsslNP-RMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRY---PHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEE 236
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-231 |
9.69e-56 |
|
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: 178.04 E-value: 9.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlveGIKIEGNVIYEGKNIYSNNfdVLEL 92
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLS--LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQtpNP---FLM-SIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIA 168
Cdd:cd03225 74 RRKVGLVFQ--NPddqFFGpTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-243 |
1.42e-55 |
|
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: 178.25 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIYSNNFDV 89
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLR--PDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 L-ELRRKIGMVFQtpNPFL---MSIYDNISYGPKIHGTKDKKTLDEIVEqsliksalwnevkDKLNTNALS--------- 156
Cdd:COG1127 77 LyELRRRIGMLFQ--GGALfdsLTVFENVAFPLREHTDLSEAEIRELVL-------------EKLELVGLPgaadkmpse 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIE 234
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
....*....
gi 224511529 235 EESPTDELF 243
Cdd:COG1127 222 AEGTPEELL 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-225 |
2.77e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.55 E-value: 2.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVLELR 93
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG-----EIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFLMSIYDNISYGPKIHGTK-DKKTLDEIVEQSLIKSALwnevkdkLNTNALSLSGGQQQRLCIARTLA 172
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDI-------LDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRT 225
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRV 201
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-255 |
8.12e-55 |
|
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: 176.72 E-value: 8.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIysNNFDVLEL 92
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINR---LIE--PTSGEIFIDGEDI--REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALwnEVKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:cd03295 74 RRKIGYVIQQIGLFpHMTVEENIALVPKLLKWP-KEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNT 249
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*.
gi 224511529 250 KTEEYI 255
Cdd:cd03295 231 FVAEFV 236
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
14-248 |
2.16e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 172.20 E-value: 2.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegikIE---GNVIYEGKNIYSnnFDV 89
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL--------IEptsGRILIDGEDIRD--LDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEqsliksalwnEVKDKLNTNALS--------L 157
Cdd:COG1125 72 VELRRRIGYVIQQiglfPH---MTVAENIATVPRLLGW-DKERIRARVD----------ELLELVGLDPEEyrdrypheL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 158 SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:COG1125 138 SGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQ 217
|
250
....*....|...
gi 224511529 236 ESPTDELFFNPKN 248
Cdd:COG1125 218 YDTPEEILANPAN 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-235 |
1.34e-50 |
|
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: 164.61 E-value: 1.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIysnnFDVLELR 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP-----DSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPF-LMSIYDNISYGPKIHGtKDKKTLDEIVEQSLiksALWnEVKDKLNTNALSLSGGQQQRLCIARTLA 172
Cdd:cd03259 72 RNIGMVFQDYALFpHLTVAENIAFGLKLRG-VPKAEIRARVRELL---ELV-GLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINLKES--YTIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-256 |
1.66e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 168.33 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYT----DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndlvegikIE----GNVIYEGKNIYS 84
Cdd:COG1135 1 MIELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------LErptsGSVLVDGVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 85 -NNFDVLELRRKIGMVFQTPNpfLMS---IYDNISYGPKIHGTkDKKTLDEIVEqSLIKsalwnEV--KDKLNTNALSLS 158
Cdd:COG1135 72 lSERELRAARRKIGMIFQHFN--LLSsrtVAENVALPLEIAGV-PKAEIRKRVA-ELLE-----LVglSDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEE 236
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|
gi 224511529 237 SPTDELFFNPKNTKTEEYIS 256
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLP 242
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-253 |
1.97e-50 |
|
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: 165.36 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY----TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNnfDV 89
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSG-----EVTFDGRPVTRR--RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTP----NPFlMSIYDNISYGPKIHGTKDKktlDEIVEQSLIKSALWNEVKDKLntnALSLSGGQQQRL 165
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRY---PHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|
gi 224511529 244 FNPKNTKTEE 253
Cdd:COG1124 228 AGPKHPYTRE 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-247 |
2.92e-50 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 164.68 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD----FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndLVEgIKIEGNVIYEGKNIYS-NNF 87
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIN----GLE-RPTSGSVLVDGTDLTLlSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTPNpfLMS---IYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQR 164
Cdd:cd03258 76 ELRKARRRIGMIFQHFN--LLSsrtVFENVALPLEIAGV-PKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLrdINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 224511529 243 FFNPK 247
Cdd:cd03258 229 FANPQ 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-231 |
3.32e-49 |
|
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: 161.50 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY----TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIkiegnVIYEGKNIY--SNNF 87
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-----VRVDGTDISklSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTPN--PFLmSIYDNISYGPKIHGTKDKKTLDEIVEqsLIKSAlwnEVKDKLNTNALSLSGGQQQRL 165
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNllPDL-TALENVELPLLLAGVPKKERRERAEE--LLERV---GLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAgRISDRTAFFLNG 231
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELA-EYADRIIELRDG 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-248 |
3.86e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNviyegkniysnnfD 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrILLDGR-------------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLEL---RRKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLiksALwneVK--DKLNTNALSLSG 159
Cdd:COG3842 69 VTGLppeKRNVGMVFQDyalfPH---LTVAENVAFGLRMRGV-PKAEIRARVAELL---EL---VGleGLADRYPHQLSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPistgKI-EELIINLKE-----SYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDA----KLrEEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
250
....*....|....*
gi 224511529 234 EEESPTDELFFNPKN 248
Cdd:COG3842 215 EQVGTPEEIYERPAT 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-242 |
1.43e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.23 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKI-EGNVIYEGKNIYSNNfdvLEL 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL------LRPtSGEVRVLGEDVARDP---AEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPFL-MSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:COG1131 72 RRRIGYVPQEPALYPdLTVRENLRFFARLYG-LPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-247 |
3.41e-48 |
|
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: 160.69 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY---TDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveG--IKIEGNVIYEGKNIYS-N 85
Cdd:TIGR04521 1 IKLKNVSYIYqpgTPFekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN-------GllKPTSGTVTIDGRDITAkK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 NFDVLELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALWNEVKDKlntNALSLSGGQQQ 163
Cdd:TIGR04521 74 KKKLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLG-LSEEEAEERVKEALELVGLDEEYLER---SPFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDE 241
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
....*.
gi 224511529 242 LFFNPK 247
Cdd:TIGR04521 230 VFSDVD 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-255 |
4.99e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.10 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvEGIKiEGNVIYEGKNIYSNNFDVLEL 92
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL----EEIT-SGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPF-LMSIYDNISYGP-KIHGTKdKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIART 170
Cdd:PRK09493 76 RQEAGMVFQQFYLFpHLTALENVMFGPlRVRGAS-KEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNT 249
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
....*.
gi 224511529 250 KTEEYI 255
Cdd:PRK09493 231 RLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-259 |
4.60e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.83 E-value: 4.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYSNNFDVLEL 92
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtIRVGDITIDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:PRK11264 84 RQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTK 250
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
....*....
gi 224511529 251 TEEYISgKF 259
Cdd:PRK11264 240 TRQFLE-KF 247
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-238 |
4.62e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFY----TDFKALNKINIKILKNSITALIGPSGCGKSTFLR---TLNRMNdlvegikiEGNVIYEGKNIY 83
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilgGLDRPT--------SGEVLIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNFDVL-ELRR-KIGMVFQTPN--PFLmSIYDNISYGPKIHGTKDKKTLDEIVEqsLIKSAlwnEVKDKLNTNALSLSG 159
Cdd:COG1136 74 SLSERELaRLRRrHIGFVFQFFNllPEL-TALENVALPLLLAGVSRKERRERARE--LLERV---GLGDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLNGCIEEES 237
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVSDE 226
|
.
gi 224511529 238 P 238
Cdd:COG1136 227 R 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-256 |
1.49e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.56 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndLVEgIKIEGNViyegkNIYSNNFD----- 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLN----LLE-TPDSGQL-----NIAGHQFDfsqkp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 ----VLELRRKIGMVFQTPN--PFLmSIYDNISYGP-KIHGTKDKKTLDEivEQSLIKSAlwnEVKDKLNTNALSLSGGQ 161
Cdd:COG4161 73 sekaIRLLRQKVGMVFQQYNlwPHL-TVMENLIEAPcKVLGLSKEQAREK--AMKLLARL---RLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESpTD 240
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DA 225
|
250
....*....|....*.
gi 224511529 241 ELFFNPKNTKTEEYIS 256
Cdd:COG4161 226 SHFTQPQTEAFAHYLS 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-224 |
5.15e-46 |
|
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: 153.40 E-value: 5.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY----TDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEG-IKI-EGNVIYEGKniysnnf 87
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLR-------IIAGlERPtSGEVLVDGE------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTPN--PFLmSIYDNISYGPKIHGTKDKKtLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRL 165
Cdd:cd03293 67 PVTGPGPDRGYVFQQDAllPWL-TVLDNVALGLELQGVPKAE-ARERAEELLELVGL----SGFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDR 224
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-247 |
7.82e-46 |
|
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: 155.60 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNL-FYTD---FKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVEGIKIEGNVIYEGKNIysNNFD 88
Cdd:COG0444 1 LLEVRNLKVyFPTRrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDL--LKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLELR----RKIGMVFQTP----NPfLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLiksalwNEVKdkLNtNALS---- 156
Cdd:COG0444 77 EKELRkirgREIQMIFQDPmtslNP-VMTVGDQIAEPLRIHGGLSKAEARERAIELL------ERVG--LP-DPERrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 157 ----LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLN 230
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYA 226
|
250
....*....|....*..
gi 224511529 231 GCIEEESPTDELFFNPK 247
Cdd:COG0444 227 GRIVEEGPVEELFENPR 243
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-224 |
1.62e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYT----DFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEG-IKI-EGNVIYEGKniy 83
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLR-------LIAGlEKPtSGEVLVDGK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 snnfDVLELRRKIGMVFQTPN--PFLmSIYDNISYGPKIHGtKDKKTLDEIVEQSLiksalwNEV--KDKLNTNALSLSG 159
Cdd:COG1116 74 ----PVTGPGPDRGVVFQEPAllPWL-TVLDNVALGLELRG-VPKAERRERARELL------ELVglAGFEDAYPHQLSG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDR 224
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLADR 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-256 |
1.65e-45 |
|
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: 152.89 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIYSnnFDVLEL 92
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-----SSGEVLLDGRDLAS--LSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPN-PFLMSIYDNISYGPKIHGT---KDKKTLDEIVEQSLiksalwnevkDKLNTNAL------SLSGGQQ 162
Cdd:COG1120 74 ARRIAYVPQEPPaPFGLTVRELVALGRYPHLGlfgRPSAEDREAVEEAL----------ERTGLEHLadrpvdELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTD 240
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|....*.
gi 224511529 241 ELFfnpkntkTEEYIS 256
Cdd:COG1120 224 EVL-------TPELLE 232
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
27-257 |
8.33e-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: 154.24 E-value: 8.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIysNNFDVLEL----RRKIGMVFQT 102
Cdd:TIGR01186 7 KGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIE--PTAGQIFIDGENI--MKQSPVELrevrRKKIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PNPF-LMSIYDNISYGPKIHGTKDKKTLDEIVEqsLIKSALWNEVKDKLNTnalSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:TIGR01186 80 FALFpHMTILQNTSLGPELLGWPEQERKEKALE--LLKLVGLEEYEHRYPD---ELSGGMQQRVGLARALAAEPDILLMD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 182 EPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYISG 257
Cdd:TIGR01186 155 EAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-248 |
9.09e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 153.76 E-value: 9.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKI--EGNVIYEGKNIYSNnfdvLE 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-------IIAGLETpdSGRIVLNGRDLFTN----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LR-RKIGMVFQtpNPFL---MSIYDNISYGPKIHGTkDKKTLDEIVEQSLiksalwNEVKdklntnaLS---------LS 158
Cdd:COG1118 72 PReRRVGFVFQ--HYALfphMTVAENIAFGLRVRPP-SKAEIRARVEELL------ELVQ-------LEgladrypsqLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEE 236
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQV 215
|
250
....*....|..
gi 224511529 237 SPTDELFFNPKN 248
Cdd:COG1118 216 GTPDEVYDRPAT 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-249 |
1.64e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.30 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI-KI-EGNVIYEGKniysnnfDVLE 91
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-------MIAGLeDPtSGEILIGGR-------DVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 L---RRKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLikSALwnEVKDKLNTNALSLSGGQQQR 164
Cdd:COG3839 70 LppkDRNIAMVFQSyalyPH---MTVYENIAFPLKLRKV-PKAEIDRRVREAA--ELL--GLEDLLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPistgKI-EELIINLKE-----SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESP 238
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDA----KLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
250
....*....|.
gi 224511529 239 TDELFFNPKNT 249
Cdd:COG3839 218 PEELYDRPANL 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-256 |
2.60e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.78 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndLVEGIKiEGNViyegkNIYSNNFD----- 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLEMPR-SGTL-----NIAGNHFDfsktp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 ----VLELRRKIGMVFQTPN--PFlMSIYDNISYGP-KIHGTKDKKTLDEIVEqsLIKSALWNEVKDKLntnALSLSGGQ 161
Cdd:PRK11124 73 sdkaIRELRRNVGMVFQQYNlwPH-LTVQQNLIEAPcRVLGLSKDQALARAEK--LLERLRLKPYADRF---PLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESpTD 240
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DA 225
|
250
....*....|....*.
gi 224511529 241 ELFFNPKNTKTEEYIS 256
Cdd:PRK11124 226 SCFTQPQTEAFKNYLS 241
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-242 |
4.04e-44 |
|
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: 158.07 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK--ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVLE 91
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG-----RILIDGIDL--RQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYG-PKIhgtkdkkTLDEIVEqSLIKSALWNEVK---DKLNT----NALSLSGGQQQ 163
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLGdPDA-------TDEEIIE-AARLAGLHDFIEalpMGYDTvvgeGGSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAgRISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-231 |
9.35e-44 |
|
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: 145.99 E-value: 9.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVLE 91
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG-----EILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNIsygpkihgtkdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIARTL 171
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAgRISDRTAFFLNG 231
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
43-259 |
1.93e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 148.02 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIY-----EGKNIYSNNFDVLELRRKIGMVFQTPNpfL---MSIYDN 113
Cdd:COG4598 38 SIIGSSGSGKSTFLRCINLLETPDSGeIRVGGEEIRlkpdrDGELVPADRRQLQRIRTRLGMVFQSFN--LwshMTVLEN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 114 ISYGPkIHGTK-DKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPIST 192
Cdd:COG4598 116 VIEAP-VHVLGrPKAEAIERAEALLAKVGLA----DKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 193 GKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYISGKF 259
Cdd:COG4598 191 GEVLKVMRDLaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-247 |
6.70e-43 |
|
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: 152.36 E-value: 6.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYT--DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndLVEGIKIEGNVIYEGKNIYSnnFD 88
Cdd:COG1123 2 TPLLEVRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLE--LS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLELRRKIGMVFQTP----NPflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQR 164
Cdd:COG1123 78 EALRGRRIGMVFQDPmtqlNP--VTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
....*
gi 224511529 243 FFNPK 247
Cdd:COG1123 231 LAAPQ 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-256 |
8.64e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.41 E-value: 8.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYT----DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYS-NNFD 88
Cdd:PRK11153 2 IELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLER-----PTSGRVLVDGQDLTAlSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLELRRKIGMVFQTPNpfLMS---IYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRL 165
Cdd:PRK11153 77 LRKARRQIGMIFQHFN--LLSsrtVFDNVALPLELAGT-PKAEIKARVTELLELVGL----SDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLkdINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|...
gi 224511529 244 FNPKNTKTEEYIS 256
Cdd:PRK11153 230 SHPKHPLTREFIQ 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-224 |
2.03e-42 |
|
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: 144.63 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVI--YEGKNIYSnnfdv 89
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsVLIDGTDInkLKGKALRQ----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 leLRRKIGMVFQTPNpfL---MSIYDNI-----SYGPKIHGTKDKKTLDEIVE--QSLIKSALwnevKDKLNTNALSLSG 159
Cdd:cd03256 76 --LRRQIGMIFQQFN--LierLSVLENVlsgrlGRRSTWRSLFGLFPKEEKQRalAALERVGL----LDKAYQRADQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDR 224
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREYADR 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-257 |
2.08e-42 |
|
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: 145.48 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNlnlfytdFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIY 83
Cdd:cd03294 22 AKGKSKEEILKKTGQ-------TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIE--PTSGKVLIDGQDIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 S-NNFDVLELRRK-IGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWNEVKDKLNtnalSL 157
Cdd:cd03294 90 AmSRKELRELRRKkISMVFQSfallPH---RTVLENVAFGLEVQGV-PRAEREERAAEALELVGLEGWEHKYPD----EL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 158 SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
250 260
....*....|....*....|..
gi 224511529 236 ESPTDELFFNPKNTKTEEYISG 257
Cdd:cd03294 242 VGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-231 |
2.61e-42 |
|
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: 141.61 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIysNNFDVLELRR 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL-----KPTSGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 KIGMVFQtpnpflmsiydnisygpkihgtkdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIARTLAIE 174
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 175 PNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-224 |
6.61e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.66 E-value: 6.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNL-FYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNNFDVL- 90
Cdd:COG3638 2 MLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSG-----EILVDGQDVTALRGRALr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNpfL---MSIYDNIsygpkIHGTkdkktLDEIveqSLIKSAL---WNEVK-------------DKLN 151
Cdd:COG3638 77 RLRRRIGMIFQQFN--LvprLSVLTNV-----LAGR-----LGRT---STWRSLLglfPPEDReralealervglaDKAY 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 152 TNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDR 224
Cdd:COG3638 142 QRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDLARRYADR 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-242 |
1.46e-41 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 141.80 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKI-EGNVIYEGKNI-YSNNFDVLe 91
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL------LPPrSGSIRFDGRDItGLPPHERA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 lRRKIGMVFQTPNPF-LMSIYDNISYGPKI-HGTKDKKTLDEIVEqsliksaLWNEVKDKLNTNALSLSGGQQQRLCIAR 169
Cdd:cd03224 74 -RAGIGYVPEGRRIFpELTVEENLLLGAYArRRAKRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 170 TLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-242 |
2.56e-41 |
|
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: 141.91 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIysNNFDVL 90
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDI--RDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSliKSA----LWNEVKDKLNT----NALSLSGGQQ 162
Cdd:cd03249 74 WLRSQIGLVSQEPVLFDGTIAENIRYG------KPDATDEEVEEAA--KKAnihdFIMSLPDGYDTlvgeRGSQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMqQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-249 |
3.66e-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: 141.22 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKI--EGNVIYEGKNIYsnnfDVLE 91
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLR-------LIAGFETptSGEILLDGKDIT----NLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCI 167
Cdd:cd03300 70 HKRPVNTVFQNyalfPH---LTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL----EGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPistgKI-EELIINLKE-----SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDE 241
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDL----KLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
....*...
gi 224511529 242 LFFNPKNT 249
Cdd:cd03300 218 IYEEPANR 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-216 |
5.50e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 5.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKI-EGNVIYEGKNIYS-NNFDV 89
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE------ERPtSGQVLVNGQDLSRlKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQT----PNpflMSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRL 165
Cdd:COG2884 75 PYLRRRIGVVFQDfrllPD---RTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQ 216
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLE 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-233 |
7.34e-41 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.30 E-value: 7.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGIKI--EGNVIYEGKNIYSNNfdvLE 91
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-------GLLKpdSGEIKVLGKDIKKEP---EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFL-MSIYDNisygpkihgtkdkktldeiveqsliksalwnevkdklntnaLSLSGGQQQRLCIART 170
Cdd:cd03230 71 VKRRIGYLPEEPSLYEnLTVREN-----------------------------------------LKLSGGMKQRLALAQA 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03230 110 LLHDPELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-257 |
1.80e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.10 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIY-----EGKNIYSNNFDVLELRRKI 96
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsIVVNGQTINlvrdkDGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 97 GMVFQTPNPF-LMSIYDNISYGP-KIHGTKdKKTLDEIVEQSLIKSALWNEVKDKLNTNalsLSGGQQQRLCIARTLAIE 174
Cdd:PRK10619 95 TMVFQHFNLWsHMTVLENVMEAPiQVLGLS-KQEARERAVKYLAKVGIDERAQGKYPVH---LSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 175 PNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEE 253
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQ 250
|
....
gi 224511529 254 YISG 257
Cdd:PRK10619 251 FLKG 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
27-242 |
5.68e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.31 E-value: 5.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGnviyegKNIysNNFDVLELRRKIGMVFQtpNP 105
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILIDG------VDI--RDLTLESLRRQIGVVPQ--DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 FL--MSIYDNISYGpkihgtKDKKTLDEiVEQSLIKSALWNEVK---DKLNT----NALSLSGGQQQRLCIARTLAIEPN 176
Cdd:COG1132 424 FLfsGTIRENIRYG------RPDATDEE-VEEAAKAAQAHEFIEalpDGYDTvvgeRGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHnmqqagRIS-----DRTAFFLNGCIEEESPTDEL 242
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-242 |
9.08e-40 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 137.81 E-value: 9.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNI-YSNNFDVL 90
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSG-----SILLEGTDItKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNpfL---MSIYDNISYG--------PKIHGT---KDKktldEIVEQSLIKSALwnevKDKLNTNALS 156
Cdd:TIGR02315 76 KLRRRIGMIFQHYN--LierLTVLENVLHGrlgykptwRSLLGRfseEDK----ERALSALERVGL----ADKAYQRADQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIE 234
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLkrINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
....*...
