|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-277 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 574.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 21 SLDLASESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIF 100
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 AKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQ 180
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|....*..
gi 15600559 261 TNPAKKQTEDYITGRYG 277
Cdd:COG1117 242 TNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
31-276 |
1.03e-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: 474.09 E-value: 1.03e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:TIGR00972 82 RRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTED 270
Cdd:TIGR00972 162 EPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTED 241
|
....*.
gi 15600559 271 YITGRY 276
Cdd:TIGR00972 242 YISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
31-259 |
2.70e-149 |
|
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: 416.58 E-value: 2.70e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHesALGLSGGQQQRLVIARTIAV 190
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-277 |
6.22e-142 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 399.54 E-value: 6.22e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 24 LASESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKG 103
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 104 VDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGInkKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLV 183
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFM---------YMGKLIEFG 254
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFD 241
|
250 260
....*....|....*....|...
gi 15600559 255 DTDTLFTNPAKKQTEDYITGRYG 277
Cdd:PRK14243 242 RTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
31-277 |
4.46e-138 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 389.13 E-value: 4.46e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTED 270
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 15600559 271 YITGRYG 277
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-277 |
9.50e-109 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 314.86 E-value: 9.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINK-KRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTI 188
Cdd:PRK14267 85 REVGMVFQYPNPFPHlTIYDNVAIGVKLNGLVKsKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQT 268
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 15600559 269 EDYITGRYG 277
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-277 |
3.58e-100 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 293.48 E-value: 3.58e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIY--ELKSKFTIVIVTHNMQQAARVSDYTAFMY-----MGKLIEFGDTDTLFTNP 263
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 15600559 264 AKKQTEDYITGRYG 277
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-275 |
1.57e-98 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 289.12 E-value: 1.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFAkgVDVAELR 110
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK--MDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGI-NKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTI 188
Cdd:PRK14247 82 RRVQMVFQIPNPIPNlSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQT 268
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*..
gi 15600559 269 EDYITGR 275
Cdd:PRK14247 242 EKYVTGR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-277 |
2.76e-80 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 243.46 E-value: 2.76e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 13 DALGRDRQSLDLASESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEI 92
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 93 RLDGHNIFAKGvDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESAL 172
Cdd:PRK14271 84 LLGGRSIFNYR-DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 173 GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIE 252
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
250 260
....*....|....*....|....*
gi 15600559 253 FGDTDTLFTNPAKKQTEDYITGRYG 277
Cdd:PRK14271 243 EGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-275 |
4.71e-78 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 237.25 E-value: 4.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 25 ASESVE--LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDG-CRVEGEIRLDGHNIFA 101
Cdd:PRK14246 3 AGKSAEdvFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 102 kgVDVAELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQ 180
Cdd:PRK14246 83 --IDAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
250
....*....|....*
gi 15600559 261 TNPAKKQTEDYITGR 275
Cdd:PRK14246 241 TSPKNELTEKYVIGR 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
31-272 |
7.00e-73 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 223.33 E-value: 7.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDGcrveGEIRLDGHNIFAKGVDVAELR 110
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE-PDS----GTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFP-KSIYENVVYGLR-IQGINKkrvlDEAVEWALkgaALWEEV--KDRLHESALGLSGGQQQRLVIAR 186
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLAPIkVKKMSK----AEAEERAM---ELLERVglADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAK 265
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
....*..