gi 224511529 235 EESPTDEL 242
Cdd:TIGR02315 226 FDGAPSEL 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-249 |
1.27e-38 |
|
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: 134.77 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIysNNFDVLElr 93
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER-----PDSGTILFGGEDA--TDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEQsliksalwneVKDKLNTNALS---------LSGGQQQ 163
Cdd:cd03296 74 RNVGFVFQHYALFRhMTVFDNVAFGLRVKPRSERPPEAEIRAK----------VHELLKLVQLDwladrypaqLSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDpistGKI-EELIINLKE-----SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEES 237
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALD----AKVrKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
250
....*....|..
gi 224511529 238 PTDELFFNPKNT 249
Cdd:cd03296 220 TPDEVYDHPASP 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-224 |
2.04e-38 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 134.10 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIKI--EGNVIYEGKNIysNNFDVLE 91
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-------NLISGFLRptSGSVLFDGEDI--TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 L-RRKIGMVFQTPNPFL-MSIYDNI------SYGPKIHGTKDKKTLDEIVEQslIKSALWnEVK--DKLNTNALSLSGGQ 161
Cdd:cd03219 72 IaRLGIGRTFQIPRLFPeLTVLENVmvaaqaRTGSGLLLARARREEREARER--AEELLE-RVGlaDLADRPAGELSYGQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDR 224
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADR 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-243 |
2.13e-38 |
|
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: 134.87 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD--FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYsnnfdvl 90
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkVTVDGLDTLDEENLW------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTP-NPFLMSIY-DNISYGPKIHGTKDKKtLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIA 168
Cdd:TIGR04520 74 EIRKKVGMVFQNPdNQFVGATVeDDVAFGLENLGVPREE-MRKRVDEALKLVGME----DFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPTDELF 243
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-260 |
6.93e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.91 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNviyegkniysnnf 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTPN---PFLMSIYDNISYG-------PKIHGTKDKktldEIVEQSLiksalwnevkDKLNTNAL-- 155
Cdd:COG1121 69 PPRRARRRIGYVPQRAEvdwDFPITVRDVVLMGrygrrglFRRPSRADR----EAVDEAL----------ERVGLEDLad 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 ----SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAfFLN 230
Cdd:COG1121 135 rpigELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVL-LLN 213
|
250 260 270
....*....|....*....|....*....|
gi 224511529 231 GCIEEESPTDELFfnpkntkTEEYISGKFG 260
Cdd:COG1121 214 RGLVAHGPPEEVL-------TPENLSRAYG 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-235 |
2.07e-37 |
|
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: 130.84 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIkiegNVIYEGKnIYSNNFDVLELR 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLR-------MIAGL----EEPTSGR-IYIGGRDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 ---RKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSliksALWNEVKDKLNTNALSLSGGQQQRLC 166
Cdd:cd03301 69 pkdRDIAMVFQNyalyPH---MTVYDNIAFGLKLRKV-PKDEIDERVREV----AELLQIEHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-256 |
2.57e-37 |
|
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: 131.30 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNkINIKILKNSITALIGPSGCGKSTFLRTlnrmndlvegikIEGNVIYEGKNIYSNNFDVLEL- 92
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLET------------IAGFIKPDSGKILLNGKDITNLp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 --RRKIGMVFQT----PNpflMSIYDNISYGPKiHGTKDKKTLDEIVEQslIKSALwnEVKDKLNTNALSLSGGQQQRLC 166
Cdd:cd03299 68 peKRDISYVPQNyalfPH---MTVYKNIAYGLK-KRKVDKKEIERKVLE--IAEML--GIDHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
250
....*....|..
gi 224511529 245 NPKNTKTEEYIS 256
Cdd:cd03299 220 KPKNEFVAEFLG 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-233 |
4.13e-37 |
|
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: 129.09 E-value: 4.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIysNNFDVLELRR 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-----SSGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 KIGmvfqtpnpflmsiydnisygpkihgtkdkktldeIVEQSLiksALWNeVKDKLNTNALSLSGGQQQRLCIARTLAIE 174
Cdd:cd03214 74 KIA----------------------------------YVPQAL---ELLG-LAHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 175 PNVILMDEPTSALDPisTGKIE--ELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03214 116 PPILLLDEPTSHLDI--AHQIEllELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-231 |
8.71e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.01 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEgKNIYsnnfd 88
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGREVNA-ENEK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 vlELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWnEVKDKlntNALSLSGGQQQRLC 166
Cdd:PRK13647 76 --WVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMW-DFRDK---PPYHLSYGQKKRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-255 |
1.31e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.94 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY---TDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIK-IEGNVIYEGKNIYSNNF 87
Cdd:PRK13637 3 IKIENLTHIYmegTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL------LKpTSGKIIIDGVDITDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTP--NPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKlntNALSLSGGQQQRL 165
Cdd:PRK13637 77 KLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
250
....*....|..
gi 224511529 244 fnpKNTKTEEYI 255
Cdd:PRK13637 234 ---KEVETLESI 242
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-247 |
1.43e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIYS-NNFDVLELRRKIGMVFQTP-- 103
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLR---LEE--PTSGEILFDGQDITGlSGRELRPLRRRMQMVFQDPya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 --NPfLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLiksalwnevkDK--LNTNALS-----LSGGQQQRLCIARTLAIE 174
Cdd:COG4608 107 slNP-RMTVGDIIAEPLRIHGLASKAERRERVAELL----------ELvgLRPEHADrypheFSGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 175 PNVILMDEPTSALDpIStgkIEELIINLKE------SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPK 247
Cdd:COG4608 176 PKLIVCDEPVSALD-VS---IQAQVLNLLEdlqdelGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-242 |
1.47e-36 |
|
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: 135.66 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK-ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkniysNNFDVLE 91
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsILINGVDL--------SDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGpKIHGTkdkktlDEIVEQSLIKSALWNEVK---DKLNT----NALSLSGGQQQR 164
Cdd:COG4988 409 WRRQIAWVPQNPYLFAGTIRENLRLG-RPDAS------DEELEAALEAAGLDEFVAalpDGLDTplgeGGRGLSGGQAQR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH---NMQQAGRIsdrtaFFL-NGCIEEESPTD 240
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI-----LVLdDGRIVEQGTHE 556
|
..
gi 224511529 241 EL 242
Cdd:COG4988 557 EL 558
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
1.51e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.74 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIYSNNFDV 89
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN-------GIlkPSSGRILFDGKPIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTPNP--FLMSIYDNISYGPkIHGTKDKKTLDEIVEQSLIKSALwNEVKDKlNTNALSLsgGQQQRLCI 167
Cdd:PRK13636 78 MKLRESVGMVFQDPDNqlFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI-EHLKDK-PTHCLSF--GQKKRVAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNM 215
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDI 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
29-185 |
7.01e-36 |
|
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: 125.07 E-value: 7.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSNnfDVLELRRKIGMVFQTPNPF-L 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-----PTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFpR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 108 MSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTS 185
Cdd:pfam00005 74 LTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-226 |
7.52e-36 |
|
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: 126.88 E-value: 7.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmnDLVEgiKIEGNVIYEGKNIYsnnfdvlELRR 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLK--PTSGSIRVFGKPLE-------KERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 KIGMVFQTPN---PFLMSIYDNIS---YGPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIA 168
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLmglYGHKGLFRRLSKADKAKVDEALERVGL----SELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISDRTA 226
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-242 |
8.02e-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: 127.10 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiEGNViyegkniysNNFDVL--- 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG---RATV---------AGHDVVrep 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 -ELRRKIGMVFQTPN-PFLMSIYDNISYGPKIHGTKDKKtLDEIVEQSLIKSALWnEVKDKLntnALSLSGGQQQRLCIA 168
Cdd:cd03265 69 rEVRRRIGIVFQDLSvDDELTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLL-EAADRL---VKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-231 |
4.25e-35 |
|
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: 124.92 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTflrTLNRMNDLVEgiKIEGNVIYEGKNIYSNNFDVle 91
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTT---TLKMLTGELR--PTSGTAYINGYSIRTDRKAA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 lRRKIGMVFQ-TPNPFLMSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIART 170
Cdd:cd03263 74 -RQSLGYCPQfDALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-260 |
1.46e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.52 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNiysnNFDVLELRRKIGMVFQTPNP 105
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtVTIGERVITAGKK----NKKLKPLRKKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 --FLMSIYDNISYGPKIHGTKD---KKTLDEIVEqsLIksALWNEVKDKlntNALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:PRK13634 97 qlFEETVEKDICFGPMNFGVSEedaKQKAREMIE--LV--GLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 181 DEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFN-----------PK 247
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADpdeleaigldlPE 249
|
250
....*....|...
gi 224511529 248 NTKTEEYISGKFG 260
Cdd:PRK13634 250 TVKFKRALEEKFG 262
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-248 |
4.95e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 126.37 E-value: 4.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYS-NNFDVLELRR-KIGMVFQT--- 102
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG-----EVLIDGEDITKlSKKELRELRRkKMSMVFQHfal 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 -PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSAL--WnevKDKLntnALSLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:COG4175 117 lPH---RTVLENVAFGLEIQGV-PKAERRERAREALELVGLagW---EDSY---PDELSGGMQQRVGLARALATDPDILL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 180 MDEPTSALDPIstgkI-----EELiINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKN 248
Cdd:COG4175 187 MDEAFSALDPL----IrremqDEL-LELQAKLkkTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN 257
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
14-248 |
5.89e-34 |
|
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: 125.53 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegnviyegkNIYSNNFDVLEL- 92
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAG------------TIYQGGRDITRLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 --RRKIGMVFQT----PNpflMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWNeVKDKLNTNalsLSGGQQQRLC 166
Cdd:TIGR03265 73 pqKRDYGIVFQSyalfPN---LTVADNIAYGLKNRGM-GRAEVAERVAELLDLVGLPG-SERKYPGQ---LSGGQQQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR 224
|
....
gi 224511529 245 NPKN 248
Cdd:TIGR03265 225 HPAT 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-247 |
1.36e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIYSNNFDV 89
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFN-------GIlkPTSGEVLIKGEPIKYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCI 167
Cdd:PRK13639 74 LEVRKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNP 246
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 224511529 247 K 247
Cdd:PRK13639 229 E 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-247 |
2.12e-33 |
|
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: 126.72 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 8 PKNEIIIETKNLNLFYT-----------DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKIEGNVI 76
Cdd:COG4172 270 PDAPPLLEARDLKVWFPikrglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 77 YEGKNIYSNNF-DVLELRRKIGMVFQTP----NPfLMSIYDNISYGPKIHGTK-DKKTLDEIVEQSLiksalwNEVKdkL 150
Cdd:COG4172 344 FDGQDLDGLSRrALRPLRRRMQVVFQDPfgslSP-RMTVGQIIAEGLRVHGPGlSAAERRARVAEAL------EEVG--L 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 151 NTNALS-----LSGGQQQRLCIARTLAIEPNVILMDEPTSALDpISTGK-IEELIINLKESY--TIIIVTHNMQQAGRIS 222
Cdd:COG4172 415 DPAARHrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHglAYLFISHDLAVVRALA 493
|
250 260
....*....|....*....|....*
gi 224511529 223 DRTAFFLNGCIEEESPTDELFFNPK 247
Cdd:COG4172 494 HRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-243 |
2.40e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFkALNkINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIK--IEGNVIYEGKniysnnfDVLE 91
Cdd:COG3840 2 LRLDDLTYRYGDF-PLR-FDLTIAAGERVAILGPSGAGKSTLL-------NLIAGFLppDSGRILWNGQ-------DLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 L---RRKIGMVFQTPNPFL-MSIYDNISYG--PKIHGTK-DKKTLDEIVEQ-SLIksalwnevkDKLNTNALSLSGGQQQ 163
Cdd:COG3840 66 LppaERPVSMLFQENNLFPhLTVAQNIGLGlrPGLKLTAeQRAQVEQALERvGLA---------GLLDRLPGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDE 241
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
..
gi 224511529 242 LF 243
Cdd:COG3840 217 LL 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-247 |
6.23e-33 |
|
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: 119.70 E-value: 6.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVL 90
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSG-----SIRFDGEDI--TGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 EL-RRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKD--KKTLDEIVEqsliksaLWNEVKDKLNTNALSLSGGQQQRLC 166
Cdd:COG0410 74 RIaRLGIGYVPEGRRIFpSLTVEENLLLGAYARRDRAevRADLERVYE-------LFPRLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFN 245
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
..
gi 224511529 246 PK 247
Cdd:COG0410 227 PE 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-243 |
1.73e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.73 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFK--ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGkniysnnf 87
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGMVLSEE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTP-NPFL-MSIYDNISYGPKIHGTKDkktlDEIVEQslIKSALwNEV--KDKLNTNALSLSGGQQQ 163
Cdd:PRK13635 75 TVWDVRRQVGMVFQNPdNQFVgATVQDDVAFGLENIGVPR----EEMVER--VDQAL-RQVgmEDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPIstGKIE--ELIINLKE--SYTIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPT 239
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKEqkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
....
gi 224511529 240 DELF 243
Cdd:PRK13635 225 EEIF 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-242 |
2.58e-32 |
|
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: 118.49 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkniysNNFDVLE 91
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGsILIDGQDI--------REVTLDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSliKSALWNEV----KDKLNT----NALSLSGGQQQ 163
Cdd:cd03253 73 LRRAIGVVPQDTVLFNDTIGYNIRYG------RPDATDEEVIEAA--KAAQIHDKimrfPDGYDTivgeRGLKLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-225 |
3.12e-32 |
|
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: 117.35 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVI--YEGKNIYSnnfd 88
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGqVRIAGEDVnrLRGRQLPL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 vleLRRKIGMVFQ----TPNpflMSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQR 164
Cdd:TIGR02673 77 ---LRRRIGVVFQdfrlLPD---RTVYENVALPLEVRG-KKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRT 225
Cdd:TIGR02673 146 VAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVAHRV 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
27-233 |
3.93e-32 |
|
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: 116.97 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSNnfdvlELRRKIGMVFQTPNP- 105
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAK-----ERRKSIGYVMQDVDYq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 -FLMSIYDNISYGPKIHGTKDkktldEIVEQSLIKSALWnEVKDKlntNALSLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:cd03226 84 lFTDSVREELLLGLKELDAGN-----EQAETVLKDLDLY-ALKER---HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 224511529 185 SALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03226 155 SGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
37-231 |
6.43e-32 |
|
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: 116.63 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 37 LKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGkniySNNFDVLELRRKIGMVFQT----PNpflMSIY 111
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtIVLNGTVLFDS----RKKINLPPQQRKIGLVFQQyalfPH---LNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 112 DNISYGPKIHGTKDKKTLdeiVEQSLIKSALwnevkDKL-NTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPI 190
Cdd:cd03297 94 ENLAFGLKRKRNREDRIS---VDELLDLLGL-----DHLlNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224511529 191 STGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-242 |
1.59e-31 |
|
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: 121.80 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD--FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNNFDvlE 91
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG-----SITLGGVDLRDLDED--D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTlDEIVEQSLIKSAL--W-NEVKDKLNT----NALSLSGGQQQR 164
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLA------RPDAT-DEELWAALERVGLgdWlAALPDGLDTwlgeGGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRIsDRTAFFLNGCIEEESPTDEL 242
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEEL 556
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-224 |
4.51e-31 |
|
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: 115.52 E-value: 4.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKI-EGNVIYEGKNIysNNFD 88
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF------YRPtSGRILFDGRDI--TGLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLEL-RRKIGMVFQTPNPFL-MSIYDNI-----------SYGPKIHGTKDKKTLDEIVEQSLiksALWNEVK--DKLNTN 153
Cdd:COG0411 73 PHRIaRLGIARTFQNPRLFPeLTVLENVlvaaharlgrgLLAALLRLPRARREEREARERAE---ELLERVGlaDRADEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 154 ALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES--YTIIIVTHNMQQAGRISDR 224
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADR 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-255 |
6.77e-31 |
|
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: 116.82 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEgkniysnnfdVLELRRKIGMVFQTPNPF-LMSIYDNISYGPKIH 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGsIMLDGEDVTN----------VPPHLRHINMVFQSYALFpHMTVEENVAFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 122 GTkDKKTLDEIVEQSLIKSALWNEVKDKLNtnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIIN 201
Cdd:TIGR01187 71 KV-PRAEIKPRVLEALRLVQLEEFADRKPH----QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 202 LKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYI 255
Cdd:TIGR01187 146 IQEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-242 |
1.52e-30 |
|
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: 115.18 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIK-IEGNVIYEGkniysnnFDVL----ELRRKIG 97
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL------LRpTSGTARVAG-------YDVVreprKVRRSIG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 98 MVFQTPNPFL-MSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALWNEVKDKLNTnalsLSGGQQQRLCIARTLAIEPN 176
Cdd:TIGR01188 70 IVPQYASVDEdLTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR01188 145 VLFLDEPTTGLDPRTRRAIWDYIRALKEEgVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-247 |
1.58e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.93 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYT-----DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkNIYSNNF 87
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGtITIAGYHI----TPETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTKDKKTLDEIVEQsLIKSALWNEVKDKlntNALSLSGGQQQRL 165
Cdd:PRK13641 79 NLKKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNG-CIEEESPtDELF 243
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGkLIKHASP-KEIF 233
|
....
gi 224511529 244 FNPK 247
Cdd:PRK13641 234 SDKE 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-215 |
2.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY---TDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNI--YSNN 86
Cdd:PRK13649 3 INLQNVSYTYqagTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLItsTSKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 87 FDVLELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALWNEVKDKlntNALSLSGGQQQR 164
Cdd:PRK13649 78 KDIKQIRKKVGLVFQFPESqlFEETVLKDVAFGPQNFGVS-QEEAEALAREKLALVGISESLFEK---NPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNM 215
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLM 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-246 |
5.28e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.80 E-value: 5.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKniysnnfDVLE 91
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLehQTSGHIRFHGT-------DVSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LR---RKIGMVFQTPNPFL-MSIYDNISYG---------PKIHGTKDKKT-LDEIVEQSLIKsalwnevkdklNTNALSL 157
Cdd:PRK10851 69 LHardRKVGFVFQHYALFRhMTVFDNIAFGltvlprrerPNAAAIKAKVTqLLEMVQLAHLA-----------DRYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 158 SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES--YTIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
250
....*....|.
gi 224511529 236 ESPTDELFFNP 246
Cdd:PRK10851 218 AGTPDQVWREP 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
27-218 |
8.97e-30 |
|
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: 110.59 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIYSNNFDVLELRRKIGMVFQTPN 104
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN-------GLlrPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 105 P--FLMSIYDNISYGPKIHGTKDKKtLDEIVEQSLIKSALwnevkDKLNTNALS-LSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:TIGR01166 79 DqlFAADVDQDVAFGPLNLGLSEAE-VERRVREALTAVGA-----SGLRERPTHcLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 224511529 182 EPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQA 218
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-242 |
1.44e-29 |
|
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: 111.17 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEgkniysnnFDVL 90
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrILIDGHDVRD--------YTLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSLIKSA--LWNEVKDKLNT----NALSLSGGQQQR 164
Cdd:cd03251 73 SLRRQIGLVSQDVFLFNDTVAENIAYG------RPGATREEVEEAARAANAheFIMELPEGYDTvigeRGVKLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHnmqqagRIS-----DRTAFFLNGCIEEESPT 239
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH------RLStienaDRIVVLEDGKIVERGTH 220
|
...
gi 224511529 240 DEL 242
Cdd:cd03251 221 EEL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-246 |
1.55e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.20 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYT-DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIYSNNfdV 89
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN-------GIlkPTSGSVLIRGEPITKEN--I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwNEVKDKLNTNalsLSGGQQQRLCI 167
Cdd:PRK13652 74 REVRKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFN 245
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
.
gi 224511529 246 P 246
Cdd:PRK13652 229 P 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-225 |
1.68e-29 |
|
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: 110.19 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY-TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVI--YEGKNIysnnfdv 89
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtIRVNGQDVsdLRGRAI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQT----PNpflMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRL 165
Cdd:cd03292 74 PYLRRKIGVVFQDfrllPD---RNVYENVAFALEVTGVP-PREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INlKESYTIIIVTHNMQQAGRISDRT 225
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkIN-KAGTTVVVATHAKELVDTTRHRV 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-246 |
1.87e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.02 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNLFYTD-----FKALNKINIKILKNSITALIGPSGCGKSTFLRTLN-----RMNDL-VEGIKIEGNVIY 77
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIqVGDIYIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 78 EGKNIYSN-----NFDvlELRRKIGMVFQTP--NPFLMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALwneVKDKL 150
Cdd:PRK13631 97 HELITNPYskkikNFK--ELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGL---DDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 151 NTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISDRTAFFL 229
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*..
gi 224511529 230 NGCIEEESPTDELFFNP 246
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQ 267
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-247 |
2.58e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.28 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYEGKNIYSNNFDvle 91
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDVTHRSIQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 lRRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKDkktlDEIVEQsliksalwneVKDKLNTNALS---------LSGGQ 161
Cdd:PRK11432 77 -QRDICMVFQSYALFpHMSLGENVGYGLKMLGVPK----EERKQR----------VKEALELVDLAgfedryvdqISGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPT 239
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
....*...
gi 224511529 240 DELFFNPK 247
Cdd:PRK11432 222 QELYRQPA 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-218 |
2.80e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.38 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKA--LNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKI--EGNVIYEGKNIYSN 85
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIGIEKvkSGEIFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 NFDvlELRRKIGMVFQTP-NPFLMSI--YDnISYGPKIHGTKDKKtLDEIVEQSLIKSalwnEVKDKLNTNALSLSGGQQ 162
Cdd:PRK13648 77 NFE--KLRKHIGIVFQNPdNQFVGSIvkYD-VAFGLENHAVPYDE-MHRRVSEALKQV----DMLERADYEPNALSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQA 218
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-223 |
6.25e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 6.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIYSnnFDVLEL 92
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-----TPQSGTVFLGDKPISM--LSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQT-PNPFLMSIYDNISYGPKIH-------GTKDKktldEIVEQSLIKSALwNEVKDKLNTnalSLSGGQQQR 164
Cdd:PRK11231 75 ARRLALLPQHhLTPEGITVRELVAYGRSPWlslwgrlSAEDN----ARVNQAMEQTRI-NHLADRRLT---DLSGGQRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISD 223
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCD 206
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-243 |
9.79e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 9.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIkiegnVIYEGKNIYSNNfdV 89
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK-----VKIDGELLTAEN--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTP-NPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwnevkDKLNTNALSLSGGQQQRLCI 167
Cdd:PRK13642 77 WNLRRKIGMVFQNPdNQFVgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPTDELF 243
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-218 |
1.68e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.31 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 7 KPKNEIIIETKNLNLFYTDFK--ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkniy 83
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeIKIDGITI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 sNNFDVLELRRKIGMVFQTP-NPFL-MSIYDNISYG---PKIHGTKDKKTLDEIVEQSLIKSALWNEvkdklntnALSLS 158
Cdd:PRK13632 74 -SKENLKEIRKKIGIIFQNPdNQFIgATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE--------PQNLS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQA 218
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEA 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-257 |
1.81e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDfkalnkINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEGIKieGNVIYEGKNIYS-NNFDV 89
Cdd:PRK10070 32 EQILEKTGLSLGVKD------ASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDIAKiSDAEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRK-IGMVFQT----PNpflMSIYDNISYGPKIHGT----KDKKTLDEIVEQSLIKSAlwNEVKDKLntnalslSGG 160
Cdd:PRK10070 101 REVRRKkIAMVFQSfalmPH---MTVLDNTAFGMELAGInaeeRREKALDALRQVGLENYA--HSYPDEL-------SGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESP 238
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
250
....*....|....*....
gi 224511529 239 TDELFFNPKNTKTEEYISG 257
Cdd:PRK10070 249 PDEILNNPANDYVRTFFRG 267
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
17-221 |
2.40e-28 |
|
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: 106.93 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYSNNFdvleLRRK 95
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGqVYLNGQETPPLNSKKASKF----RREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 IGMVFQtpNPFLM---SIYDNISYGPKIHgTKDKKTLDEIVEQSLIKSALWNevkdKLNTNALSLSGGQQQRLCIARTLA 172
Cdd:TIGR03608 78 LGYLFQ--NFALIeneTVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALARAIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNM---QQAGRI 221
Cdd:TIGR03608 151 KPPPLILADEPTGSLDPKNRDEVLDLLLELnDEGKTIIIVTHDPevaKQADRV 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-224 |
3.27e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIysnNFDVl 90
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL-------GIlaPDSGEVLWDGEPL---DPED- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 elRRKIGmvfqtpnpFL---------MSIYDNISYGPKIHG---TKDKKTLDEIVEQsliksaLwnEVKDKLNTNALSLS 158
Cdd:COG4152 70 --RRRIG--------YLpeerglypkMKVGEQLVYLARLKGlskAEAKRRADEWLER------L--GLGDRANKKVEELS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDR 224
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDR 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-248 |
7.00e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.65 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKI--EGNVIYEGKNIYsnnfDVL 90
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGFETpdSGRIMLDGQDIT----HVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPF-LMSIYDNISYGPKIhgtkdKKT-LDEIVEQsliksalwneVKDKL---------NTNALSLSG 159
Cdd:PRK09452 83 AENRHVNTVFQSYALFpHMTVFENVAFGLRM-----QKTpAAEITPR----------VMEALrmvqleefaQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDpistGKI-EELIINLKE-----SYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALD----YKLrKQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
250
....*....|....*
gi 224511529 234 EEESPTDELFFNPKN 248
Cdd:PRK09452 224 EQDGTPREIYEEPKN 238
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
41-221 |
8.32e-28 |
|
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: 106.40 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGPKi 120
Cdd:cd03248 42 VTALVGPSGSGKSTVVALLENFYQPQGG-----QVLLDGKPI--SQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQ- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 121 hgtkdKKTLDEIVEQ----------SLIKSALWNEVKDKLNtnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPI 190
Cdd:cd03248 114 -----SCSFECVKEAaqkahahsfiSELASGYDTEVGEKGS----QLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190
....*....|....*....|....*....|....
gi 224511529 191 STGKIEELIINLKESYTIIIVTHNM---QQAGRI 221
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLstvERADQI 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-224 |
8.53e-28 |
|
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: 104.43 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNIYSNNfdVLE 91
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLykPDSGEILVDGKEVSFAS--PRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 -LRRKIGMVFQtpnpflmsiydnisygpkihgtkdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIART 170
Cdd:cd03216 72 aRRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDR 224
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-243 |
1.48e-27 |
|
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: 105.77 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK-ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkniysNNFDVLE 91
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqILIDGIDI--------RDISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSLIKSA------LWNEVKDKLNTNALSLSGGQQQRL 165
Cdd:cd03254 75 LRSMIGVVLQDTFLFSGTIMENIRLG------RPNATDEEVIEAAKEAGAhdfimkLPNGYDTVLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAgRISDRTAFFLNGCIEEESPTDELF 243
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-243 |
1.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.74 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKI--EGNVIYEGKNIYSNNf 87
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDGLLEaeSGQIIIDGDLLTEEN- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 dVLELRRKIGMVFQTP-NPFL-MSIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwNEVKDKlntNALSLSGGQQQRL 165
Cdd:PRK13650 76 -VWDIRHKIGMVFQNPdNQFVgATVEDDVAFGLENKGI-PHEEMKERVNEALELVGM-QDFKER---EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPisTGKIE--ELIINLKESY--TIIIVTHNMQQAGrISDRTAFFLNGCIEEESPTDE 241
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
..
gi 224511529 242 LF 243
Cdd:PRK13650 227 LF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-218 |
1.77e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.81 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFK--ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndLVEGIKIEGNVIYEGKNIYSNNfdVL 90
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKT--VW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTP-NPFL-MSIYDNISYGPKIHGTKDKKTLdEIVEQSLiksalwNEVK--DKLNTNALSLSGGQQQRLC 166
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFVgATVGDDVAFGLENRAVPRPEMI-KIVRDVL------ADVGmlDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQA 218
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEA 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-239 |
1.97e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.38 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIYsnnfDVLEL 92
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE-----QPTAGQIMLDGVDLS----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPF-LMSIYDNISYGPKihgtKDKKTLDEI---VEQSLIKSALWNEVKDKLNtnalSLSGGQQQRLCIA 168
Cdd:PRK11607 90 QRPINMMFQSYALFpHMTVEQNIAFGLK----QDKLPKAEIasrVNEMLGLVHMQEFAKRKPH----QLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHN----MQQAGRIS--DRTAFFLNGCIEE--ESP 238
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDqeeaMTMAGRIAimNRGKFVQIGEPEEiyEHP 241
|
.
gi 224511529 239 T 239
Cdd:PRK11607 242 T 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-233 |
2.02e-27 |
|
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: 104.98 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIysNNFDVLE 91
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY-----KPTSGSVLLDGTDI--RQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGPKIHgtKDKKTLdEIVEQSLIkSALWNEVKDKLNT----NALSLSGGQQQRLCI 167
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLGAPLA--DDERIL-RAAELAGV-TDFVNKHPNGLDLqigeRGRGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMqQAGRISDRTAFFLNGCI 233
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-250 |
3.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFK------ALNKINIKILKNSITALIGPSGCGKSTFLRtlnRMNDLVegIKIEGNVIYEGKNIy 83
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAK---HMNALL--IPSEGKVYVDGLDT- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNFDVLELRRKIGMVFQTP-NPFLMSIYD-NISYGPKIHGTKDKKtLDEIVEQSLIKSALWnEVKDKlntNALSLSGGQ 161
Cdd:PRK13633 75 SDEENLWDIRNKAGMVFQNPdNQIVATIVEeDVAFGPENLGIPPEE-IRERVDESLKKVGMY-EYRRH---APHLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPT 239
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
250
....*....|.
gi 224511529 240 DELFFNPKNTK 250
Cdd:PRK13633 229 KEIFKEVEMMK 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-240 |
5.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 105.59 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKniySNNFDVLELRRKIGMVFQTPNP- 105
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSST---SKQKEIKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 -FLMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALWNEVKDKlntNALSLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:PRK13643 97 lFEETVLKDVAFGPQNFGIP-KEKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 185 SALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG-CIEEESPTD 240
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGhIISCGTPSD 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-242 |
5.39e-27 |
|
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: 104.14 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKIE-GNVIYEGKNIysnnfDVLE-- 91
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGL------LPVKsGSIRLDGEDI-----TKLPph 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 --LRRKIGMVFQTPNPF-LMSIYDNISYGPKIHGTKDKKTLDEIVEqsliksaLWNEVKDKLNTNALSLSGGQQQRLCIA 168
Cdd:TIGR03410 71 erARAGIAYVPQGREIFpRLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES--YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-233 |
6.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY-----TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGiKIEGNVIYEGKNIYSNNFD 88
Cdd:PRK13651 3 IKVKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG-TIEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VL------------------ELRRKIGMVFQTP--NPFLMSIYDNISYGPKIHGTKDKKTLDEIVEqsLIKSALWNEvkD 148
Cdd:PRK13651 82 KVleklviqktrfkkikkikEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK--YIELVGLDE--S 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 149 KLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAF 227
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*.
gi 224511529 228 FLNGCI 233
Cdd:PRK13651 238 FKDGKI 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-213 |
6.58e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.95 E-value: 6.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 1 MVKEKDKPKNEII-----IETKNLNLFYT--DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikieg 73
Cdd:PRK11176 324 LEQEKDEGKRVIErakgdIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG----- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 74 NVIYEGKNIysNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGpkihgTKDKKTLDEIVEQSLIKSAL--WNEVKDKLN 151
Cdd:PRK11176 399 EILLDGHDL--RDYTLASLRNQVALVSQNVHLFNDTIANNIAYA-----RTEQYSREQIEEAARMAYAMdfINKMDNGLD 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 152 T----NALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:PRK11176 472 TvigeNGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-245 |
7.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.48 E-value: 7.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 25 DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRM------NDLVEGIKIEGNViyegKNIYsnnfDVLELRRKIGM 98
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIVGDYAIPANL----KKIK----EVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 99 VFQTP--NPFLMSIYDNISYGPkIHGTKDKKTLDEIVEQSLiksALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPN 176
Cdd:PRK13645 95 VFQFPeyQLFQETIEKDIAFGP-VNLGENKQEAYKKVPELL---KLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKESYT--IIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFN 245
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-247 |
7.77e-27 |
|
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: 108.23 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNL-FYTD---FKALNKINIKILKNSITALIGPSGCGKS-TFLRTLNRMNDlvEGIKIEGNVIYEGKNIys 84
Cdd:COG4172 3 SMPLLSVEDLSVaFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPD--PAAHPSGSILFDGQDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 85 NNFDVLELRR----KIGMVFQTP----NPfLMSIYDNISYGPKIH-GTKDKKTLDEIVEqsliksaLWNEV-----KDKL 150
Cdd:COG4172 79 LGLSERELRRirgnRIAMIFQEPmtslNP-LHTIGKQIAEVLRLHrGLSGAAARARALE-------LLERVgipdpERRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 151 NTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFF 228
Cdd:COG4172 151 DAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVM 230
|
250
....*....|....*....
gi 224511529 229 LNGCIEEESPTDELFFNPK 247
Cdd:COG4172 231 RQGEIVEQGPTAELFAAPQ 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-256 |
1.15e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.40 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 19 LNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIYSNNFDVLE-LRRKIG 97
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR---LVE--SQGGEIIFNGQRIDTLSPGKLQaLRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 98 MVFQTPNPFL---MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEvkdklntNAL----SLSGGQQQRLCIART 170
Cdd:PRK10261 405 FIFQDPYASLdprQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPE-------HAWryphEFSGGQRQRICIARA 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKN 248
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
....*...
gi 224511529 249 TKTEEYIS 256
Cdd:PRK10261 558 PYTRKLMA 565
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-213 |
1.49e-26 |
|
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: 102.66 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIkILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNiysnnfdvlEL 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGtIRIDGQDVLKQPQ---------KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKtLDEIVEQSLIKSALWNEVKDKLNtnalSLSGGQQQRLCIARTL 171
Cdd:cd03264 71 RRRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-213 |
1.53e-26 |
|
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: 107.37 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEgkniysnnFDVLE 91
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsIAVNGVPLAD--------ADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISygpkiHGTKDKKtlDEIVEQSLIKSALWNEVKD-------KLNTNALSLSGGQQQR 164
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIR-----LARPDAS--DAEIREALERAGLDEFVAAlpqgldtPIGEGGAGLSGGQAQR 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-246 |
1.62e-26 |
|
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: 105.57 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRT---LNRmndLVEG-IKIEGNVIYEGkniySNNFDVLELRRKIGMVFQTPNPFL-MSIYDNIS 115
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAiagLER---PDSGrIRLGGEVLQDS----ARGIFLPPHRRRIGYVFQEARLFPhLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 116 YGPK-IHGTKDKKTLDEIVEqsliksalWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGK 194
Cdd:COG4148 100 YGRKrAPRAERRISFDEVVE--------LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 224511529 195 IEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNP 246
Cdd:COG4148 172 ILPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-213 |
1.82e-26 |
|
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: 101.86 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNrmnDLVEGIKIEGNVIYEGKNIYSNNFdvlelRRKIGMVFQtpnpflm 108
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---GRRTGLGVSGEVLINGRPLDKRSF-----RKIIGYVPQ------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 siyDNISYGpkihgtkdkkTLdeIVEQSLIKSAlwnevkdKLNtnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:cd03213 90 ---DDILHP----------TL--TVRETLMFAA-------KLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 224511529 189 PISTGKIEELIINL-KESYTIIIVTH 213
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIH 169
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
43-242 |
1.96e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.35 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyEGKNIYSnnfdvleLRRKIGMVFQTPNPFLMSIYDNISYGpkih 121
Cdd:PRK13657 365 AIVGPTGAGKSTLINLLQRVFDPQSGrILIDGTDI-RTVTRAS-------LRRNIAVVFQDAGLFNRSIEDNIRVG---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 122 gtKDKKTLDEIVEQSLIKSAL-WNEVK-DKLNTNA----LSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKI 195
Cdd:PRK13657 433 --RPDATDEEMRAAAERAQAHdFIERKpDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 224511529 196 EELIINLKESYTIIIVTHNMQQAgRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK13657 511 KAALDELMKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDEL 556
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-231 |
2.12e-26 |
|
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: 102.54 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIK--IEGNVIYEGKNIYSNNFDVLelrrkigMVFQTPNPF 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL-------NLISGLAqpTSGGVILEGKQITEPGPDRM-------VVFQNYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 107 -LMSIYDNISYGPK-IHGTKDKKTLDEIVEQSLIKSALwNEVKDKLNTNalsLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:TIGR01184 67 pWLTVRENIALAVDrVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQ---LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224511529 185 SALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
9-256 |
2.64e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.79 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNLFYT-------------DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEGIkiEGNV 75
Cdd:PRK15079 4 GKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKAT--DGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 76 IYEGKNIYS-NNFDVLELRRKIGMVFQTP----NPfLMSIYDNIS-----YGPKIHgtkdKKTLDEIVEQSLIKSALWNE 145
Cdd:PRK15079 79 AWLGKDLLGmKDDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAeplrtYHPKLS----RQEVKDRVKAMMLKVGLLPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 146 VkdkLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDpIStgkIEELIINL-----KE-SYTIIIVTHNMQQAG 219
Cdd:PRK15079 154 L---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-VS---IQAQVVNLlqqlqREmGLSLIFIAHDLAVVK 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 224511529 220 RISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYIS 256
Cdd:PRK15079 227 HISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMS 263
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-248 |
3.39e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.11 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNviyEGKNiysnnfDVLELRRKI 96
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMN------DVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 97 GMVFQT----PNpflMSIYDNISYGPKIHGTKdKKTLDEIVEQsliksalwneVKDKLNTNAL------SLSGGQQQRLC 166
Cdd:PRK11000 78 GMVFQSyalyPH---LSVAENMSFGLKLAGAK-KEEINQRVNQ----------VAEVLQLAHLldrkpkALSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPI--STGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAAlrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
....
gi 224511529 245 NPKN 248
Cdd:PRK11000 224 YPAN 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-260 |
4.58e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 102.76 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIysNNFDVLELRRKI 96
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHI--QHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 97 GMVFQTP-NPFLMSIYDNISYGPKIHG---TKDKKTLDEIVEQSLIKSALWNEVKDKLNTnalsLSGGQQQRLCIARTLA 172
Cdd:PRK10253 84 GLLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPtdelffnPKNTK 250
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIV 232
|
250
....*....|
gi 224511529 251 TEEYISGKFG 260
Cdd:PRK10253 233 TAELIERIYG 242
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-242 |
1.13e-25 |
|
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: 105.42 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlvegIKIE----GNVIYEGKNIYSnnFDVLELRRKIGMVFQTP 103
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL---------LGFEtpesGSVFYDGQDLAG--LDVQAVRRQLGVVLQNG 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NPFLMSIYDNISYGPKIhgtkdkkTLDEIVEqSLIKSALWNEVKD---KLNT----NALSLSGGQQQRLCIARTLAIEPN 176
Cdd:TIGR03797 537 RLMSGSIFENIAGGAPL-------TLDEAWE-AARMAGLAEDIRAmpmGMHTviseGGGTLSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKesYTIIIVTHnmqqagRIS-----DRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAH------RLStirnaDRIYVLDAGRVVQQGTYDEL 671
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-243 |
2.65e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 25 DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIK-IEGNVIYEGKNIYSNNFD--VLELRRKIGMVFQ 101
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL------LKpTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 TPNPFLM--SIYDNISYGPKIHGTKdkktLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:PRK13646 93 FPESQLFedTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 180 MDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-242 |
2.75e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFlrtlnrmndlvegIKI--------EGNVIYEGKN 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTL-------------MKIlsgvyqpdSGEILLDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 82 I-YSNNFDVLELRrkIGMVFQTPNPF-LMSIYDNISYG--PKIHGTKDKKTLDEIVEQSLiksalwNEVKDKLNTNAL-- 155
Cdd:COG1129 68 VrFRSPRDAQAAG--IAIIHQELNLVpNLSVAENIFLGrePRRGGLIDWRAMRRRARELL------ARLGLDIDPDTPvg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIE 234
Cdd:COG1129 140 DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
....*...