gi 15600559 266 KQTEDYI 272
Cdd:COG1126 230 ERTRAFL 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
17-263 |
6.78e-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: 6.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 17 RDRQSLDLASESVELEVPGLNLFY-----GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGE 91
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 92 IRLDGHNIFA-KGVDVAELRRRVGMVFQKP----NPFpKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDR 166
Cdd:COG1123 322 ILFDGKDLTKlSRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 167 L-HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTA 243
Cdd:COG1123 401 YpHE----LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVA 476
|
250 260
....*....|....*....|
gi 15600559 244 FMYMGKLIEFGDTDTLFTNP 263
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-254 |
1.27e-59 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 188.50 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRMNdlvdgcrvEGEIRLDGHNIFakgvDVA 107
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLiagLERPD--------SGEILIDGRDVT----GVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFP-KSIYENVVYGLRIQGInKKRVLDEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIAR 186
Cdd:cd03259 69 PERRNIGMVFQDYALFPhLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
31-263 |
2.76e-59 |
|
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: 188.31 E-value: 2.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmndlvdGC--RVEGEIRLDGHNIFAKgvDVA 107
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-------GLlkPTSGEVLVDGKDITKK--NLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQkpNP----FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKDRlheSALGLSGGQQQRLV 183
Cdd:COG1122 72 ELRRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGLPREEI-RERVEEALELVGL-EHLADR---PPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF-TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 15600559 263 P 263
Cdd:COG1122 225 Y 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-250 |
9.91e-59 |
|
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: 186.20 E-value: 9.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDGcrveGEIRLDGHNIFAKGVDVAELR 110
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE-PDS----GTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFP-KSIYENVVYGLR-IQGINKkrvlDEAVEWALKgaaLWEEV--KDRLHESALGLSGGQQQRLVIAR 186
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIkVKGMSK----AEAEERALE---LLEKVglADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-267 |
1.91e-57 |
|
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: 183.86 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHNIFA-KGVDVAEL 109
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLR--PDSGEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNPF-PKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTI 188
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF--TNPA 264
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
...
gi 15600559 265 KKQ 267
Cdd:cd03261 232 VRQ 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
31-249 |
6.75e-57 |
|
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: 180.46 E-value: 6.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFP-KSIYENVvyglriqginkkrvldeavewalkgaalweevkdrlhesALGLSGGQQQRLVIARTIA 189
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENI---------------------------------------ALGLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGK 249
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-273 |
1.90e-55 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 178.67 E-value: 1.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmndLVDGCRvEGEIRLDGHNI-FAKGVD---V 106
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLEMPR-SGTLNIAGNHFdFSKTPSdkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPK-SIYENVVYG-LRIQGINKKRVLDEAVEwALKGAALwEEVKDR--LHesalgLSGGQQQRL 182
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHlTVQQNLIEApCRVLGLSKDQALARAEK-LLERLRL-KPYADRfpLH-----LSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTlFT 261
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FT 229
|
250
....*....|..
gi 15600559 262 NPAKKQTEDYIT 273
Cdd:PRK11124 230 QPQTEAFKNYLS 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
27-264 |
3.05e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 181.83 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 27 ESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRmndlVDgcrvEGEIRLDGHnifakg 103
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagFET----PD----SGRILLDGR------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 104 vDVAEL---RRRVGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKDRL-HEsalgLSGGQ 178
Cdd:COG3842 68 -DVTGLppeKRNVGMVFQDYALFPhLTVAENVAFGLRMRGVPKAEI-RARVAELLELVGL-EGLADRYpHQ----LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 179 QQRLVIARTIAVEPEVLLLDEPCSALDPisTLKiEELIYELKS-----KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEF 253
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDA--KLR-EEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQV 217
|
250
....*....|.
gi 15600559 254 GDTDTLFTNPA 264
Cdd:COG3842 218 GTPEEIYERPA 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
42-263 |
1.65e-54 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 177.64 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 42 AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmndlvdGC--RVEGEIRLDGHNIFA-KGVDVAELRRRVGMVFQ 118
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN-------GLlkPTSGTVTIDGRDITAkKKKKLKDLRKKVGLVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRlheSALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:TIGR04521 90 FPEHqlFEETVYKDIAFGPKNLGLSEEEA-EERVKEALELVGLDEEYLER---SPFELSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 197 LDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
30-272 |
1.88e-54 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 176.36 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMnDLVDgcrvEGEIRLDGHNI-FAKGVD--- 105
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-ETPD----SGQLNIAGHQFdFSQKPSeka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRRVGMVFQKPNPFPK-SIYENVVYG-LRIQGINKKRVLDEAVEwALKGAALweevKDRLHESALGLSGGQQQRLV 183
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWPHlTVMENLIEApCKVLGLSKEQAREKAMK-LLARLRL----TDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTdTLFTN 262
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQ 230
|
250
....*....|
gi 15600559 263 PAKKQTEDYI 272
Cdd:COG4161 231 PQTEAFAHYL 240
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-267 |
6.51e-54 |
|
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: 174.78 E-value: 6.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 26 SESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLV--DgcrvEGEIRLDGHNIF-AK 102
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKL---IIGLLrpD----SGEILVDGQDITgLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 GVDVAELRRRVGMVFQKPNPF-PKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALwEEVKDRL-HEsalgLSGGQQQ 180
Cdd:COG1127 74 EKELYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMpSE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
250
....*....|.