gi 224511529 235 EESPTDEL 242
Cdd:COG1129 220 GTGPVAEL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-236 |
2.77e-25 |
|
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: 99.21 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKI-EGNVIYEGKNiYSNNFDVLel 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL------IKPdSGEITFDGKS-YQKNIEAL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 rRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKktldeIVEQSLIKSALWNEVKDKlnTNALSLsgGQQQRLCIARTL 171
Cdd:cd03268 72 -RRIGALIEAPGFYPnLTARENLRLLARLLGIRKK-----RIDEVLDVVGLKDSAKKK--VKGFSL--GMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEE 236
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
29-243 |
3.64e-25 |
|
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: 100.26 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYEGKNIYS-NNFDVLELRRKIGMVFQ---- 101
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLAR-------LLLGLEkpAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQdsps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 TPNPfLMSIYDNISYgPKIHGTKDKKTLDEIVEQSLIKSA-LWNEVKDKLNTNalsLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:TIGR02769 100 AVNP-RMTVRQIIGE-PLRHLTSLDESEQKARIAELLDMVgLRSEDADKLPRQ---LSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 181 DEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-231 |
7.12e-25 |
|
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: 98.21 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 16 TKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmnDLVEGIKieGNVIYEGKNIYSNNFDVlelRRK 95
Cdd:cd03266 8 TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA---GLLEPDA--GFATVDGFDVVKEPAEA---RRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 IGMVFQTPNPF-LMSIYDNISYGPKIHGTKD---KKTLDEIVEQSliksalwnEVKDKLNTNALSLSGGQQQRLCIARTL 171
Cdd:cd03266 80 LGFVSDSTGLYdRLTARENLEYFAGLYGLKGdelTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-216 |
8.87e-25 |
|
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: 103.02 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIysNNFDVLE 91
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQP-----TEGSVLLDGVDI--RQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYG-PKIHgtkdkktlDEIVEQSLIKSALWNEVKD-------KLNTNALSLSGGQQQ 163
Cdd:TIGR03375 537 LRRNIGYVPQDPRLFYGTLRDNIALGaPYAD--------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQRQ 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPIStgkiEELII-NLK---ESYTIIIVTHNMQ 216
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRS----EERFKdRLKrwlAGKTLVLVTHRTS 661
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-233 |
9.50e-25 |
|
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: 97.95 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 34 IKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIKI--EGNVIYEGKniysnnfDVLEL---RRKIGMVFQTPNPFL- 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLINGV-------DVTAAppaDRPVSMLFQENNLFAh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 MSIYDNISYG--PKIHGTKdkktldeiVEQSLIKSALWNE-VKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:cd03298 85 LTVEQNVGLGlsPGLKLTA--------EDRQAIEVALARVgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224511529 185 SALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03298 157 AALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-216 |
1.69e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 96.77 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD-----FKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndLVEGIKIEGNVIYEGKniysnnfd 88
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----LGELEKLSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 vlelrrkIGMVFQTPnpFLM--SIYDNISYGPKIhgtkDKKTLDEIVEQSLIKSALwNEVKDKLNT----NALSLSGGQQ 162
Cdd:cd03250 68 -------IAYVSQEP--WIQngTIRENILFGKPF----DEERYEKVIKACALEPDL-EILPDGDLTeigeKGINLSGGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPiSTGK--IEELII-NLKESYTIIIVTHNMQ 216
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDA-HVGRhiFENCILgLLLNNKTRILVTHQLQ 189
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-213 |
2.34e-24 |
|
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: 96.79 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD--FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIysNNFDVLE 91
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSG-----SILIDGVDI--SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISygpkIHGTKDKKTLDEIVEQSLIKSaLWNEVKDKLNT----NALSLSGGQQQRLCI 167
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLD----PFGEYSDEELWQALERVGLKE-FVESLPGGLDTvveeGGENLSVGQRQLLCL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-242 |
3.50e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 101.35 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIysNNFDVLELRRKIGMVFQTPNPF 106
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSL--KDIDRHTLRQFINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 107 LMSIYDNISYGPKIHGTKDKktLDEIVEQSLIKSALWN---EVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEP 183
Cdd:TIGR01193 561 SGSILENLLLGAKENVSQDE--IWAACEIAEIKDDIENmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 184 TSALDPISTGKIEELIINLKESyTIIIVTHNMQQAGRiSDRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-242 |
5.66e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 98.65 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 31 KINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGkniySNNFDVLELRRKIGMVFQTPNPFL-M 108
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRTLFDS----RKGIFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 SIYDNISYGPKihgtkdkktlDEIVEQSLIKsalWNEVKDKLNTNAL------SLSGGQQQRLCIARTLAIEPNVILMDE 182
Cdd:TIGR02142 91 SVRGNLRYGMK----------RARPSERRIS---FERVIELLGIGHLlgrlpgRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 183 PTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-221 |
1.64e-23 |
|
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: 93.43 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKA--LNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKNIysNNFDV 89
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLAR-------LILGLlrPTSGRVRLDGADI--SQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LELRRKIGMVFQTPNPFLMSIYDNIsygpkihgtkdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIAR 169
Cdd:cd03246 72 NELGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 170 TLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNM---QQAGRI 221
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-216 |
2.04e-23 |
|
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: 94.71 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 24 TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndLVEGIKIEGNVIYEGKNIYSNNFDVLELRRKIGMVFQTP 103
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NPFLM--SIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEvKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:cd03290 87 KPWLLnaTVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGD-QTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 224511529 182 EPTSALD-PISTGKIEELIINL--KESYTIIIVTHNMQ 216
Cdd:cd03290 166 DPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-242 |
3.42e-23 |
|
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: 94.48 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIYSnnFDVLELRRKIGMVFQTPNPFL 107
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-----VPENGRVLVDGHDLAL--ADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 MSIYDNISYgpkihgTKDKKTLDEIVEQSLIKSA--LWNEVKDKLNT----NALSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:cd03252 90 RSIRDNIAL------ADPGMSMERVIEAAKLAGAhdFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 182 EPTSALDPISTGKIEELIINLKESYTIIIVTHNMqQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
32-221 |
8.93e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 32 INIKILKNSITALIGPSGCGKSTFLRTLNrmNDLVEGIKIEGNVIYEGKNIYsnnfDVLELRRKIGMVFQTP--NPFlMS 109
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLT----ALPAEQRRIGILFQDDllFPH-LS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 110 IYDNISYG--PKIHGTKDKKTldeiVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSAL 187
Cdd:COG4136 93 VGENLAFAlpPTIGRAQRRAR----VEQALEEAGL----AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 224511529 188 DPISTGKIEELIINLKESYTI--IIVTHNMQ---QAGRI 221
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIpaLLVTHDEEdapAAGRV 203
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
17-247 |
1.07e-22 |
|
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: 93.11 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTflrTLNRMNDLVEgiKIEGNVIYEGKNIYSNNFDvLELRRKI 96
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHLPMH-ERARLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 97 GMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwNEVKDKLntnALSLSGGQQQRLCIARTLAIEP 175
Cdd:TIGR04406 79 GYLPQEASIFRkLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI-SHLRDNK---AMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 176 NVILMDEPTSALDPISTGKIEELIINLKE-SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPK 247
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-242 |
2.20e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.95 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTlnrmndlvegikIEGNVIYEGKNIYSNNFDVLEL---RRKIGMVFQTPNPFL-MSIYDNISYGp 118
Cdd:PRK10771 29 AILGPSGAGKSTLLNL------------IAGFLTPASGSLTLNGQDHTTTppsRRPVSMLFQENNLFShLTVAQNIGLG- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 119 kIH-GTK----DKKTLDEIVEQSLIKSALwnevkDKLNTnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTG 193
Cdd:PRK10771 96 -LNpGLKlnaaQREKLHAIARQMGIEDLL-----ARLPG---QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 224511529 194 KIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK10771 167 EMLTLVsqVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-246 |
2.60e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 7 KPKN-EIIIETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNI 82
Cdd:TIGR00958 471 APLNlEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ-----PTGGQVLLDGVPL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 83 ysNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSLIKSA--LWNEVKDKLNTN----ALS 156
Cdd:TIGR00958 546 --VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG------LTDTPDEEIMAAAKAANAhdFIMEFPNGYDTEvgekGSQ 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDpistGKIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLNGCIE 234
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAsrTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
250
....*....|..
gi 224511529 235 EESPTDELFFNP 246
Cdd:TIGR00958 693 EMGTHKQLMEDQ 704
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-223 |
3.07e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlveGIKIE---GNVIYEGKNIYSNNFDV 89
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI--------GGQIApdhGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 L-ELRRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCI 167
Cdd:PRK11831 79 LyTVRKRMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL----RGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISD 223
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIAD 212
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
27-224 |
3.86e-22 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 90.93 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNI----YSNNfdvLELRRK-IGMVFQ 101
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSL-----DSGSLTLAGKEVtnlsYSQK---IILRRElIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 TPN--PFLmSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALWNEVKDKlntnALSLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:NF038007 91 SFNliPHL-SIFDNVALPLKYRGVA-KKERIERVNQVLNLFGIDNRRNHK----PMQLSGGQQQRVAIARAMVSNPALLL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 180 MDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNmQQAGRISDR 224
Cdd:NF038007 165 ADEPTGNLDSKNARAVLQQLKYINQKgTTIIMVTHS-DEASTYGNR 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-218 |
5.48e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.46 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK----ALNKINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIK--IEGNVIYEGKNIYSNNF 87
Cdd:COG4525 4 LTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLL-------NLIAGFLapSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DvlelrRkiGMVFQtpNPFLM---SIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQR 164
Cdd:COG4525 77 D-----R--GVVFQ--KDALLpwlNVLDNVAFGLRLRGV-PKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQA 218
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEA 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-247 |
8.82e-22 |
|
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: 90.29 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTflrTLNRMNDLVegikiegnVIYEGKnIYSNNFDVLEL- 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLV--------KPDSGK-ILLDGQDITKLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 -----RRKIGMVFQTPNPFL-MSIYDNISYGPKIHGtKDKKTLDEIVEQSLIKSALwnevkDKL-NTNALSLSGGQQQRL 165
Cdd:cd03218 69 mhkraRLGIGYLPQEASIFRkLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI-----THLrKSKASSLSGGERRRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
...
gi 224511529 245 NPK 247
Cdd:cd03218 223 NEL 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-245 |
1.04e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 12 IIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndLVEGIKIEGNVIYEGKNIYSNNFDVLe 91
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL-----CGDPRATSGRIVFDGKDITDWQTAKI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFL-MSIYDNISYGPKIhgtKDKKTLDEIVEQSLiksALWNEVKDKLNTNALSLSGGQQQRLCIART 170
Cdd:PRK11614 78 MREAVAIVPEGRRVFSrMTVEENLAMGGFF---AERDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFN 245
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
1.48e-21 |
|
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: 93.24 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEI-----IIETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVI 76
Cdd:TIGR02203 316 EKDTGTRAIerargDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG-----QIL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 77 YEGKNIysNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGPKihGTKDKKTLDEIVEQSLIKSaLWNEVKDKLNT---- 152
Cdd:TIGR02203 391 LDGHDL--ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRT--EQADRAEIERALAAAYAQD-FVDKLPLGLDTpige 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 153 NALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNM---QQAGRI 221
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKADRI 537
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-236 |
1.76e-21 |
|
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: 88.14 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY--TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmnDLVEGikiEGNVIYEGKNIySNNFDvlE 91
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPV-SDLEK--A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNIsygpkihGTKdkktldeiveqsliksalwnevkdklntnalsLSGGQQQRLCIARTL 171
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL-------GRR--------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRIsDRTAFFLNGCIEEE 236
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-217 |
3.53e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.22 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 3 KEKDKPKNEII-IETKNLNLFYTDFKALNK-INIKILKNSITALIGPSGCGKSTFLRTLnrmndLvegikieGNVIYEGK 80
Cdd:PRK11174 338 GEKELASNDPVtIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNAL-----L-------GFLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 81 ----NIYSNNFDVLELRRKIGMVFQTPNPFLMSIYDNISYGpKIHGTKDKktLDEIVEQSLIKSALwNEVKDKLNT---- 152
Cdd:PRK11174 406 lkinGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQ--LQQALENAWVSEFL-PLLPQGLDTpigd 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 153 NALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQ 217
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-225 |
3.65e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYEGKNIYS-NNFDVLELRRKIGMVFQTP 103
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-------LICGIErpSAGKIWFSGHDITRlKNREVPFLRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NpFLM--SIYDNISYgPKIHGTKDKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:PRK10908 89 H-LLMdrTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLL----DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224511529 182 EPTSALDpistGKIEELIINLKESY-----TIIIVTHNMQQAGRISDRT 225
Cdd:PRK10908 163 EPTGNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYRM 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-231 |
4.40e-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: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTflrTLNRMNDLVEgiKIEGNVIYEGKNIySNNFDVLelRRKIGMVFQTPNPFL 107
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLP--PTSGTVLVGGKDI-ETNLDAV--RQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 -MSIYDNISYGPKIHG-TKDKKTLDeiVEQSLIKSALWNevkdKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTS 185
Cdd:TIGR01257 1017 hLTVAEHILFYAQLKGrSWEEAQLE--MEAMLEDTGLHH----KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 186 ALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-230 |
5.01e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.40 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 7 KPKNEI--IIETKNLNlfytdFKALNKINIKILKN--------SITALIGPSGCGKSTFLRTLNRMNDLVEGIKI----- 71
Cdd:PTZ00265 1157 KNKNDIkgKIEIMDVN-----FRYISRPNVPIYKDltfscdskKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkne 1231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 72 ---------------EGNVIYEGKN---------------IYSNNFDVL------------ELRRKIGMVFQTPNPFLMS 109
Cdd:PTZ00265 1232 htndmtneqdyqgdeEQNVGMKNVNefsltkeggsgedstVFKNSGKILldgvdicdynlkDLRNLFSIVSQEPMLFNMS 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 110 IYDNISYGPKIHGTKDKK------TLDEIVEqsliksALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEP 183
Cdd:PTZ00265 1312 IYENIKFGKEDATREDVKrackfaAIDEFIE------SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 224511529 184 TSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLN 230
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-216 |
5.84e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.47 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGnviyegKNIYSnnFDVL 90
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGkIEIDG------IDIST--IPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNISygpkihgTKDKKTLDEIVEqsliksALwnevkdKLNTNALSLSGGQQQRLCIART 170
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLD-------PFDEYSDEEIYG------AL------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQ 216
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLR 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-224 |
7.49e-21 |
|
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: 87.34 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRM--NDlvegikiEGNVIYEGKNIysnnfdVLE 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIilPD-------SGEVLFDGKPL------DIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVEqsLIKSAlwnEVKDKLNTNALSLSGGQQQRLCIART 170
Cdd:cd03269 68 ARNRIGYLPEERGLYPkMKVIDQLVYLAQLKGLKKEEARRRIDE--WLERL---ELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDR 224
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDR 197
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
33-239 |
7.87e-21 |
|
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: 87.61 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 33 NIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegnviyegkNIYSNNFDVLEL---RRKIGMVFQTPNPFL-M 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASG------------SIKVNDQSHTGLapyQRPVSMLFQENNLFAhL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 SIYDNISYGPKiHGTKdkktLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:TIGR01277 86 TVRQNIGLGLH-PGLK----LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224511529 189 PISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPT 239
Cdd:TIGR01277 161 PLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
11-260 |
9.48e-21 |
|
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: 87.83 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIE------GNViyegkniys 84
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 85 nnfDVLELRRKIGMV---FQTPNPFLMSIYDNI------SYGPKIHGTKDKKtldEIVEQSLiksALWnEVKDKLNTNAL 155
Cdd:COG1119 72 ---DVWELRKRIGLVspaLQLRFPRDETVLDVVlsgffdSIGLYREPTDEQR---ERARELL---ELL-GLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250 260
....*....|....*....|....*..
gi 224511529 234 EEESPTDELFfnpkntkTEEYISGKFG 260
Cdd:COG1119 222 VAAGPKEEVL-------TSENLSEAFG 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-214 |
1.06e-20 |
|
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: 90.88 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSnnFDVLELRRKIGMVFQTPNPFL 107
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 MSIYDNISYGpkihgtkDKKTLDEIVEQSLIKSALWN---EVKDKLNT----NALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:TIGR02868 423 TTVRENLRLA-------RPDATDEELWAALERVGLADwlrALPDGLDTvlgeGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 224511529 181 DEPTSALDPISTGKIEELIINLKESYTIIIVTHN 214
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-224 |
4.05e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.61 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRM--NDLVEGIKIE--GNVIYEGKNIYSnn 86
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIEllGRTVQREGRLAR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 87 fDVLELRRKIGMVFQTPNPF-LMSIYDNISYGpKIHGTKDKKTL--------DEIVEQSLIKSALWNEVKDKLNTnalsL 157
Cdd:PRK09984 80 -DIRKSRANTGYIFQQFNLVnRLSVLENVLIG-ALGSTPFWRTCfswftreqKQRALQALTRVGMVHFAHQRVST----L 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 158 SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDR 224
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCER 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-247 |
5.40e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.33 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTflrtLNRMNDLVEgIKIEGNVIYEGKNIYSNNFDVL-ELRRKIGMVFQTP-- 103
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIE-TPTGGELYYQGQDLLKADPEAQkLLRQKIQIVFQNPyg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 --NPflmsiydnisygpkihgtkdKKTLDEIVEQSLIksalwnevkdkLNTN---------ALSL--------------- 157
Cdd:PRK11308 104 slNP--------------------RKKVGQILEEPLL-----------INTSlsaaerrekALAMmakvglrpehydryp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 158 ---SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE----SYTIIivTHNMQQAGRISDRT-AFFL 229
Cdd:PRK11308 153 hmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelglSYVFI--SHDLSVVEHIADEVmVMYL 230
|
250
....*....|....*...
gi 224511529 230 NGCIeEESPTDELFFNPK 247
Cdd:PRK11308 231 GRCV-EKGTKEQIFNNPR 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-225 |
5.82e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTlnrmndlvegikIEGNVIYEGKNIYSNNFDVLELR-----RKIGMVFQ 101
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA------------IAGSLPPDSGSILIDGKDVTKLPeykraKYIGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 tpNPFL-----MSIYDNIS--------YGPKIHGTKDKKtlDEIVEQsLikSALWNEVKDKLNTNALSLSGGQQQRLC-I 167
Cdd:COG1101 88 --DPMMgtapsMTIEENLAlayrrgkrRGLRRGLTKKRR--ELFREL-L--ATLGLGLENRLDTKVGLLSGGQRQALSlL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 168 ARTLAiEPNVILMDEPTSALDPISTGKIEEL---IINlKESYTIIIVTHNMQQAGRISDRT 225
Cdd:COG1101 161 MATLT-KPKLLLLDEHTAALDPKTAALVLELtekIVE-ENNLTTLMVTHNMEQALDYGNRL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
42-225 |
6.19e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.18 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 42 TALIGPSGCGKSTFLRTLNRmNDLVEGIKIEGNVIYEGKNIYS-NNFDVLELRRK-IGMVFQtpnpFLMSIydnisygPK 119
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYG-NYLPDSGSILVRHDGGWVDLAQaSPREILALRRRtIGYVSQ----FLRVI-------PR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 120 IhgtkdkKTLDeIVEQSL----------------------IKSALWNevkdklntnaLS---LSGGQQQRLCIARTLAIE 174
Cdd:COG4778 108 V------SALD-VVAEPLlergvdreearararellarlnLPERLWD----------LPpatFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224511529 175 PNVILMDEPTSALDPISTGKIEELIINLKESYTIII-VTHNMQQAGRISDRT 225
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVADRV 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
44-188 |
6.27e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.59 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegkniysNNfdvLELR-RKIGMVFQtpNPFL---MSIYDNISYGP 118
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGeIWIGGRVV--------NE---LEPAdRDIAMVFQ--NYALyphMSVRENMAYGL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 119 KIHGTkDKKTLDEIVEqsliksalwnEVKDKLNTNAL------SLSGGQQQRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:PRK11650 102 KIRGM-PKAEIEERVA----------EAARILELEPLldrkprELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-233 |
7.04e-20 |
|
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: 85.46 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNiysnnfdvlELRRKIGMVFQ 101
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGeVRVAGLVPWKRRK---------KFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 TPNPFL--MSIYDNISYGPKIHGTKD---KKTLDEIVEqsliksALwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPN 176
Cdd:cd03267 102 QKTQLWwdLPVIDSFYLLAAIYDLPParfKKRLDELSE------LL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-245 |
1.24e-19 |
|
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: 84.37 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIYSNNFdvlelr 93
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGIL-----RPTSGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFL-MSIYDNIsygpKIHGTK---DKKTLDEIVEqsliKSALWNEVKDKlntnALSLSGGQQQRLCIAR 169
Cdd:TIGR03740 70 HKIGSLIESPPLYEnLTARENL----KVHTTLlglPDSRIDEVLN----IVDLTNTGKKK----AKQFSLGMKQRLGIAI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 170 TLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGC------IEEESPTDEL 242
Cdd:TIGR03740 138 ALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVlgyqgkINKSENLEKL 217
|
...
gi 224511529 243 FFN 245
Cdd:TIGR03740 218 FVE 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
14-242 |
1.75e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.75 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEgiKIEGNVIYEGKNIysNNFDVLELR 93
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---LLP--PDSGEVLVDGLDV--ATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFL-MSIYDNISYG--PKIHG---TKDKktldEIVEQSLIKSALwNEVKDK-LNTnalsLSGGQQQRLC 166
Cdd:COG4604 75 KRLAILRQENHINSrLTVRELVAFGrfPYSKGrltAEDR----EIIDEAIAYLDL-EDLADRyLDE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-242 |
1.78e-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: 87.17 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVegiKIEGNVIYE--------------- 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYE---PTSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 79 --------GKNIYSNNFDVLEL--------RRKIGMVFQtpNPFLM----SIYDNISYGPKIHGTKDKKTLDEIVEqsLI 138
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDFWNLsdklrrriRKRIAIMLQ--RTFALygddTVLDNVLEALEEIGYEGKEAVGRAVD--LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 139 KSAlwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQ 216
Cdd:TIGR03269 154 EMV---QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 224511529 217 QAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-246 |
2.09e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.93 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNL-FYT---DFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVEGIKIEGNVIYEGKNIYs 84
Cdd:PRK09473 8 QADALLDVKDLRVtFSTpdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREIL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 85 nNFDVLELRR----KIGMVFQTP----NPFlMSIYDNISYGPKIHGTKDKKtldEIVEQS--LIKSALWNEVKDKLNTNA 154
Cdd:PRK09473 85 -NLPEKELNKlraeQISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKA---EAFEESvrMLDAVKMPEARKRMKMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 155 LSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGC 232
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGR 239
|
250
....*....|....
gi 224511529 233 IEEESPTDELFFNP 246
Cdd:PRK09473 240 TMEYGNARDVFYQP 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
43-237 |
5.91e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSNNFDV-LELR-RKIGMVFQTpnpFLM----SIYDNISY 116
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQS---FMLiptlNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 117 GPKIHGTKDKKTLDEIVEqsLIKSALWNEvkdKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIE 196
Cdd:PRK10584 112 PALLRGESSRQSRNGAKA--LLEQLGLGK---RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224511529 197 ELIINLKESY--TIIIVTHNMQQAGRiSDRTAFFLNGCIEEES 237
Cdd:PRK10584 187 DLLFSLNREHgtTLILVTHDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-242 |
5.96e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKNIysnnfDVL 90
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFY-------MVVGIvpRDAGNIIIDDEDI-----SLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 EL----RRKIGMVFQTPNPFL-MSIYDNISYGPKIH----GTKDKKTLDEIVEQSLIksalwNEVKDKLNTnalSLSGGQ 161
Cdd:PRK10895 71 PLharaRRGIGYLPQEASIFRrLSVYDNLMAVLQIRddlsAEQREDRANELMEEFHI-----EHLRDSMGQ---SLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG-CIEEESPT 239
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGhLIAHGTPT 222
|
...
gi 224511529 240 DEL 242
Cdd:PRK10895 223 EIL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
29-242 |
6.61e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.58 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYEGKNIYS-NNFDVLELRRKIGMVFQTP-- 103
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLAR-------LLVGLEspSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDSis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 --NPfLMSIYDNISYgPKIHGTkdkkTLDEI-----VEQSLIKSALWNEVKDKLNTnalSLSGGQQQRLCIARTLAIEPN 176
Cdd:PRK10419 101 avNP-RKTVREIIRE-PLRHLL----SLDKAerlarASEMLRAVDLDDSVLDKRPP---QLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 177 VILMDEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-224 |
6.94e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEgkniysnnfdvlELRRKIGMVFQT 102
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA------------EAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PN--PFlMSIYDNISYGPKIHGTKDkktldeiVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:PRK11247 90 ARllPW-KKVIDNVGLGLKGQWRDA-------ALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 181 DEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDR 224
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADR 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-214 |
7.32e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSNNFDv 89
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-----PTSGTLLFEGEDISTLKPE- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 lELRRKIGMVFQTPNPFLMSIYDNISYGPKIHgtkdKKTLDE-IVEQSLIKSALWNEVKDKlNTNALSlsGGQQQRLCIA 168
Cdd:PRK10247 78 -IYRQQVSYCAQTPTLFGDTVYDNLIFPWQIR----NQQPDPaIFLDDLERFALPDTILTK-NIAELS--GGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIII--VTHN 214
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-235 |
8.82e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 8.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 12 IIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVegiKIEGNVIYeGKNI----YSNNF 87
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELE---PDSGTVKL-GETVkigyFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRrkigmvfqtpnpflMSIYDNISYGpkiHGTKDKKTLDEIVEQSLIKSalwnevkDKLNTNALSLSGGQQQRLCI 167
Cdd:COG0488 388 EELDPD--------------KTVLDELRDG---APGGTEQEVRGYLGRFLFSG-------DDAFKPVGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEELIINlkesY--TIIIVTHNMQQAGRISDRTAFFLNGCIEE 235
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD----FpgTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-247 |
9.00e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKST-FlrtlnRMndlvegikIEGNVIYEGKNIYSNNFDV 89
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtF-----YM--------IVGLVKPDSGRIFLDGEDI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 LEL------RRKIGMVFQTPNPFL-MSIYDNISYGPKIHGtKDKKTLDEIVEQsliksaLWNE--VKDKLNTNALSLSGG 160
Cdd:COG1137 68 THLpmhkraRLGIGYLPQEASIFRkLTVEDNILAVLELRK-LSKKEREERLEE------LLEEfgITHLRKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPT 239
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
....*...
gi 224511529 240 DELFFNPK 247
Cdd:COG1137 221 EEILNNPL 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
41-213 |
1.38e-18 |
|
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: 81.37 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRT---LNRMNdlvegikiEGNVIYEGKNIYSnnfDVLELRRKIGMVFQTP--NPFLmSIYDNIS 115
Cdd:COG4133 30 ALALTGPNGSGKTTLLRIlagLLPPS--------AGEVLWNGEPIRD---AREDYRRRLAYLGHADglKPEL-TVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 116 YGPKIHGTK-DKKTLDEIVEQSLIKSALWNEVKdklntnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGK 194
Cdd:COG4133 98 FWAALYGLRaDREAIDEALEAVGLAGLADLPVR--------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|
gi 224511529 195 IEELIINLKES-YTIIIVTH 213
Cdd:COG4133 170 LAELIAAHLARgGAVLLTTH 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-246 |
1.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD-FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGknIYSNNFDVL- 90
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-----PQKGKVLVSG--IDTGDFSKLq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLM--SIYDNISYGPK---IHGTKDKKTLDEIVEQSLIKSALWNEVKdklntnalSLSGGQQQRL 165
Cdd:PRK13644 74 GIRKLVGIVFQNPETQFVgrTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPK--------TLSGGQGQCV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAgRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLS 224
|
..
gi 224511529 245 NP 246
Cdd:PRK13644 225 DV 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-224 |
3.20e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTflrtlnrmndLVegiKI--------EGNVIYEGK- 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST----------LM---KIlyglyqpdSGEILIDGKp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 81 -NIYSNNfDVLELrrKIGMVFQ----TPNpflMSIYDNISYG--PKIHGTKDKKTLDEIVEqsliksalwnEVKDK---- 149
Cdd:COG3845 69 vRIRSPR-DAIAL--GIGMVHQhfmlVPN---LTVAENIVLGlePTKGGRLDRKAARARIR----------ELSERygld 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 150 LNTNAL--SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPistGKIEELIINLK----ESYTIIIVTHNMQQAGRISD 223
Cdd:COG3845 133 VDPDAKveDLSVGEQQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIAD 209
|
.
gi 224511529 224 R 224
Cdd:COG3845 210 R 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-256 |
3.85e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMndlvegIKIEGNVIYEGKNIYS-NNFDVLELRRKIGMVFQTPNPFL---MSIYDNISYGPK 119
Cdd:PRK15134 317 LVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNSSLnprLNVLQIIEEGLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 120 IHgtkdKKTLDEIVEQSLIKSALwNEVKDKLNTN---ALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIE 196
Cdd:PRK15134 391 VH----QPTLSAAQREQQVIAVM-EEVGLDPETRhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 197 ELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYIS 256
Cdd:PRK15134 466 ALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-240 |
3.95e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSNnfd 88
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS-----PDAGKITVLGVPVPAR--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLELRRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTldEIVEQSLIKSAlwnEVKDKLNTNALSLSGGQQQRLCI 167
Cdd:PRK13536 109 ARLARARIGVVPQFDNLDLeFTVRENLLVFGRYFGMSTREI--EAVIPSLLEFA---RLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKI-EELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGC-IEEESPTD 240
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRkIAEGRPHA 258
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-221 |
6.50e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIkiegnviYE--GKNIYSNNFDVL-ELRRK-IGMVFQT 102
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-------YRvaGQDVATLDADALaQLRREhFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PN--PFLmSIYDNISYgPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:PRK10535 95 YHllSHL-TAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224511529 181 DEPTSALDPISTgkiEELIINLKE----SYTIIIVTHNMQ---QAGRI 221
Cdd:PRK10535 169 DEPTGALDSHSG---EEVMAILHQlrdrGHTVIIVTHDPQvaaQAERV 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-243 |
1.40e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmnDLVEGIKieGNVIYEGKNIYSNNFDVLEL 92
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLS---GLLRPQK--GAVLWQGKPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNP--FLMSIYDNISYGPKIHGTKDkktlDEIVEQslIKSALWNEVKDKLNTNALS-LSGGQQQRLCIAR 169
Cdd:PRK13638 76 RQQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPE----AEITRR--VDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 170 TLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELF 243
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-252 |
1.79e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.17 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 24 TDFKALNKINIKILKNSITALIGPSGCGKStflrtlnrmndlVEGIKIEGNVIYEGK----NIYSNNFDVLEL----RRK 95
Cdd:PRK11022 18 APFRAVDRISYSVKQGEVVGIVGESGSGKS------------VSSLAIMGLIDYPGRvmaeKLEFNGQDLQRIsekeRRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 I-----GMVFQTPNPFLMSIYD---NISYGPKIHGTKDKKTLdeivEQSLIKsaLWNEV-----KDKLNTNALSLSGGQQ 162
Cdd:PRK11022 86 LvgaevAMIFQDPMTSLNPCYTvgfQIMEAIKVHQGGNKKTR----RQRAID--LLNQVgipdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTD 240
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH 239
|
250
....*....|..
gi 224511529 241 ELFFNPKNTKTE 252
Cdd:PRK11022 240 DIFRAPRHPYTQ 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
42-213 |
2.06e-17 |
|
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: 81.40 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 42 TALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGnviyegkniysnnFDVLE-----LRRKIGMVFQTPNPFLMSIYDNIS 115
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGrILIDG-------------QDIRDvtqasLRAAIGIVPQDTVLFNDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 116 YGpkihgtKDKKTLDEIVE-------QSLIKSalwneVKDKLNTN----ALSLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:COG5265 454 YG------RPDASEEEVEAaaraaqiHDFIES-----LPDGYDTRvgerGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180
....*....|....*....|....*....
gi 224511529 185 SALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:COG5265 523 SALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-233 |
2.64e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.08 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlVEGIKI-EGNVIYEGKNIYSNNFdvlelRRKIGMVFQTPN- 104
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTtSGQILFNGQPRKPDQF-----QKCVAYVRQDDIl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 105 -PFLmSIYDNISYGPKI--HGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNalsLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:cd03234 93 lPGL-TVRETLTYTAILrlPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 182 EPTSALDPISTGKIEELIINLKESYTIIIVThnMQQAG----RISDRTAFFLNGCI 233
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILT--IHQPRsdlfRLFDRILLLSSGEI 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-221 |
2.66e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD--FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIysNNFDVLE 91
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD-----PQQGEILLNGQPI--ADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGpkihgtKDKKTlDEIVEQSLIKSALWNEVKDKLNTNAL------SLSGGQQQRL 165
Cdd:PRK11160 412 LRQAISVVSQRVHLFSATLRDNLLLA------APNAS-DEALIEVLQQVGLEKLLEDDKGLNAWlgeggrQLSGGEQRRL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHN---MQQAGRI 221
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRltgLEQFDRI 543
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-222 |
6.36e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.16 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFK----ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYS- 84
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT-----PTSGDVIFNGQPMSKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 85 NNFDVLELR-RKIGMVFQ----TPNpflMSIYDNISYgPKIHGTKDKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSG 159
Cdd:PRK11629 77 SSAAKAELRnQKLGFIYQfhhlLPD---FTALENVAM-PLLIGKKKPAEINSRALEMLAAVGL----EHRANHRPSELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRIS 222
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-242 |
6.54e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 12 IIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmNDLVEGikiEGNVIYEGKNIysNNFDVLE 91
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPD---SGEVRLNGRPL--ADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPN---PFLMSiyDNISYGpKIHGTKDKKTLDEIVEQSLIKSALWnEVKDKLntnALSLSGGQQQRLCIA 168
Cdd:PRK13548 74 LARRRAVLPQHSSlsfPFTVE--EVVAMG-RAPHGLSRAEDDALVAAALAQVDLA-HLAGRD---YPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 169 RTLA------IEPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEE-SPT 239
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADgTPA 226
|
...
gi 224511529 240 DEL 242
Cdd:PRK13548 227 EVL 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
13-256 |
8.01e-17 |
|
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: 77.56 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTL-NRMndlvegIKIEGNVIYEGKNiySNNFDVLE 91
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLaGRL------APDHGTATYIMRS--GAELELYQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 L----RRKI-----GMVFQTPNPFL---MSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALwneVKDKLNTNALSLSG 159
Cdd:TIGR02323 75 LseaeRRRLmrtewGFVHQNPRDGLrmrVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI---DPTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEES 237
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250
....*....|....*....
gi 224511529 238 PTDELFFNPKNTKTEEYIS 256
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVS 250
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
43-213 |
8.01e-17 |
|
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: 79.60 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKNIYSNNFDVLelRRKIGMVFQTPNPFLMSIYDNISYGpki 120
Cdd:TIGR03796 509 ALVGGSGSGKSTIAK-------LVAGLyqPWSGEILFDGIPREEIPREVL--ANSVAMVDQDIFLFEGTVRDNLTLW--- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 121 hgtkDKKTLDEIVEQSLIKSALWNEV---KDKLNTNAL----SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPIStg 193
Cdd:TIGR03796 577 ----DPTIPDADLVRACKDAAIHDVItsrPGGYDAELAeggaNLSGGQRQRLEIARALVRNPSILILDEATSALDPET-- 650
|
170 180
....*....|....*....|...
gi 224511529 194 kieELII--NLKE-SYTIIIVTH 213
Cdd:TIGR03796 651 ---EKIIddNLRRrGCTCIIVAH 670
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
28-218 |
8.34e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTlnrmndlvegikIEGNVIYEGKNIYSNNFDVLELRRKIGMVFQtpNPFL 107
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNL------------IAGFVPYQHGSITLDGKPVEGPGAERGVVFQ--NEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 M---SIYDNISYGPKIHGTkDKKTLDEIVEQSLIKSALWNEVKDKLntnaLSLSGGQQQRLCIARTLAIEPNVILMDEPT 184
Cdd:PRK11248 82 LpwrNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYI----WQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 224511529 185 SALDPISTGKIEELIINL--KESYTIIIVTHNMQQA 218
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEA 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-215 |
1.07e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIegnvIYEGKNIYSNNFDVL 90
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII----INDSHNLKDINLKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 elRRKIGMVFQTPNPFLMSIYDNISYG-------------------------------------------------PKIH 121
Cdd:PTZ00265 459 --RSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 122 GTKDKKTLD--EIVEQS---LIK---SALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTG 193
Cdd:PTZ00265 537 MRKNYQTIKdsEVVDVSkkvLIHdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|....
gi 224511529 194 KIEELIINLK--ESYTIIIVTHNM 215
Cdd:PTZ00265 617 LVQKTINNLKgnENRITIIIAHRL 640
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-241 |
1.78e-16 |
|
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: 75.93 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKA----LNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlvEGIKI--EGNVIYEGKNIY 83
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLL-------AGLDRptSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNFD-VLELR-RKIGMVFQT----PNpflMSIYDNISYGPKIHGTKD-----KKTLDEI-VEQSLikSALWNEvkdkln 151
Cdd:COG4181 78 ALDEDaRARLRaRHVGFVFQSfqllPT---LTALENVMLPLELAGRRDararaRALLERVgLGHRL--DHYPAQ------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 152 tnalsLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPiSTG-KIEELIINLKESY--TIIIVTHNMQQAGRiSDRTAFF 228
Cdd:COG4181 147 -----LSGGEQQRVALARAFATEPAILFADEPTGNLDA-ATGeQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRVLRL 219
|
250
....*....|...
gi 224511529 229 LNGCIEEESPTDE 241
Cdd:COG4181 220 RAGRLVEDTAATA 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-251 |
2.01e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLfYTDFKALNKINIKILKNSITALIGPSGCGKStfLRTLNRMNDLVEGI-KIEGNVIYEGKNIYSNnfdvlEL 92
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVrQTAGRVLLDGKPVAPC-----AL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 R-RKIGMVFQTP----NPfLMSIYDNISYGPKIHG-TKDKKTLDEIVEqslikSALWNEVKDKLNTNALSLSGGQQQRLC 166
Cdd:PRK10418 77 RgRKIATIMQNPrsafNP-LHTMHTHARETCLALGkPADDATLTAALE-----AVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYT--IIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFF 244
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
....*..
gi 224511529 245 NPKNTKT 251
Cdd:PRK10418 231 APKHAVT 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-235 |
2.27e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 73.64 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYegkniysnnfdvlelr 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 rkigmvfqtpnpflmsiydnISYgpkihgtkdkktldeiVEQsliksalwnevkdklntnalsLSGGQQQRLCIARTLAI 173
Cdd:cd03221 65 --------------------IGY----------------FEQ---------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 174 EPNVILMDEPTSALDPIStgkIEELIINLKESY-TIIIVTHnmqqagrisDRtaFFLNGCIEE 235
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALKEYPgTVILVSH---------DR--YFLDQVATK 136
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-260 |
2.42e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmNDLVEGikiEGNVIYEGKNIYSnnFDVLELR 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTPT---AGTVLVAGDDVEA--LSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQ-TPNPFLMSIYDNISYGPKIHGTK---DKKTLDEIVEQSLIKSalwnEVKDKLNTNALSLSGGQQQRLCIAR 169
Cdd:PRK09536 77 RRVASVPQdTSLSFEFDVRQVVEMGRTPHRSRfdtWTETDRAAVERAMERT----GVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 170 TLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPtdelffnPKN 248
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP-------PAD 225
|
250
....*....|..
gi 224511529 249 TKTEEYISGKFG 260
Cdd:PRK09536 226 VLTADTLRAAFD 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-188 |
3.20e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFlrtLNRMNDLVEGikiEGNVIYEGKNIysNNFDVLELRRKIGMVFQ-TPNPFLMSIYDNIS--YG 117
Cdd:COG4138 24 LIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPL--SDWSAAELARHRAYLSQqQSPPFAMPVFQYLAlhQP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 118 PKIHGTKDKKTLDEIVEqsliksALwnEVKDKLNTNALSLSGGQQQRLCIARTL-----AIEPN--VILMDEPTSALD 188
Cdd:COG4138 96 AGASSEAVEQLLAQLAE------AL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-241 |
3.59e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYegkniysnnfdVLELrrkiGMVFq 101
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrVEVNGRVSA-----------LLEL----GAGF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 tpNPFLmSIYDNISYGPKIHG-TKD--KKTLDEIVEQSliksalwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVI 178
Cdd:COG1134 100 --HPEL-TGRENIYLNGRLLGlSRKeiDEKFDEIVEFA--------ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 179 LMDEPTSALDPI----STGKIEELIinlKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDE 241
Cdd:COG1134 169 LVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-236 |
5.22e-16 |
|
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: 74.49 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 23 YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYegkniysnnfdVLELrrkiGMVFQ 101
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtVTVRGRVSS-----------LLGL----GGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 tPNpflMSIYDNISYGPKIHGTKDK---KTLDEIVEQSliksalwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVI 178
Cdd:cd03220 97 -PE---LTGRENIYLNGRLLGLSRKeidEKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 179 LMDEPTSALDPI----STGKIEELIinlKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEE 236
Cdd:cd03220 165 LIDEVLAVGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-252 |
6.70e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTD----FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKN---IYSN 85
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 NFDVLELRR----KIGMVFQTP----NPfLMSIYDNISYGPKIH-GTKDKKTLDE---IVEQSLIKsalwnEVKDKLNTN 153
Cdd:PRK10261 92 EQSAAQMRHvrgaDMAMIFQEPmtslNP-VFTVGEQIAESIRLHqGASREEAMVEakrMLDQVRIP-----EAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 154 ALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKemSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260
....*....|....*....|.
gi 224511529 232 CIEEESPTDELFFNPKNTKTE 252
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTR 266
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-189 |
9.70e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmnDLVEGikiEGNVIYEGKNIysNNFDVLELR 93
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPN---PFlmSIYDNISYGpKIHGTKDKKTLDEIVEQSLIKSALWnevkDKLNTNALSLSGGQQQRLCIART 170
Cdd:COG4559 75 RRRAVLPQHSSlafPF--TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLA----HLAGRSYQTLSGGEQQRVQLARV 147
|
170 180
....*....|....*....|....*.
gi 224511529 171 LA-------IEPNVILMDEPTSALDP 189
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-253 |
9.95e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKS-TFLRTLnRMNDLVEGIKIEGNVIYEGKNIYsnNFDVLELRR----KIGMVFQTP----NPfLMSIYDN 113
Cdd:PRK15134 39 ALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESLL--HASEQTLRGvrgnKIAMIFQEPmvslNP-LHTLEKQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 114 ISYGPKIH-GTKDKKTLDEIV---EQSLIKSAlwnevKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDP 189
Cdd:PRK15134 115 LYEVLSLHrGMRREAARGEILnclDRVGIRQA-----AKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 190 ISTGKIEELIINLKE--SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEE 253
Cdd:PRK15134 190 SVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQK 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-242 |
1.27e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.99 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 3 KEKDKPKNEIIIETKNLNLFYTDF-----KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGiKIEGNVIY 77
Cdd:TIGR03269 269 KECEVEVGEPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG-EVNVRVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 78 EGKNIYSNNFDVL-ELRRKIGMVFQTPNPFL-MSIYDNISYGPKIHGTKDKKTLDEIVeqsLIKSALWNEVKDK--LNTN 153
Cdd:TIGR03269 348 EWVDMTKPGPDGRgRAKRYIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAVI---TLKMVGFDEEKAEeiLDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 154 ALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDG 504
|
250
....*....|.
gi 224511529 232 CIEEESPTDEL 242
Cdd:TIGR03269 505 KIVKIGDPEEI 515
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-213 |
2.04e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 24 TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNNFDvlELRRKIGMVFQTP 103
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-----DIRFHDIPLTKLQLD--SWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NPFLMSIYDNISYGpkihgtKDKKTLDEIVEQSLIKS----------ALWNEVKDKlntnALSLSGGQQQRLCIARTLAI 173
Cdd:PRK10789 399 FLFSDTVANNIALG------RPDATQQEIEHVARLASvhddilrlpqGYDTEVGER----GVMLSGGQKQRISIARALLL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224511529 174 EPNVILMDEPTSALDpistGKIEELII-NLK---ESYTIIIVTH 213
Cdd:PRK10789 469 NAEILILDDALSAVD----GRTEHQILhNLRqwgEGRTVIISAH 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-238 |
1.04e-14 |
|
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: 70.63 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDlvEGIKI-EGNVIYEGKNIysNNFDVLE- 91
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGH--PKYEVtEGEILFKGEDI--TDLPPEEr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPnpflmsiydnisygPKIHGTKDKKTLDEIveqsliksalwNEvkdklntnalSLSGGQQQRLCIARTL 171
Cdd:cd03217 75 ARLGIFLAFQYP--------------PEIPGVKNADFLRYV-----------NE----------GFSGGEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 172 AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRI-SDRTAFFLNGCIEEESP 238
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKLREEgKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-243 |
1.46e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.06 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 5 KDKPKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIY 83
Cdd:TIGR00957 630 KPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMKGSVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNfdvlelrrkigmvfqtpnpflMSIYDNISYGPKIHGTKDKKTLDE---IVEQSLIKSALWNEVKDKlntnALSLSGG 160
Cdd:TIGR00957 710 IQN---------------------DSLRENILFGKALNEKYYQQVLEAcalLPDLEILPSGDRTEIGEK----GVNLSGG 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELII---NLKESYTIIIVTHNMQQAGRIsDRTAFFLNGCIEEES 237
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
....*.