gi 15600559 259 LF--TNPAKKQ 267
Cdd:COG1127 229 LLasDDPWVRQ 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
31-240 |
8.36e-54 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 173.81 E-value: 8.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYG----AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGhnifakgV 104
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLR-------IIAGLErpTSGEVLVDG-------E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 DVAELRRRVGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEWA----LKGAAlweevKDRLHEsalgLSGGQQ 179
Cdd:cd03293 67 PVTGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLelvgLSGFE-----NAYPHQ----LSGGMR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSD 240
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLAD 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
31-240 |
1.27e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 174.51 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY----GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGcrVEGEIRLDGHnifakgvDV 106
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRL---IAGLEKP--TSGEVLVDGK-------PV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEWA----LKGAAlweevkDRL-HEsalgLSGGQQQ 180
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLelvgLAGFE------DAYpHQ----LSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSD 240
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLAD 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
31-259 |
6.15e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.17 E-value: 6.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHNIFAkgvDVAELR 110
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRM---LLGLLR--PTSGEVRVLGEDVAR---DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRvLDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIA 189
Cdd:COG1131 73 RRIGYVPQEPALYPDlTVRENLRFFARLYGLPRKE-ARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSKF-TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGkTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
39-272 |
1.14e-52 |
|
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: 171.71 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAkgVDVAELRRRVGMVFQ 118
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE-----PTSGEIFIDGEDIRE--QDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWE-EVKDRL-HEsalgLSGGQQQRLVIARTIAVEPEVL 195
Cdd:cd03295 83 QIGLFPhMTVEENIALVPKLLKWPKEKIRERADE-LLALVGLDPaEFADRYpHE----LSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYI 272
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
30-264 |
1.82e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.18 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrV-------EGEIRLDGHNIFak 102
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRI------------IagletpdSGRIVLNGRDLF-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 gVDVAELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEWaLKGAALwEEVKDRL-HEsalgLSGGQQQ 180
Cdd:COG1118 68 -TNLPPRERRVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEIRARVEEL-LELVQL-EGLADRYpSQ----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
....*.
gi 15600559 259 LFTNPA 264
Cdd:COG1118 221 VYDRPA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
31-254 |
2.86e-52 |
|
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: 169.99 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY----GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIFAKGVDV 106
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSG-----SIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRR-VGMVFQKP----NPFpKSIYENVVYGLRIQGINKKRV-LDEAVEWALKGAALWEEVKDRL-HEsalgLSGGQQ 179
Cdd:cd03257 77 RKIRRKeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRYpHE----LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
40-272 |
1.16e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 169.12 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIFAKGVDVAELRRRVGMVFQK 119
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG-----DLIVDGLKVNDPKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPK-SIYENVVYG-LRIQGINKKRVLDEAVEwALKGAALWEevkdRLHESALGLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PRK09493 86 FYLFPHlTALENVMFGpLRVRGASKEEAEKQARE-LLAKVGLAE----RAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 198 DEPCSALDPistlkieELIYE-LK-------SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTE 269
Cdd:PRK09493 161 DEPTSALDP-------ELRHEvLKvmqdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
...