gi 224511529 238 PTDELF 243
Cdd:TIGR00957 844 SYQELL 849
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-224 |
2.24e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 31 KINIKILKNSITALIGPSGCGKSTFLrtlNRMNDLV---EG-IKIEGNVIYE-GKNIYsnnfdvleL---RRKIGMVFQT 102
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTrpqKGrIVLNGRVLFDaEKGIC--------LppeKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PNPF-LMSIYDNISYGPKihgTKDKKTLDEIVEQSLIKSALwnevkdklNTNALSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGMA---KSMVAQFDKIVALLGIEPLL--------DRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224511529 182 EPTSALD-PistgKIEELI---------INLKesytIIIVTHNMQQAGRISDR 224
Cdd:PRK11144 154 EPLASLDlP----RKRELLpylerlareINIP----ILYVSHSLDEILRLADR 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-231 |
3.22e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 8 PKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNiysnn 86
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsISLCGEPVPSRAR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 87 fdvlELRRKIGMVFQTPN--PFLmSIYDNISYGPKIHGTKdKKTLDEIVeQSLIKSAlwnEVKDKLNTNALSLSGGQQQR 164
Cdd:PRK13537 77 ----HARQRVGVVPQFDNldPDF-TVRENLLVFGRYFGLS-AAAARALV-PPLLEFA---KLENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKI-EELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
39-214 |
4.14e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 39 NSITALIGPSGCGKSTFLRTLNRMndlvegIKIE-GNVIYEGKNI-YSNNFDVLE-LRRKIGMvfqtpNPFLmSIYDNIS 115
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGL------LPPAaGTIKLDGGDIdDPDVAEACHyLGHRNAM-----KPAL-TVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 116 YGPKIHGTKDKKTLD--EIVEQSLIksalwnevkdkLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTG 193
Cdd:PRK13539 96 FWAAFLGGEELDIAAalEAVGLAPL-----------AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 224511529 194 KIEELI-INLKESYTIIIVTHN 214
Cdd:PRK13539 165 LFAELIrAHLAQGGIVIAATHI 186
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
43-260 |
4.74e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYSNnfdvlelrRKIGMVFQTPNPFL---MSIYDNISYGP 118
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGeLLIDDHPLHFGDYSYRS--------QRIRMIFQDPSTSLnprQRISQILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 119 KIHGTKDKKTLDEIVEQSLIKSALwneVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEEL 198
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 199 IINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPTDELFFNPKNTKTEEYISGKFG 260
Cdd:PRK15112 192 MLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFG 255
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-213 |
5.86e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.99 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALnkinIKILKNSITA----LI-GPSGCGKSTFLRTLNrmndlveGI--KIEGNVIY-EGKNiysn 85
Cdd:COG4178 363 LALEDLTLRTPDGRPL----LEDLSLSLKPgerlLItGPSGSGKSTLLRAIA-------GLwpYGSGRIARpAGAR---- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 nfdvlelrrkigMVF--QTPNPFLMSIYDNISYgPKIHGTKDkktlDEIVEQSLIKSALwNEVKDKLNTNAL---SLSGG 160
Cdd:COG4178 428 ------------VLFlpQRPYLPLGTLREALLY-PATAEAFS----DAELREALEAVGL-GHLAERLDEEADwdqVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-213 |
8.23e-14 |
|
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: 70.45 E-value: 8.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGIKIE--GNVIYEGKNIysNNFDVLELRRKIGMVFQTPNPF 106
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIV-------GIWPPtsGSVRLDGADL--KQWDRETFGKHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 107 LMSIYDNISYgpkihgTKDKKTLDEIVEQSLIKSA------LWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:TIGR01842 405 PGTVAENIAR------FGENADPEKIIEAAKLAGVhelilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190
....*....|....*....|....*....|....
gi 224511529 181 DEPTSALDPISTGKIEELIINLK-ESYTIIIVTH 213
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKaRGITVVVITH 512
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-241 |
1.38e-13 |
|
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: 69.78 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 7 KPKNEIIIEtknlNLFY----TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlVeGI--KIEGNVIYEGK 80
Cdd:COG4618 326 RPKGRLSVE----NLTVvppgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL------V-GVwpPTAGSVRLDGA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 81 NIYSNNFDvlELRRKIGMVFQTPNPFLMSIYDNISygpkihgtkdkkTLDEIVEQSLIKSALWNEVKD-----------K 149
Cdd:COG4618 395 DLSQWDRE--ELGRHIGYLPQDVELFDGTIAENIA------------RFGDADPEKVVAAAKLAGVHEmilrlpdgydtR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 150 LNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMqQAGRISDRTAFF 228
Cdd:COG4618 461 IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVL 539
|
250
....*....|...
gi 224511529 229 LNGCIEEESPTDE 241
Cdd:COG4618 540 RDGRVQAFGPRDE 552
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-225 |
1.49e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 67.26 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYEGKniysnnfdvlelrRKIGMVFQ---T 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLK-------VLAGVLrpTSGTVRRAGG-------------ARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PNPFLMSIYDNISYG--PKI-----HGTKDKKTLDEIVEQSLIksalwnevkDKLNTNAL-SLSGGQQQRLCIARTLAIE 174
Cdd:NF040873 67 PDSLPLTVRDLVAMGrwARRglwrrLTRDDRAAVDDALERVGL---------ADLAGRQLgELSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224511529 175 PNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRT 225
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-224 |
1.55e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyEGKNIYsnnfdvlE 91
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGtILLRGQHI-EGLPGH-------Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKiGMV--FQTPNPFL-MSIYDNI-------SYGPKIHGTKDKKTLDEIVEQSLIKSALWNEV---KDKLNTNALSLS 158
Cdd:PRK11300 77 IARM-GVVrtFQHVRLFReMTVIENLlvaqhqqLKTGLFSGLLKTPAFRRAESEALDRAATWLERvglLEHANRQAGNLA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDR 224
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-214 |
3.28e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 15 ETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDlvEGIKI-EGNVIYEGKNIysnnfdvLEL- 92
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGH--PKYEVtSGSILLDGEDI-------LELs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 -----RRKIGMVFQTPNP--------FLMSIYDNISyGPKIHGTKDKKTLDEIVE-----QSLIKSALwNEvkdklntna 154
Cdd:COG0396 71 pderaRAGIFLAFQYPVEipgvsvsnFLRTALNARR-GEELSAREFLKLLKEKMKelgldEDFLDRYV-NE--------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 155 lSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHN 214
Cdd:COG0396 140 -GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPdRGILIITHY 199
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-260 |
3.93e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVE-----GIKIEGNVIYEGKNIYSnnFDVLELRRKIGMVFQTP 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGggaprGARVTGDVTLNGEPLAA--IDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NP-FLMSIYDNISYGPKIHGTKDKKTldEIVEQSLIKSALWNEVKDKL-NTNALSLSGGQQQRLCIARTLA--------- 172
Cdd:PRK13547 93 QPaFAFSAREIVLLGRYPHARRAGAL--THRDGEIAWQALALAGATALvGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 173 IEPNVILMDEPTSALDPISTGKIEELIINLKESYTI--IIVTHNMQQAGRISDRTAFFLNGCIEEESPtdelffnPKNTK 250
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHADRIAMLADGAIVAHGA-------PADVL 243
|
250
....*....|
gi 224511529 251 TEEYISGKFG 260
Cdd:PRK13547 244 TPAHIARCYG 253
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-213 |
6.43e-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: 64.87 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMNDLVEGiKIEgnvIYEGKNIYsnnfdvlelrrkigMVFQTPnpflmsiydnisYGPKihGT 123
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSG-RIG---MPEGEDLL--------------FLPQRP------------YLPL--GT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 124 kdkktLDEIVeqslikSALWNEVkdklntnalsLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIinLK 203
Cdd:cd03223 80 -----LREQL------IYPWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--KE 136
|
170
....*....|
gi 224511529 204 ESYTIIIVTH 213
Cdd:cd03223 137 LGITVISVGH 146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-224 |
7.75e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNL------------------NLF---YTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI-- 69
Cdd:COG4586 1 IIEVENLsktyrvyekepglkgalkGLFrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-------GIlv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 70 ------KIEGNVIYEGKNiysnnfdvlELRRKIGMVF----QtpnpfL---MSIYDNISYGPKIHGTKD---KKTLDEIV 133
Cdd:COG4586 74 ptsgevRVLGYVPFKRRK---------EFARRIGVVFgqrsQ-----LwwdLPAIDSFRLLKAIYRIPDaeyKKRLDELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 134 EQsliksaLwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIV 211
Cdd:COG4586 140 EL------L--DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLT 211
|
250
....*....|...
gi 224511529 212 THNMQQAGRISDR 224
Cdd:COG4586 212 SHDMDDIEALCDR 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-231 |
9.43e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIyegknIYSNNFDVLElrRKIGMVFQ---- 101
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGsILIDGQEM-----RFASTTAALA--AGVAIIYQelhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 102 TPNpflMSIYDNISYG--PKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNtnalSLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:PRK11288 91 VPE---MTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLK----YLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 180 MDEPTSALdpiSTGKIEEL--IIN-LK-ESYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:PRK11288 164 FDEPTSSL---SAREIEQLfrVIReLRaEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-223 |
1.08e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNI-YSNNFDVLElrRKIGMVFQTP 103
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLF-------GIyqKDSGSILFQGKEIdFKSSKEALE--NGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NPFLM-SIYDNISYG--PKIHGTKDKKTLDEivEQSLIKSALWNEVKDKLNTNALSLSggQQQRLCIARTLAIEPNVILM 180
Cdd:PRK10982 83 NLVLQrSVMDNMWLGryPTKGMFVDQDKMYR--DTKAIFDELDIDIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 224511529 181 DEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISD 223
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCD 202
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-246 |
2.62e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.95 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNR--MNDlvegikiEGNVIYEGKNiySNNFDVLEL-- 92
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArlAPD-------AGEVHYRMRD--GQLRDLYALse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 --RRKI-----GMVFQTPNPFL---MSIYDNIS-----YGPKIHGTKDKKTLD--EIVEQSLiksalwnevkDKLNTNAL 155
Cdd:PRK11701 81 aeRRRLlrtewGFVHQHPRDGLrmqVSAGGNIGerlmaVGARHYGDIRATAGDwlERVEIDA----------ARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESY--TIIIVTHNMQQAGRISDRTAFFLNGCI 233
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|...
gi 224511529 234 EEESPTDELFFNP 246
Cdd:PRK11701 231 VESGLTDQVLDDP 243
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-213 |
3.07e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK-ALNKINIKILKNSITALIGPSGCGKSTflrtlnrMNDLVEGIKI--EGNVIYEGKNIYSNNFDVL 90
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKST-------LASLLMGYYPltEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 elRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLdEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIART 170
Cdd:PRK10790 414 --RQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-224 |
3.77e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNiYSNNFDVLELR 93
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNIN-YNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPF-LMSIYDNISYG----PKIHGTK--DKKTLDEIVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLC 166
Cdd:PRK09700 80 LGIGIIYQELSVIdELTVLENLYIGrhltKKVCGVNiiDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDR 224
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDR 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-212 |
4.90e-12 |
|
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: 63.03 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNlFYTDFKA-----LNKINIKILKNSITALIGPSGCGKSTFLRTL-NRMNDLVegikIEGNVIYEGKNIYSNn 86
Cdd:cd03232 3 VLTWKNLN-YTVPVKGgkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGV----ITGEILINGRPLDKN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 87 fdvleLRRKIGMVFQTP--NPFLMsiydnisygpkihgtkdkktldeiVEQSLIKSALWNEvkdklntnalsLSGGQQQR 164
Cdd:cd03232 77 -----FQRSTGYVEQQDvhSPNLT------------------------VREALRFSALLRG-----------LSVEQRKR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVT 212
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCT 164
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-230 |
5.00e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 16 TKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNViyegkniysnnfdvlelrr 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGeVSIPKGL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 KIGMVFQTPNPFL-MSIYDNISYGPKiHGTKDKKTLDEIVEQSLIKSALWNEV--------------------------- 146
Cdd:COG0488 62 RIGYLPQEPPLDDdLTVLDTVLDGDA-ELRALEAELEELEAKLAEPDEDLERLaelqeefealggweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 147 --KDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKesYTIIIVTHnmqqagrisDR 224
Cdd:COG0488 141 fpEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP--GTVLVVSH---------DR 209
|
....*.
gi 224511529 225 taFFLN 230
Cdd:COG0488 210 --YFLD 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-231 |
6.21e-12 |
|
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: 65.32 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 21 LFYTDFK-----ALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVEGikiEGNVIYEGKNIYSNNFdvlelrrk 95
Cdd:TIGR01271 429 LFFSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSGRISFSPQT-------- 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 igmvfqtpnPFLM--SIYDNISYGpkihgtkdkKTLDEIVEQSLIKSALWNE------VKDK--LNTNALSLSGGQQQRL 165
Cdd:TIGR01271 496 ---------SWIMpgTIKDNIIFG---------LSYDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGITLSGGQRARI 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 166 CIARTLAIEPNVILMDEPTSALDPISTGKI-EELIINLKESYTIIIVTHNMQQAGRiSDRTAFFLNG 231
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
27-255 |
8.43e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.05 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvEGIKIEGNviyegkNIYSNNFDVLEL----RRK-----IG 97
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--DNWRVTAD------RMRFDDIDLLRLspreRRKlvghnVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 98 MVFQTPNPFL-------MSIYDNI-------SYGPKIHGTKDKKTldEIVEQSLIKsalwnEVKDKLNTNALSLSGGQQQ 163
Cdd:PRK15093 93 MIFQEPQSCLdpservgRQLMQNIpgwtykgRWWQRFGWRKRRAI--ELLHRVGIK-----DHKDAMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI--INLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDE 241
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtrLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
250
....*....|....
gi 224511529 242 LFFNPKNTKTEEYI 255
Cdd:PRK15093 246 LVTTPHHPYTQALI 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-255 |
1.10e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 1 MVKEKDKPKNEIIIETKNLNLFytDFKALNKINIKILKNSITALIGPSGCGKSTFlrtlnrMNDLVeGI--KIEGNVIYE 78
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTEL------MNCLF-GVdkRAGGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 79 GKNIY-SNNFDVLelrrKIGMVFQTP----NPFL--MSIYDNISYGPKI------------HGTKDKKTLDEIVEQSLIK 139
Cdd:PRK09700 324 GKDISpRSPLDAV----KKGMAYITEsrrdNGFFpnFSIAQNMAISRSLkdggykgamglfHEVDEQRTAENQRELLALK 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 140 SAlwnevkdKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQA 218
Cdd:PRK09700 400 CH-------SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEI 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 224511529 219 GRISDRTAFFLNGCIEEEsptdelfFNPKNTKTEEYI 255
Cdd:PRK09700 473 ITVCDRIAVFCEGRLTQI-------LTNRDDMSEEEI 502
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-242 |
1.18e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKNI-YSNNFDVLElrRKIGMVFQTP 103
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLT-------GIytRDAGSILYLGKEVtFNGPKSSQE--AGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 N--PFLmSIYDNISYGpkihgtkdkktlDEIVeqSLIKSALWNEVKD-------KLNTNALS------LSGGQQQRLCIA 168
Cdd:PRK10762 89 NliPQL-TIAENIFLG------------REFV--NRFGRIDWKKMYAeadkllaRLNLRFSSdklvgeLSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 169 RTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-231 |
1.55e-11 |
|
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: 63.69 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI----KIEGNVIYEGKNIYSNNFD 88
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS-------GVyphgTWDGEIYWSGSPLKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VLElRRKIGMVFQ----TPNpflMSIYDNISYGPKIHGTKDKKTLDEIVEQSlikSALWNEVKDKLNTNALS---LSGGQ 161
Cdd:TIGR02633 74 DTE-RAGIVIIHQeltlVPE---LSVAENIFLGNEITLPGGRMAYNAMYLRA---KNLLRELQLDADNVTRPvgdYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE-SYTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-221 |
2.36e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFlrtLNRMNDLVEGikiEGNVIYEGKNI--YSNNfdvlEL-RRKIGMVFQTPNPFLMSI--YDNIS 115
Cdd:PRK03695 24 ILHLVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPLeaWSAA----ELaRHRAYLSQQQTPPFAMPVfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 116 YGPKIHGTKDKKTLDEIVEQSLIksalwnevKDKLNTNALSLSGGQQQR-------LCIARTLAIEPNVILMDEPTSALD 188
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGL--------DDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 224511529 189 PISTGKIEELIINLKESYTIIIVT-----HNMQQAGRI 221
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSshdlnHTLRHADRV 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-212 |
2.43e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 30 NKINIKILKNSIT---------ALIGPSGCGKSTFLRTLnrMNDLVEGIKIEGNVIYEGKNIysnnfDVLELRRKIGMVF 100
Cdd:TIGR00955 33 RERPRKHLLKNVSgvakpgellAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI-----DAKEMRAISAYVQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 101 QTpNPFL--MSIYDNISYGPKI----HGTKDKKTL--DEIVEQ-SLIKSA-----LWNEVKdklntnalSLSGGQQQRLC 166
Cdd:TIGR00955 106 QD-DLFIptLTVREHLMFQAHLrmprRVTKKEKRErvDEVLQAlGLRKCAntrigVPGRVK--------GLSGGERKRLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 167 IARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVT 212
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
41-242 |
4.12e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIYSnnFDVLELRRKIGMVFQT-PNPFLMSIYDNISYG-- 117
Cdd:PRK10575 39 VTGLIGHNGSGKSTLLKMLGRHQP-----PSEGEILLDAQPLES--WSSKAFARKVAYLPQQlPAAEGMTVRELVAIGry 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 118 PkIHGT------KDKKTLDEIVEQSLIKSaLWNEVKDklntnalSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPIS 191
Cdd:PRK10575 112 P-WHGAlgrfgaADREKVEEAISLVGLKP-LAHRLVD-------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 224511529 192 TGKIEELIINLKE--SYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK10575 183 QVDVLALVHRLSQerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-223 |
5.54e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI----KIEGNVIYEGKNIYSN 85
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-------GVyphgTYEGEIIFEGEELQAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 NFDVLElRRKIGMVFQ----TPNpflMSIYDNISYGPKI--HGTKDkktLDEIVEQSlikSALWNEVKDKLNTNA--LSL 157
Cdd:PRK13549 75 NIRDTE-RAGIAIIHQelalVKE---LSVLENIFLGNEItpGGIMD---YDAMYLRA---QKLLAQLKLDINPATpvGNL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 158 SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISD 223
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISD 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-213 |
1.45e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 26 FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRmndLVEGIKIEGNVIYEGKNIYSNnfdvlelrrkigmvfqtpnp 105
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGRE-------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 flMSIYDNISygpkihgtkDKKTLDEIVEqsLIKSAlwnevkdKLNTNAL------SLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:COG2401 100 --ASLIDAIG---------RKGDFKDAVE--LLNAV-------GLSDAVLwlrrfkELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 224511529 180 MDEPTSALDPiSTGKIEELIINL---KESYTIIIVTH 213
Cdd:COG2401 160 IDEFCSHLDR-QTAKRVARNLQKlarRAGITLVVATH 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-192 |
1.47e-10 |
|
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: 59.20 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 24 TDFKALNKINIKILKN--------SITALIGPSGCGKSTFLRTLNrmNDLVEGIKIEGNVIYegkniysNNFDVLELRRK 95
Cdd:cd03233 10 SFTTGKGRSKIPILKDfsgvvkpgEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHY-------NGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 igmvfqtpnPFLMSIYDNISygpKIHgtkdKKTLdeIVEQSLIKSAlwnevkdKLNTNALS--LSGGQQQRLCIARTLAI 173
Cdd:cd03233 81 ---------YPGEIIYVSEE---DVH----FPTL--TVRETLDFAL-------RCKGNEFVrgISGGERKRVSIAEALVS 135
|
170
....*....|....*....
gi 224511529 174 EPNVILMDEPTSALDPIST 192
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTA 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-242 |
2.86e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNLnlfyTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI--KIEGNVIYEGKN 81
Cdd:COG1129 247 KRAAAPGEVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALF-------GAdpADSGEIRLDGKP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 82 IYSNNfdVLE-LRRKIGMVfqtpnP--------FL-MSIYDNI--------SYGPKIHGTKDKKTLDEIVEQSLIKSAlw 143
Cdd:COG1129 316 VRIRS--PRDaIRAGIAYV-----PedrkgeglVLdLSIRENItlasldrlSRGGLLDRRRERALAEEYIKRLRIKTP-- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 144 nevkdKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDpISTgK--IEELIINL-KESYTIIIVTHNMQQAGR 220
Cdd:COG1129 387 -----SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGA-KaeIYRLIRELaAEGKAVIVISSELPELLG 459
|
250 260
....*....|....*....|..
gi 224511529 221 ISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG1129 460 LSDRILVMREGRIVGELDREEA 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-213 |
4.99e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 9 KNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVegiKIEGNVIYEGKNIysNNFD 88
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYK---ILEGDILFKGESI--LDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 VlELRRKIG--MVFQTP--------NPFLMSIYDNisygpkIHGTKDKKTLDEIVEQSLIKSALwnevkDKLNTNALSL- 157
Cdd:CHL00131 78 P-EERAHLGifLAFQYPieipgvsnADFLRLAYNS------KRKFQGLPELDPLEFLEIINEKL-----KLVGMDPSFLs 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 158 -------SGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYT-IIIVTH 213
Cdd:CHL00131 146 rnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENsIILITH 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-213 |
5.32e-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: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYSNNfdVLELRRKIGMvfqtpnPFLMSIYDNISYGPKIHG 122
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDFQRDSIARG--LLYLGHAPGI------KTTLSVLENLRFWHADHS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 123 tkdkktlDEIVEQSLIKSALwNEVKDKLntnALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELII-N 201
Cdd:cd03231 103 -------DEQVEEALARVGL-NGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAgH 171
|
170
....*....|..
gi 224511529 202 LKESYTIIIVTH 213
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-216 |
6.91e-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: 57.94 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTD--FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMndlvegIKIEGNVIYEGKNIysNNFDVLE 91
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVSW--NSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 92 LRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKsalwnEVKDKLNTNALS----LSGGQQQRLCI 167
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIE-----QFPGQLDFVLVDggcvLSHGHKQLMCL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 224511529 168 ARTLAIEPNVILMDEPTSALDPISTGKIEEliiNLKESY---TIIIVTHNMQ 216
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRK---TLKQAFadcTVILSEHRIE 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-231 |
7.39e-10 |
|
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: 56.67 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 10 NEIIIETKNLnlfyTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGIK--IEGNVIYEGKNIYSNNF 87
Cdd:cd03215 1 GEPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-------GLRppASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 D---------VLELRRKIGMVFQtpnpflMSIYDNIsygpkihgtkdkktldeiveqsliksalwnevkdklnTNALSLS 158
Cdd:cd03215 70 RdairagiayVPEDRKREGLVLD------LSVAENI-------------------------------------ALSSLLS 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 159 GGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNG 231
Cdd:cd03215 107 GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-199 |
7.51e-10 |
|
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: 56.98 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 43 ALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGKNIYSNNfdVLELRRKIGMvfqtpNPFLmSIYDNISYGPKIH 121
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGTPLAEQRDEPHEN--ILYLGHLPGL-----KPEL-SALENLHFWAAIH 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 122 GTKDKKtldeiVEQSLIKSALwnevKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI 199
Cdd:TIGR01189 102 GGAQRT-----IEDALAAVGL----TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-231 |
8.83e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 8.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNLnlfyTDFK--ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKN 81
Cdd:PRK10982 241 DKENKPGEVILEVRNL----TSLRqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 82 I--------YSNNFD-VLELRRKIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIveQSLIKSAlwnEVKD-KLN 151
Cdd:PRK10982 312 InnhnaneaINHGFAlVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDT--QWVIDSM---RVKTpGHR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 152 TNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLN 230
Cdd:PRK10982 387 TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSN 466
|
.
gi 224511529 231 G 231
Cdd:PRK10982 467 G 467
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-231 |
9.68e-10 |
|
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: 57.56 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 20 NLFYTDFK-----ALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVEGikiEGNVIYEGKNIYSNNFDvlelrr 94
Cdd:cd03291 39 NLFFSNLClvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSGRISFSSQFS------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 kigmvfqtpnpFLM--SIYDNISYGpkihgtkdkKTLDEIVEQSLIKSALWNE------VKDK--LNTNALSLSGGQQQR 164
Cdd:cd03291 108 -----------WIMpgTIKENIIFG---------VSYDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 165 LCIARTLAIEPNVILMDEPTSALDPISTGKI-EELIINLKESYTIIIVTHNMQQAgRISDRTAFFLNG 231
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHL-KKADKILILHEG 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-243 |
1.44e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.20 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEGkniysnnfdvleLRRK-IGMVFQTPN- 104
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkISILGQPTRQA------------LQKNlVAYVPQSEEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 105 --PFLMSIYDNISYGPKIHG---TKDKKTLDEIVEQSLIKSalwnEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVIL 179
Cdd:PRK15056 90 dwSFPVLVEDVVMMGRYGHMgwlRRAKKRDRQIVTAALARV----DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 180 MDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISDRTAfFLNGCIEEESPTDELF 243
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTF 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-223 |
1.69e-09 |
|
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: 55.79 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 28 ALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndlvEGIKIEGNVIYEgkniysnnfDVLELRRKIGMVFqtpnpfl 107
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLI---------SFLPKFSRNKLIF------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 msiydnisygpkihgtkdkktLDEIveQSLIKSALwNEVKdkLNTNALSLSGGQQQRLCIARTLA--IEPNVILMDEPTS 185
Cdd:cd03238 65 ---------------------IDQL--QFLIDVGL-GYLT--LGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPST 118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224511529 186 ALDPISTGKIEELIINL-KESYTIIIVTHN---MQQAGRISD 223
Cdd:cd03238 119 GLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-213 |
2.65e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVegiKIEGNVIYEGKniysnnfDVLEL 92
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE---VTGGTVEFKGK-------DLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 R------RKIGMVFQTP-------NPFLMSIYDNisygpKIHGTKDKKTLDEIVEQSLI--KSALWNEVKDKLNTNA-LS 156
Cdd:PRK09580 71 SpedragEGIFMAFQYPveipgvsNQFFLQTALN-----AVRSYRGQEPLDRFDFQDLMeeKIALLKMPEDLLTRSVnVG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTH 213
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTH 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-228 |
2.72e-09 |
|
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: 55.88 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 36 ILKNSITALIGPSGCGKSTFLRTLnrmndlVEGIKIEGNviyegkniysnnfDVLELRRKIGMVFQTPNP-FLMSIYDNI 114
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKML------AGVLKPDEG-------------DIEIELDTVSYKPQYIKAdYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 115 SYGPKIHGTKDK-KTldEIVEQSLIKSALWNEVKDklntnalsLSGGQQQRLCIARTLAIEPNVILMDEPTSALDP---- 189
Cdd:cd03237 83 SSITKDFYTHPYfKT--EIAKPLQIEQILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrl 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 224511529 190 ISTGKIEELIINLKEsyTIIIVTHNMQQAGRISDRTAFF 228
Cdd:cd03237 153 MASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVF 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-215 |
4.43e-09 |
|
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: 56.88 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYT---DFkALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlvegiKIEGNVIYEGKNIysNNFDVL 90
Cdd:TIGR00957 1285 VEFRNYCLRYRedlDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI--AKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFLMSIYDNI----SYGpkihgtkdkktlDEIVEQSLIKSALWNEVK---DKLN----TNALSLSG 159
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLdpfsQYS------------DEEVWWALELAHLKTFVSalpDKLDhecaEGGENLSV 1424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNM 215
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-221 |
4.43e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFlrtLNRMNDLVEGIKIEGNVIYEGKNIYSnnfdvlELRRKIGMVFQTP--NPF 106
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRKPTK------QILKRTGFVTQDDilYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 107 LMS----IYDNISYGPKIHgTKDKKTLdeiVEQSLIKSALWNEVKDKL--NTNALSLSGGQQQRLCIARTLAIEPNVILM 180
Cdd:PLN03211 155 LTVretlVFCSLLRLPKSL-TKQEKIL---VAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224511529 181 DEPTSALDPISTGKIEELIINLKESYTiIIVTHNMQQAGRI 221
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-216 |
4.53e-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: 56.84 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 17 KNLNLFYTDF--KALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGnviyegknIYSNNFDVLELRR 94
Cdd:TIGR01271 1221 QGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG--------VSWNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 95 KIGMVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKsalwnEVKDKLN----TNALSLSGGQQQRLCIART 170
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIE-----QFPDKLDfvlvDGGYVLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEEliiNLKESY---TIIIVTHNMQ 216
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRK---TLKQSFsncTVILSEHRVE 1413
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
157-224 |
4.74e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 4.74e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQAGRISDR 224
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGMSDR 464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-246 |
7.88e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDlVEGikieGNVIYEGKNIYSnnFDVLELRRKIGMVFQTPNPFLM 108
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-VCG----GEIRVNGREIGA--YGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 SIYDNISygPKIHGTKDKK-------TLDEIV--EQSLIKSalwnevkdKLNTNALSLSGGQQQRLCIARTLAIEPN-VI 178
Cdd:PTZ00243 1399 TVRQNVD--PFLEASSAEVwaalelvGLRERVasESEGIDS--------RVLEGGSNYSVGQRQLMCMARALLKKGSgFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 179 LMDEPTSALDPISTGKIEELIINLKESYTIIIVTHNMQQAGRIsDRTAFFLNGCIEEESPTDELFFNP 246
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-223 |
8.23e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 21 LFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYE------GKNIYSNNFD-VLEL 92
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGrIIYEQDLIVArlqqdpPRNVEGTVYDfVAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMvfqtpnpfLMSIYDNISYgpKIHGTKDKKTLDEI--VEQSLIKSALW------NEVKDKLNTNA---LS-LSGG 160
Cdd:PRK11147 91 IEEQAE--------YLKRYHDISH--LVETDPSEKNLNELakLQEQLDHHNLWqlenriNEVLAQLGLDPdaaLSsLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDpISTgkIEELIINLKE-SYTIIIVTH------NMqqAGRISD 223
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirNM--ATRIVD 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-216 |
1.67e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 12 IIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlVEGIKIEGNVIYEGKNIYSNNFD--- 88
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM------LGQLQADSGRIHCGTKLEVAYFDqhr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 89 -VLELRRkigmvfqtpnpflmSIYDNISYGPK---IHGtKDKKTLDEIveQSLI---KSALwNEVKdklntnalSLSGGQ 161
Cdd:PRK11147 392 aELDPEK--------------TVMDNLAEGKQevmVNG-RPRHVLGYL--QDFLfhpKRAM-TPVK--------ALSGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 162 QQRLCIARTLAIEPNVILMDEPTSALDpistgkIE--ELIINLKESY--TIIIVTHNMQ 216
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLD------VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-215 |
2.24e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 38 KNSITALIGPSGCGKSTFLRTLN-----RMNDLVEGIKIEgNVI--YEG-------KNIYSNNFDVLelrRKIGMVFQTP 103
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEPSWD-EVLkrFRGtelqnyfKKLYNGEIKVV---HKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 NPFLMSIYDNISygpkihGTKDKKTLDEIVEQSLIKSALWNEVKDklntnalsLSGGQQQRLCIARTLAIEPNVILMDEP 183
Cdd:PRK13409 174 KVFKGKVRELLK------KVDERGKLDEVVERLGLENILDRDISE--------LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 224511529 184 TSALDPISTGKIEELIINLKESYTIIIVTHNM 215
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-245 |
2.42e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNlFYTDFK----ALNKINIKILKNSITALIGPSGCGK----STFLRTLNRMNDlvEGIKIEGNVIYegkniysn 85
Cdd:PLN03232 615 ISIKNGY-FSWDSKtskpTLSDINLEIPVGSLVAIVGGTGEGKtsliSAMLGELSHAET--SSVVIRGSVAY-------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 nfdvlelrrkigmVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQ---SLIKSALWNEVKDKlntnALSLSGGQQ 162
Cdd:PLN03232 684 -------------VPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQhdlDLLPGRDLTEIGER----GVNISGGQK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALDP-ISTGKIEELIINLKESYTIIIVTHNMQQAGRIsDRTAFFLNGCIEEESPTDE 241
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAE 825
|
....
gi 224511529 242 LFFN 245
Cdd:PLN03232 826 LSKS 829
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-213 |
2.74e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLnrMNDLVEGikiegnviyEGKNIY 83
Cdd:PRK15064 310 EQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---------SGTVKW 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 84 SNNfdvlelrRKIGMVFQTPNPFL---MSIYDNISygpKIHGTKDkktlDEIVEQSLIKSALWNEvkDKLNTNALSLSGG 160
Cdd:PRK15064 379 SEN-------ANIGYYAQDHAYDFendLTLFDWMS---QWRQEGD----DEQAVRGTLGRLLFSQ--DDIKKSVKVLSGG 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPIStgkIEELIINLkESY--TIIIVTH 213
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMAL-EKYegTLIFVSH 493
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-215 |
3.74e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNVIYEgkniysnnFDVLELRRKIGMVFQTPNPFLMSIYDNISYGPKiHG 122
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGrIMIDDCDVAK--------FGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSE-HN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 123 TKDkktLDEIVEQSLIKSALWNE---VKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI 199
Cdd:PLN03232 1338 DAD---LWEALERAHIKDVIDRNpfgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
170
....*....|....*.
gi 224511529 200 INLKESYTIIIVTHNM 215
Cdd:PLN03232 1415 REEFKSCTMLVIAHRL 1430
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
29-213 |
5.09e-08 |
|
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: 52.60 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLvegikIEGNVIYEGKNIysNNFDVLELRRKIGMVFQTPNPFLM 108
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHTLRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 SIYDNISygpkihgtKDKKTLDEIVEQSLIKSALWNEVK------DKLNTNA-LSLSGGQQQRLCIARTLAIEPNVILMD 181
Cdd:cd03288 110 SIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKslpgglDAVVTEGgENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190
....*....|....*....|....*....|..
gi 224511529 182 EPTSALDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:cd03288 182 EATASIDMATENILQKVVMTAFADRTVVTIAH 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-242 |
5.87e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIKIE--GNVIYEGKNiYSNNFDVL 90
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMK-------IIAGIVPPdsGTLEIGGNP-CARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 ELRRKIGMVFQTPNPFL-MSIYDNISYG-PKihGTKDKKTLDEIVEQslIKSALwnevkdKLNTNALSLSGGQQQRLCIA 168
Cdd:PRK15439 83 AHQLGIYLVPQEPLLFPnLSVKENILFGlPK--RQASMQKMKQLLAA--LGCQL------DLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 169 RTLAIEPNVILMDEPTSALDPIST----GKIEELiinLKESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETerlfSRIREL---LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-224 |
6.92e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTD---FKALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmnDLVEGiKIEGNVIYEGKNIYSNNF 87
Cdd:TIGR02633 255 DVILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALF---GAYPG-KFEGNVFINGKPVDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 D---------VLELRRKIGMVFQtpnpflMSIYDNISYGPKIHGTKdKKTLDEIVEQSLIKSALwNEVKDKLNTNAL--- 155
Cdd:TIGR02633 331 AqairagiamVPEDRKRHGIVPI------LGVGKNITLSVLKSFCF-KMRIDAAAELQIIGSAI-QRLKVKTASPFLpig 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDR 224
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDR 472
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-222 |
7.41e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 8 PKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTflrTLNRMNDLVEGIkiEGNVIYEGKNIYSNNf 87
Cdd:NF033858 261 DDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST---TMKMLTGLLPAS--EGEAWLFGQPVDAGD- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 dvLELRRKIGMVFQTpnpFlmSIYDNIS-----------YGpkIHGTKDKKTLDEIVEQ-SLIksalwnEVKDKLnTNAL 155
Cdd:NF033858 335 --IATRRRVGYMSQA---F--SLYGELTvrqnlelharlFH--LPAAEIAARVAEMLERfDLA------DVADAL-PDSL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 156 SLsgGQQQRLCIArtLAI--EPNVILMDEPTSALDPISTGKIEELIINL--KESYTIIIVTHNMQQAG---RIS 222
Cdd:NF033858 399 PL--GIRQRLSLA--VAVihKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAErcdRIS 468
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-242 |
1.70e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 32 INIKILKNSITALIGPSGCGKSTFLRTLnrmndlvEGIK--IEGNVIYEGKNIysNNFDVLElRRKIGMVF-----QTPN 104
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETL-------YGLRpaRGGRIMLNGKEI--NALSTAQ-RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 105 PFL-MSIYDNIS---YGPK---IHGTKDKKTLDEIVEQSLIKsalWNEVKDKLNTnalsLSGGQQQRLCIARTLAIEPNV 177
Cdd:PRK15439 352 LYLdAPLAWNVCaltHNRRgfwIKPARENAVLERYRRALNIK---FNHAEQAART----LSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 178 ILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
29-213 |
1.90e-07 |
|
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: 51.67 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG---IKIEGNVIYegkniysnnfdvlelrrkigmVFQTPNP 105
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGrltKPAKGKLFY---------------------VPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 FLMSIYDNISYGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALS-----LSGGQQQRLCIARTLAIEPNVILM 180
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|...
gi 224511529 181 DEPTSALDPISTGKIEELIINLKesYTIIIVTH 213
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLCREFG--ITLFSVSH 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-224 |
2.26e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 4 EKDKPKNEIIIETKNLNLFYTDFKaLNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlVEGIK-IEGNVIYEGKNI 82
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLL------AGVLKpDEGEVDPELKIS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 83 Y-----SNNFDVlelrrkigmvfqTPNPFLMSIYDNISygpkihgtkdkktldeiveqsliKSALWNEVKDKLNTNAL-- 155
Cdd:PRK13409 404 YkpqyiKPDYDG------------TVEDLLRSITDDLG-----------------------SSYYKSEIIKPLQLERLld 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 156 ----SLSGGQQQRLCIARTLAIEPNVILMDEPTSALD---PISTGKIEELIINLKESyTIIIVTHNMQQAGRISDR 224
Cdd:PRK13409 449 knvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRIAEEREA-TALVVDHDIYMIDYISDR 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-213 |
2.45e-07 |
|
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: 51.09 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 8 PKNEIIietKNLNL-FYTDfkalNKINIkilknsitalIGPSGCGKSTFLRtlnrmndLVEGIKIEgnviYEGKNIYSNN 86
Cdd:TIGR03719 16 PKKEIL---KDISLsFFPG----AKIGV----------LGLNGAGKSTLLR-------IMAGVDKD----FNGEARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 87 FdvlelrrKIGMVFQTP--NPFLmSIYDNISYGpkIHGTKDK-KTLDEIVE-------------------QSLIKSA-LW 143
Cdd:TIGR03719 68 I-------KVGYLPQEPqlDPTK-TVRENVEEG--VAEIKDAlDRFNEISAkyaepdadfdklaaeqaelQEIIDAAdAW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 144 N-EVKDKLNTNAL----------SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKEsyTIIIVT 212
Cdd:TIGR03719 138 DlDSQLEIAMDALrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVT 215
|
.
gi 224511529 213 H 213
Cdd:TIGR03719 216 H 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-242 |
2.49e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFY---TDFKALNKINIKILKNSITALIGPSGCGkstflRTlnrmnDLVEGI------KIEGNVIYEGKN 81
Cdd:PRK13549 257 EVILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAG-----RT-----ELVQCLfgaypgRWEGEIFIDGKP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 82 IYSNNFD---------VLELRRKIGMVfqtpnPfLMSIYDNI---SYGPKIHGTkdkkTLDEIVEQSLIKSALwNEVKDK 149
Cdd:PRK13549 327 VKIRNPQqaiaqgiamVPEDRKRDGIV-----P-VMGVGKNItlaALDRFTGGS----RIDDAAELKTILESI-QRLKVK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 150 LNTNAL---SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTHNMQQAGRISDRT 225
Cdd:PRK13549 396 TASPELaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRV 475
|
250
....*....|....*..
gi 224511529 226 AFFLNGCIEEESPTDEL 242
Cdd:PRK13549 476 LVMHEGKLKGDLINHNL 492
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
65-242 |
3.03e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 65 LVEGI----KIE-GNVIYEGKNIysNNFDVLELRR-----------KIGMVfqtPNpflMSIYDNI----SYGPKI--HG 122
Cdd:COG3845 300 LAEALaglrPPAsGSIRLDGEDI--TGLSPRERRRlgvayipedrlGRGLV---PD---MSVAENLilgrYRRPPFsrGG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 123 TKDKKTLDEIVEQsLIKSAlwnEVK-DKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIIN 201
Cdd:COG3845 372 FLDRKAIRAFAEE-LIEEF---DVRtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224511529 202 LKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESPTDEL 242
Cdd:COG3845 448 LRDAgAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-259 |
3.39e-07 |
|
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: 51.17 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 24 TDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGikiegNVIYEGKNIYSNnfdVLELRRKIGMVFQ-T 102
Cdd:TIGR01257 1950 TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATVAGKSILTN---ISDVHQNMGYCPQfD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 103 PNPFLMSIYDNISYGPKIHGTKDKKTldEIVEQSLIKSALWNEVKDKLntnALSLSGGQQQRLCIARTLAIEPNVILMDE 182
Cdd:TIGR01257 2022 AIDDLLTGREHLYLYARLRGVPAEEI--EKVANWSIQSLGLSLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDE 2096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 183 PTSALDPISTGKIEELIIN-LKESYTIIIVTHNMQQAGRISDRTAFFLNGC---------------------IEEESPTD 240
Cdd:TIGR01257 2097 PTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKGAfqclgtiqhlkskfgdgyivtMKIKSPKD 2176
|
250
....*....|....*....
gi 224511529 241 ELFfnPKNTKTEEYISGKF 259
Cdd:TIGR01257 2177 DLL--PDLNPVEQFFQGNF 2193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-202 |
3.72e-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: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 3 KEKDKPKNEIIIETKNLNlfYTdfkalnkINIK-----ILKN--------SITALIGPSGCGKSTFLRTL-NRMNdlvEG 68
Cdd:TIGR00956 749 KDMEKESGEDIFHWRNLT--YE-------VKIKkekrvILNNvdgwvkpgTLTALMGASGAGKTTLLNVLaERVT---TG 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 69 IKIEGNVIYEGKNIYSNnfdvleLRRKIGMVFQTP-------------------NPFLMSIYDNISYGPKIHgtkdkktl 129
Cdd:TIGR00956 817 VITGGDRLVNGRPLDSS------FQRSIGYVQQQDlhlptstvreslrfsaylrQPKSVSKSEKMEYVEEVI-------- 882
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224511529 130 dEIVEQSLIKSALWNEVKDKLNTNalslsggQQQRLCIARTLAIEPNVIL-MDEPTSALDPISTGKIEELIINL 202
Cdd:TIGR00956 883 -KLLEMESYADAVVGVPGEGLNVE-------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-215 |
3.82e-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: 49.67 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRTLNrmNDLVEGIKIEGN------VI--YEGKNIySNNF-----DVLELRRKIGMVFQTPNPFL 107
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILA--GKLKPNLGKFDDppdwdeILdeFRGSEL-QNYFtklleGDVKVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 108 MSIYDNISygpkihGTKDKKTLDEIVEQSLIKSALWNEVKDklntnalsLSGGQQQRLCIARTLAIEPNVILMDEPTSAL 187
Cdd:cd03236 105 GKVGELLK------KKDERGKLDELVDQLELRHVLDRNIDQ--------LSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*....