gi 15600559 270 DYI 272
Cdd:PRK09493 234 EFL 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-265 |
1.38e-51 |
|
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: 176.25 E-value: 1.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndLVDGCRVEGEIRLDGHNIfaKGVDVAE 108
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDL--LELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKP--NPFPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIAR 186
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEA-RARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
.
gi 15600559 265 K 265
Cdd:COG1123 236 A 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
31-250 |
5.09e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 5.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGCrvEGEIRLDGHNIfaKGVDVAELR 110
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRA---LADLDPPT--SGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPKSIYENVVYGLRIQginKKRVLDEAVEWALKGAALWEEVKDRlheSALGLSGGQQQRLVIARTIAV 190
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDK---PVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
31-261 |
5.39e-51 |
|
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: 167.53 E-value: 5.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAELR 110
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDL--ASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPN-PFPKSIYENVVYGL-----RIQGINKKrvLDEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVI 184
Cdd:COG1120 75 RRIAYVPQEPPaPFGLTVRELVALGRyphlgLFGRPSAE--DREAVEEALERTGL-EHLADRPVDE---LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-263 |
1.63e-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: 166.13 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAK----QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDV 106
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPV--TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKP----NPFpKSIYENVVYGLRIQGInkkRVLDEAVEWALKGAALWEEVKDRL-HEsalgLSGGQQQR 181
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGL---PDREERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELK--SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
....
gi 15600559 260 FTNP 263
Cdd:COG1124 227 LAGP 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
31-250 |
3.72e-50 |
|
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: 164.59 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGA----KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMnDLVDgcrvEGEIRLDGHNIF-AKGVD 105
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL-DRPT----SGEVRVDGTDISkLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRR-VGMVFQKPNPFPK-SIYENVVYGLRIQGINKKrvldEAVEWALKgaaLWEEV--KDRLHESALGLSGGQQQR 181
Cdd:cd03255 76 LAAFRRRhIGFVFQSFNLLPDlTALENVELPLLLAGVPKK----ERRERAEE---LLERVglGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMqQAARVSDYTAFMYMGKL 250
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
41-263 |
7.17e-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: 164.29 E-value: 7.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMnDLVDgcrvEGEIRLDGHNIFA-KGVDVAELRRRVGMVFQK 119
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-ERPT----SGSVLVDGTDLTLlSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPF-PKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:cd03258 91 FNLLsSRTVFENVALPLEIAGVPKAEI-EERVLELLELVGL----EDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 199 EPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-249 |
8.19e-50 |
|
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: 163.41 E-value: 8.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 32 EVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKgvDVAEL 109
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-----PTSGEVLVDGKDLTKL--SLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIART 187
Cdd:cd03225 74 RRKVGLVFQNPDDqfFGPTVEEEVAFGLENLGLPEEEI-EERVEEALELVGLEGLRDRSPFT----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGK 249
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-264 |
2.30e-49 |
|
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: 165.61 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY----GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLVDGCRVEGEIRLDGHNIFA-KGVD 105
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLLKlSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELR-RRVGMVFQKP----NPFpKSIYENVVYGLRIQGINKKRVLDEAVEWALK--GAALWEEVKDRL-HEsalgLSGG 177
Cdd:COG0444 80 LRKIRgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLErvGLPDPERRLDRYpHE----LSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGD 255
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
....*....
gi 15600559 256 TDTLFTNPA 264
Cdd:COG0444 235 VEELFENPR 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
41-272 |
4.24e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 165.25 E-value: 4.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgcRV-EGEIRLDGHNIFA-KGVDVAELRRRVGMVFQ 118
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE------RPtSGSVLVDGVDLTAlSERELRAARRKIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPFP-KSIYENVVYGLRIQGINK----KRVldeavewalkgAALWEEV--KDRLHESALGLSGGQQQRLVIARTIAVE 191
Cdd:COG1135 90 HFNLLSsRTVAENVALPLEIAGVPKaeirKRV-----------AELLELVglSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTE 269
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
...
gi 15600559 270 DYI 272
Cdd:COG1135 239 RFL 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
41-264 |
4.37e-49 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 164.49 E-value: 4.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKP 120
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPT-----SGRILIDGEDI--RDLDPVELRRRIGYVIQQI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NPFP-KSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALW-EEVKDRL-HEsalgLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:COG1125 86 GLFPhMTVAENIATVPRLLGWDKERI-RARVDELLELVGLDpEEYRDRYpHE----LSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 198 DEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPA 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-264 |
5.59e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.25 E-value: 5.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 28 SVELEvpGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRMNdlvdgcrvEGEIRLDGhnifakgV 104
Cdd:COG3839 3 SLELE--NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLEDPT--------SGEILIGG-------R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 DVAEL---RRRVGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVlDEAVEWALKgaALweEVKDRLHESALGLSGGQQQ 180
Cdd:COG3839 66 DVTDLppkDRNIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEI-DRRVREAAE--LL--GLEDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPisTLKiEELIYELK-----SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGD 255
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDA--KLR-VEMRAEIKrlhrrLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
....*....
gi 15600559 256 TDTLFTNPA 264
Cdd:COG3839 218 PEELYDRPA 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
41-274 |
7.43e-48 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 160.12 E-value: 7.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRmndLVDGCRveGEIRLDGHNIFAkgVDVAEL----RRRVGMV 116
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAA--MSRKELrelrRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 117 FQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVL 195
Cdd:cd03294 108 FQSFALLPhRTVLENVAFGLEVQGVPRAEREERAAE-ALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYIT 273
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
.
gi 15600559 274 G 274
Cdd:cd03294 263 G 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
31-264 |
1.19e-47 |
|
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: 158.55 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIfakgVDVAE 108
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLR-------LIAGFETptSGEILLDGKDI----TNLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKrVLDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIART 187
Cdd:cd03300 70 HKRPVNTVFQNYALFPHlTVFENIAFGLRLKKLPKA-EIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 188 IAVEPEVLLLDEPCSALDpistLKI-EELIYELKS-----KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:cd03300 145 LVNEPKVLLLDEPLGALD----LKLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
...
gi 15600559 262 NPA 264
Cdd:cd03300 221 EPA 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
31-252 |
1.25e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.89 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYG----AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdGC--RV-EGEIRLDGHNIFA-K 102
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGldRPtSGEVLIDGQDISSlS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 GVDVAELRRR-VGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEWAlkgaalwEEV--KDRLHESALGLSGGQ 178
Cdd:COG1136 77 ERELARLRRRhIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELL-------ERVglGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 179 QQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARvSDYTAFMYMGKLIE 252
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-259 |
1.17e-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: 160.00 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 16 GRDRQSLDLASESVELEvpGLNLFYG--AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIR 93
Cdd:COG2274 461 GRSKLSLPRLKGDIELE--NVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRIL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 94 LDGHNIfaKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD-------R 166
Cdd:COG2274 534 IDGIDL--RQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEAlpmgydtV 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 167 LHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVsDYTAFMY 246
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLD 683
|
250
....*....|...
gi 15600559 247 MGKLIEFGDTDTL 259
Cdd:COG2274 684 KGRIVEDGTHEEL 696
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
41-238 |
2.88e-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: 147.53 E-value: 2.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKP 120
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD-----PTSGEILIDGVDL--RDLDLESLRKNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NPFPKSIYENVvyglriqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:cd03228 86 FLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600559 201 CSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARV 238
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA 161
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
41-274 |
3.06e-44 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.47 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRmndLVDGCRveGEIRLDGHNIFAkgVDVAEL----RRRVGMV 116
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIEPTA--GQIFIDGENIMK--QSPVELrevrRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 117 FQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVL 195
Cdd:TIGR01186 77 FQQFALFPhMTILQNTSLGPELLGWPEQERKEKALE-LLKLVGLEEYEHRYPDE----LSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYIT 273
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
.