gi 224511529 188 DPISTGKIEELIINL-KESYTIIIVTHNM 215
Cdd:cd03236 171 DIKQRLNAARLIRELaEDDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-188 |
4.47e-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: 50.55 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 38 KNSITALIGPSGCGKSTFLRTLNrmndlvegikieGNVI-----YEGKNIYSnnfDVLELRRkiGMVFQTpnpFLMSIYD 112
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILS------------GELKpnlgdYDEEPSWD---EVLKRFR--GTELQD---YFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 113 N----------ISYGPKIH---------GTKDKKTLDEIVEQSLIKSALWNEVKDklntnalsLSGGQQQRLCIARTLAI 173
Cdd:COG1245 158 GeikvahkpqyVDLIPKVFkgtvrelleKVDERGKLDELAEKLGLENILDRDISE--------LSGGELQRVAIAAALLR 229
|
170
....*....|....*
gi 224511529 174 EPNVILMDEPTSALD 188
Cdd:COG1245 230 DADFYFFDEPSSYLD 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-213 |
5.81e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLRTLnrmndlvegikiegnviyegkniySNNFDVLELR----RKIGMVFQtpN 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSL------------------------LSQFEISEGRvwaeRSIAYVPQ--Q 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 105 PFLM--SIYDNISYgpkiHGTKDKKTLDEIVEQS-------LIKSALWNEVKDKlntnALSLSGGQQQRLCIARTLAIEP 175
Cdd:PTZ00243 730 AWIMnaTVRGNILF----FDEEDAARLADAVRVSqleadlaQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANR 801
|
170 180 190
....*....|....*....|....*....|....*....
gi 224511529 176 NVILMDEPTSALDP-ISTGKIEELIINLKESYTIIIVTH 213
Cdd:PTZ00243 802 DVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATH 840
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-225 |
1.05e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 27 KALNKINIKILKNSITALIGPSGCGKSTFLRTLNrmndlveGI----KIEGNVIYEG-----KNIYSNNfdvlelRRKIG 97
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-------GVyphgSYEGEILFDGevcrfKDIRDSE------ALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 98 MVFQ----TPnpfLMSIYDNISYGpkihgtkdkktlDEIVEQSLIKsalWNEVKDK---------LNTNALSLSG----G 160
Cdd:NF040905 82 IIHQelalIP---YLSIAENIFLG------------NERAKRGVID---WNETNRRarellakvgLDESPDTLVTdigvG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRT 225
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSI 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
157-224 |
1.12e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDR 224
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADR 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
154-242 |
1.31e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 154 ALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKI-EELIINLKESYTIIIVTHNMQQAGRISDRTAFFLNGC 232
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
90
....*....|
gi 224511529 233 IEEESPTDEL 242
Cdd:NF000106 222 VIADGKVDEL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-188 |
1.50e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNlFYTDFKA----LNKINIKILKNSITALIGPSGCGK----STFLRTLNRMNDlvegikieGNVIYEGKNIYsn 85
Cdd:PLN03130 615 ISIKNGY-FSWDSKAerptLSNINLDVPVGSLVAIVGSTGEGKtsliSAMLGELPPRSD--------ASVVIRGTVAY-- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 86 nfdvlelrrkigmVFQTPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQ---SLIKSALWNEVKDKlntnALSLSGGQQ 162
Cdd:PLN03130 684 -------------VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQhdlDLLPGGDLTEIGER----GVNISGGQK 746
|
170 180
....*....|....*....|....*.
gi 224511529 163 QRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-213 |
1.73e-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: 48.78 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNViyegkniysnnfdv 89
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGtIEIGETV-------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 90 lelrrKIGMVFQT-----PNPflmSIYDNISYGpkihgtkdkktLDEIV---------------------EQSLIKSalw 143
Cdd:TIGR03719 386 -----KLAYVDQSrdaldPNK---TVWEEISGG-----------LDIIKlgkreipsrayvgrfnfkgsdQQKKVGQ--- 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 144 nevkdklntnalsLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESYTII---------IVTH 213
Cdd:TIGR03719 444 -------------LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVIshdrwfldrIATH 509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-213 |
2.51e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 44 LIGPSGCGKSTFLRTLNRmndLVEgikIE-GNVIYEGKNIysNNFDVLELRRKIGMVFQTPNPFLMSIYDNisygpkihg 122
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFR---IVE---LErGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSGTVRFN--------- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 123 tkdkktLDEIVEQSliKSALWN-----EVKDKLNTNALSL-----------SGGQQQRLCIARTLAIEPNVILMDEPTSA 186
Cdd:PLN03130 1333 ------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180
....*....|....*....|....*..
gi 224511529 187 LDPISTGKIEELIINLKESYTIIIVTH 213
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAH 1431
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-231 |
2.58e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 8 PKNEIIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIKIEGnviyegkniYSNNF 87
Cdd:PRK10938 255 PANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-------SLITGDHPQG---------YSNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 88 DVLELRRKIGmvfQTpnpfLMSIYDNISY-GPKIHgtkdkktLDEIVEQSL---IKSA------LWNEVKDKLNTNAL-- 155
Cdd:PRK10938 319 TLFGRRRGSG---ET----IWDIKKHIGYvSSSLH-------LDYRVSTSVrnvILSGffdsigIYQAVSDRQQKLAQqw 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 ----------------SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELI-INLKESYT-IIIVTHNMQQ 217
Cdd:PRK10938 385 ldilgidkrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdVLISEGETqLLFVSHHAED 464
|
250
....*....|....*
gi 224511529 218 AGR-ISDRTAFFLNG 231
Cdd:PRK10938 465 APAcITHRLEFVPDG 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-224 |
2.76e-06 |
|
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: 47.86 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 35 KILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGiKIEGNViyegkniysnnfdvlelrrkigmvfqtpnpflmsiydNI 114
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-EVDEDL-------------------------------------KI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 115 SYGP-----KIHGTKDKkTLDEIVEQSLIKSALWNEVKDKLNTNAL------SLSGGQQQRLCIARTLAIEPNVILMDEP 183
Cdd:COG1245 404 SYKPqyispDYDGTVEE-FLRSANTDDFGSSYYKTEIIKPLGLEKLldknvkDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224511529 184 TSALD---PISTGKIeelIINLKESY--TIIIVTHNMQQAGRISDR 224
Cdd:COG1245 483 SAHLDveqRLAVAKA---IRRFAENRgkTAMVVDHDIYLIDYISDR 525
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-213 |
2.83e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIinLKESYTIIIVTH 213
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-215 |
9.40e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.49 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKniysnnfdvl 90
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR-------VVLGLvaPDEGVIKRNGK---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 eLRrkIGMVFQ----------TPNPFLMsiydnisYGPKIHGTKDKKTLDEIVEQSLIKSALWNevkdklntnalsLSGG 160
Cdd:PRK09544 67 -LR--IGYVPQklyldttlplTVNRFLR-------LRPGTKKEDILPALKRVQAGHLIDAPMQK------------LSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 161 QQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNM 215
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-188 |
2.11e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 12 IIIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEG-IKIEGNViyegkniysnnfdvl 90
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGtIKIGETV--------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 elrrKIGMVFQT-----PNPflmSIYDNISYGpkihgtkdkktLDEI-VEQSLIKS----ALWN--------EVKDklnt 152
Cdd:PRK11819 388 ----KLAYVDQSrdaldPNK---TVWEEISGG-----------LDIIkVGNREIPSrayvGRFNfkggdqqkKVGV---- 445
|
170 180 190
....*....|....*....|....*....|....*.
gi 224511529 153 nalsLSGGQQQRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:PRK11819 446 ----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-188 |
3.77e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 11 EIIIETKNLNLF---YTDFKALNKINIKILKNSITALIGPSGCGK-----STFLRTLnrmndlveGIKIEGNVIYEGKNI 82
Cdd:NF040905 255 EVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSY--------GRNISGTVFKDGKEV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 83 YSNNFD---------VLELRRKIGMVFqtpnpfLMSIYDNISyGPKIHGTKDKKTLDEIVEqslIKSAlwNEVKDKLNTN 153
Cdd:NF040905 327 DVSTVSdaidaglayVTEDRKGYGLNL------IDDIKRNIT-LANLGKVSRRGVIDENEE---IKVA--EEYRKKMNIK 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 224511529 154 ALS-------LSGGQQQRLCIARTLAIEPNVILMDEPTSALD 188
Cdd:NF040905 395 TPSvfqkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
5.49e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 18 NLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGI--KIEGNVIYEGKNIysnNFDVLELRRK 95
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLK-------LIAGLlnPEKGEILFERQSI---KKDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 96 IGMVFQTP--NPFLmSIYDNISYgpKIHGTKDKKTLDEIVeqSLIKsalwneVKDKLNTNALSLSGGQQQRLCIARTLAI 173
Cdd:PRK13540 76 LCFVGHRSgiNPYL-TLRENCLY--DIHFSPGAVGITELC--RLFS------LEHLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170 180
....*....|....*....|....*...
gi 224511529 174 EPNVILMDEPTSALDPIS----TGKIEE 197
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSlltiITKIQE 172
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
41-188 |
6.20e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRTL--NRMNDLVEG-IKIEG-----------NVIYEGKNIYSNNFDVLElrrkigmvfqtpnpf 106
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLagRKTGGYIEGdIRISGfpkkqetfariSGYCEQNDIHSPQVTVRE--------------- 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 107 lMSIYDNISYGPKIHGTKDKKT-LDEIVEqsLIKsalWNEVKDKLN--TNALSLSGGQQQRLCIARTLAIEPNVILMDEP 183
Cdd:PLN03140 973 -SLIYSAFLRLPKEVSKEEKMMfVDEVME--LVE---LDNLKDAIVglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 224511529 184 TSALD 188
Cdd:PLN03140 1047 TSGLD 1051
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
156-255 |
7.58e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVI--LMDEPTSALDPISTGKIEELIINLK-ESYTIIIVTHNMQQ---AGRISD---RTA 226
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMislADRIIDigpGAG 555
|
90 100
....*....|....*....|....*....
gi 224511529 227 FFLNGCIEEESPTDelFFNPKNTKTEEYI 255
Cdd:PRK00635 556 IFGGEVLFNGSPRE--FLAKSDSLTAKYL 582
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
150-223 |
8.23e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 150 LNTNALSLSGGQQQRLCIARTLAIEPNVIL--MDEPTSALDPISTGKIEELIINLKE-SYTIIIVTHN---MQQAGRISD 223
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDedtIRAADHVID 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-228 |
9.54e-05 |
|
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: 42.17 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 143 WNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKE--SYTIIIVTHNMQQAGR 220
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDY 137
|
....*...
gi 224511529 221 ISDRTAFF 228
Cdd:cd03222 138 LSDRIHVF 145
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-242 |
1.23e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 5 KDKPKNEIIIETKNlnlfyTDFKALNKINIKILKNSITALIGPSGCGKSTflrtlnrMNDLVEGI--KIEGNVIYEGkni 82
Cdd:PRK13546 21 KERMKDALIPKHKN-----KTFFALDDISLKAYEGDVIGLVGINGSGKST-------LSNIIGGSlsPTVGKVDRNG--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 83 ysnnfDVLELRRKIGMVFQtpnpflMSIYDNISYGPKIHGTKDK---KTLDEIVEQSLIKSALWNEVKdklntnalSLSG 159
Cdd:PRK13546 86 -----EVSVIAISAGLSGQ------LTGIENIEFKMLCMGFKRKeikAMTPKIIEFSELGEFIYQPVK--------KYSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 160 GQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNMQQAGRISDRTAFFLNGCIEEESP 238
Cdd:PRK13546 147 GMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQnKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
....
gi 224511529 239 TDEL 242
Cdd:PRK13546 227 LDDV 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-227 |
1.39e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 38 KNSITALIGPSGCGKSTFLRTLnrmndlvegikiegnviyeGKNIYSNNFDVLELrrkigmvfqtpnpflmsiydnisyg 117
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-------------------ARELGPPGGGVIYI------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 118 pkihgtkdkkTLDEIVEQsliksALWNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEE 197
Cdd:smart00382 37 ----------DGEDILEE-----VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190
....*....|....*....|....*....|....*..
gi 224511529 198 LI-------INLKESYTIIIVTHNMQQAGRISDRTAF 227
Cdd:smart00382 102 LEelrllllLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-212 |
1.39e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 22 FYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGIK--IEGNVIYegKNIYSNNFdvlelrrkigmv 99
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLR-------MIAGIMqpSSGNIYY--KNCNINNI------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 100 fqtPNPFLMSIYDNISYGPKIHGTKDKKTLDEIVEQS-LIKSAL-WNEVKDKLNTNALSLSGGQQQRLCIARTLAIEPNV 177
Cdd:PRK13541 68 ---AKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAeTLYAAIhYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190
....*....|....*....|....*....|....*
gi 224511529 178 ILMDEPTSALDPISTGKIEELIINLKESYTIIIVT 212
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLS 179
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
26-213 |
1.78e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 26 FKALNKINIKILKNsITALIGPSGCGKSTFLRTLNRMNDLVEGIKIEGNVIYEGKNIYSNNFDV-LELRRKIGMVFQTP- 103
Cdd:COG3593 11 FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIeLTFGSLLSRLLRLLl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 -------------------NPFLMSIYDNIS-YGPKIHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQ 163
Cdd:COG3593 90 keedkeeleealeelneelKEALKALNELLSeYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 224511529 164 RLCIARTLAI-------EPNVILMDEPTSALDPISTGKIEELIINL-KESYTIIIVTH 213
Cdd:COG3593 170 LILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTH 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-221 |
2.17e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFK-ALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNdlvegIKIEGNVIYEGKNIYSNNFDvlEL 92
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKPVTAEQPE--DY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 93 RRKIGMVFQTPNPFlmsiydnisygPKIHGTKDKKTLDEIVEQSLIKSALWN--EVKDKLNTNaLSLSGGQQQRLCIART 170
Cdd:PRK10522 396 RKLFSAVFTDFHLF-----------DQLLGPEGKPANPALVEKWLERLKMAHklELEDGRISN-LKLSKGQKKRLALLLA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 171 LAIEPNVILMDEPTSALDPISTgKI--EELIINLKES-YTIIIVTHN---MQQAGRI 221
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFR-REfyQVLLPLLQEMgKTIFAISHDdhyFIHADRL 519
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
26-68 |
3.00e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 3.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 224511529 26 FKALNKINIKIlkNSITALIGPSGCGKSTFLRTLNRMNDLVEG 68
Cdd:COG4637 10 FKSLRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARG 50
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-214 |
3.61e-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: 40.04 E-value: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224511529 157 LSGGQQQRLCIARTLAIEPN----VILMDEPTSALDPISTGKIEELII-NLKESYTIIIVTHN 214
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHL 140
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
156-215 |
5.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 156 SLSGGQQQRLCIARTL---AIEPNVILMDEPTSALdpiSTGKIEELIINLK----ESYTIIIVTHNM 215
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM 872
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
157-213 |
6.15e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 6.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 224511529 157 LSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEEliiNLKEsY--TIIIVTH 213
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ---FLHD-YpgTVVAVTH 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
75-215 |
8.62e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 75 VIYEGKNIysnnFDVLElrrkigmvfqtpnpflMSIY------DNIsygPKIHgtKDKKTLDEIVEQSLiksalwnevkd 148
Cdd:TIGR00630 778 VKYKGKNI----ADVLD----------------MTVEeayeffEAV---PSIS--RKLQTLCDVGLGYI----------- 821
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224511529 149 KLNTNALSLSGGQQQRLCIARTL---AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNM 215
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL 892
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
41-213 |
1.05e-03 |
|
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: 39.13 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 41 ITALIGPSGCGKSTFLRTL-----------NRMNDLVEGIKIEGNVIYEGKNIYSNNFDV-LELRRKigmvfqtpnpflM 108
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkyaltgelppnSKGGAHDPKLIREGEVRAQVKLAFENANGKkYTITRS------------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 109 SIYDNISYgpkIH-GTKDKKTLDEIVeqsliksalwnevkdklntnalSLSGGQQQ------RLCIARTLAIEPNVILMD 181
Cdd:cd03240 92 AILENVIF---CHqGESNWPLLDMRG----------------------RCSGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 224511529 182 EPTSALDPistGKIEELIINLKESYT------IIIVTH 213
Cdd:cd03240 147 EPTTNLDE---ENIEESLAEIIEERKsqknfqLIVITH 181
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
148-214 |
1.20e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 148 DKLNTNALSLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELIINLKESytIIIVTHN 214
Cdd:PRK10636 422 DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA--LVVVSHD 486
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-59 |
2.12e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.15 E-value: 2.12e-03
10 20
....*....|....*....|....*
gi 224511529 35 KILKNSITALIGPSGCGKSTFLRTL 59
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNAL 105
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-188 |
2.28e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 26 FKALNkinIKILKNSITALIGPSGCGKSTFLRtlnrmndLVEGikiegnviyegkniysnnfdvlELRRKIGMVFQTPNp 105
Cdd:PLN03073 525 FKNLN---FGIDLDSRIAMVGPNGIGKSTILK-------LISG----------------------ELQPSSGTVFRSAK- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 106 FLMSIYD-------NISYGPKIHGTKdkkTLDEIVEQSLIKSALWNEVKDKLNTNAL-SLSGGQQQRLCIARTLAIEPNV 177
Cdd:PLN03073 572 VRMAVFSqhhvdglDLSSNPLLYMMR---CFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHI 648
|
170
....*....|.
gi 224511529 178 ILMDEPTSALD 188
Cdd:PLN03073 649 LLLDEPSNHLD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-259 |
2.36e-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: 39.23 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 150 LNTNALSLSGGQQQRLCIARTLAIEPNVIL--MDEPTSALDPISTGKIEELIINLKE-SYTIIIVTHN---MQQAGRISD 223
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVVEHDedtIRAADYVID 561
|
90 100 110
....*....|....*....|....*....|....*...
gi 224511529 224 --RTAFFLNGCIEEESPTDELFFNPKNTkTEEYISGKF 259
Cdd:TIGR00630 562 igPGAGEHGGEVVASGTPEEILANPDSL-TGQYLSGRK 598
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
14-214 |
3.46e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 14 IETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLRTLNRMNDLVEGIkiegnviYEGKNIYSNNFDVLELR 93
Cdd:pfam13304 106 EREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGL-------LLEDWAVLDLAADLALF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 94 RKIGMVFQTPNPFLMSIYDNISygpkiHGTKDKKTLDEIVEQSLIKSALWNEVKDKLNTNALSLSGGQQQRLCIA---RT 170
Cdd:pfam13304 179 PDLKELLQRLVRGLKLADLNLS-----DLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLaalLS 253
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 224511529 171 LAIEPNVILMDEPTSALDPISTGKIEELIINLKESYT-IIIVTHN 214
Cdd:pfam13304 254 ALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
37-59 |
3.57e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 3.57e-03
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
40-61 |
4.99e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.35 E-value: 4.99e-03
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-220 |
5.74e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.80 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 13 IIETKNLNLFYTDFKALNKINIKILKNSITALIGPSGCGKSTFLrtlnrmnDLVEGIKI--EGNVIYEGKNIYSNNFdvl 90
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEVLGGDMADARH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 91 elRRKIG-----MvfqtP-----N--PFLmSIYDNIS-----YGpkiHGTKDKKT-LDEiveqsLIKSalwnevkdklnT 152
Cdd:NF033858 71 --RRAVCpriayM----PqglgkNlyPTL-SVFENLDffgrlFG---QDAAERRRrIDE-----LLRA-----------T 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 153 N--------ALSLSGGQQQR--LCIArtLAIEPNVILMDEPTSALDPISTGKIEELIINLKE---SYTIIIVTHNMQQAG 219
Cdd:NF033858 125 GlapfadrpAGKLSGGMKQKlgLCCA--LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAerpGMSVLVATAYMEEAE 202
|
.
gi 224511529 220 R 220
Cdd:NF033858 203 R 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
156-224 |
6.98e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 36.71 E-value: 6.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 156 SLSGGQQQRLCIARTLAIEPNVILMDEPTSALDPISTGKIEELII-NLKESYTIIIVTHnmQQAGRISDR 224
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAqHAEQGGMVILTTH--QDLPVASDK 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
29-215 |
7.09e-03 |
|
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: 36.82 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 29 LNKINIKILKNSITALIGPSGCGKSTFLrtlnrmND-LVEGIKIEGNviyeGKNIYSNNFDVLELRRKIGMVF---QTP- 103
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI------NDtLYPALARRLH----LKKEQPGNHDRIEGLEHIDKVIvidQSPi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224511529 104 ------NPF-LMSIYDNIS--YGPKIHGTK----------DKKTLDEIVEQSLIKSALWNE----VKDKLNT-------- 152
Cdd:cd03271 81 grtprsNPAtYTGVFDEIRelFCEVCKGKRynretlevryKGKSIADVLDMTVEEALEFFEnipkIARKLQTlcdvglgy 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224511529 153 -----NALSLSGGQQQRLCIARTL---AIEPNVILMDEPTSALDPISTGKIEELIINLKES-YTIIIVTHNM 215
Cdd:cd03271 161 iklgqPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNL 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
164-230 |
8.31e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.18 E-value: 8.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224511529 164 RLCIARTLAIEPNVILMDEPTSALDpISTGKIEELIINLKESyTIIIVTHnmqqagrisDRtaFFLN 230
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INTIRWLEDVLNERNS-TMIIISH---------DR--HFLN 216
|
|
| |