gi 15600559 274 G 274
Cdd:TIGR01186 232 K 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
31-240 |
5.80e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.44 E-value: 5.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNL-FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIFA-KGVDVAE 108
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYG-------LR-IQGINKKRVLDEAVEwalkgaALwEEV--KDRLHESALGLSGG 177
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRlSVLTNVLAGrlgrtstWRsLLGLFPPEDRERALE------AL-ERVglADKAYQRADQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSD 240
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
31-272 |
1.06e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 148.74 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDG-HNIFAKGVDVAEL 109
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTaRSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNPFP-KSIYENVVYGlriQGINKKRVLDEAVEwalKGAALWEEVKDRLHESALG--LSGGQQQRLVIAR 186
Cdd:PRK11264 84 RQHVGFVFQNFNLFPhRTVLENIIEG---PVIVKGEPKEEATA---RARELLAKVGLAGKETSYPrrLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPistlkieELIYEL--------KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDP-------ELVGEVlntirqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....
gi 15600559 259 LFTNPAKKQTEDYI 272
Cdd:PRK11264 231 LFADPQQPRTRQFL 244
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
63-264 |
1.23e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 152.56 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRCFNRmndLVDGCRveGEIRLDGHNIFAkgVDVAEL----RRRVGMVFQKPNPFP-KSIYENVVYGLRI 137
Cdd:COG4175 60 GLSGSGKSTLVRCLNR---LIEPTA--GEVLIDGEDITK--LSKKELrelrRKKMSMVFQHFALLPhRTVLENVAFGLEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 138 QGINKKRVLDEAVEW-ALKGAALWEevkDRL-HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPIstlkI--- 212
Cdd:COG4175 133 QGVPKAERRERAREAlELVGLAGWE---DSYpDE----LSGGMQQRVGLARALATDPDILLMDEAFSALDPL----Irre 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 213 --EELIyELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:COG4175 202 mqDELL-ELQAKLkkTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPA 256
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
46-202 |
1.33e-43 |
|
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: 145.48 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIFAKgvDVAELRRRVGMVFQKPNPFP- 124
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 125 KSIYENVVYGLRIQGINKKRVLDEAvEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCS 202
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
31-250 |
1.37e-43 |
|
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: 146.00 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHNIFAKGVDVaelR 110
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKI---ILGLLK--PDSGEIKVLGKDIKKEPEEV---K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYglriqginkkrvldeavewalkgaalweevkdrlhesalglSGGQQQRLVIARTIA 189
Cdd:cd03230 73 RRIGYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSKF-TIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
31-263 |
2.71e-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: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGCrvEGEIRLDGHNI-FAKGVD---- 105
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRC---INLLETPD--SGEIRVGGEEIrLKPDRDgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 ------VAELRRRVGMVFQKPNPFP-KSIYENVVYG-LRIQGINKkrvlDEAVEWALkgaALWEEV--KDRLHESALGLS 175
Cdd:COG4598 84 padrrqLQRIRTRLGMVFQSFNLWShMTVLENVIEApVHVLGRPK----AEAIERAE---ALLAKVglADKRDAYPAHLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 176 GGQQQRLVIARTIAVEPEVLLLDEPCSALDPistlkieELIYE-LK-------SKFTIVIVTHNMQQAARVSDYTAFMYM 247
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmrdlaeEGRTMLVVTHEMGFARDVSSHVVFLHQ 229
|
250
....*....|....*.
gi 15600559 248 GKLIEFGDTDTLFTNP 263
Cdd:COG4598 230 GRIEEQGPPAEVFGNP 245
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
31-264 |
3.96e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 149.50 E-value: 3.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALF-----------DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNI 99
Cdd:COG4608 8 LEVRDLKKHFPVRGGLFgrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-----SGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 100 F-AKGVDVAELRRRVGMVFQKP----NPfPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRL-HEsalg 173
Cdd:COG4608 83 TgLSGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYpHE---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpIStlkIE----ELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYM 247
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMYL 233
|
250
....*....|....*..
gi 15600559 248 GKLIEFGDTDTLFTNPA 264
Cdd:COG4608 234 GKIVEIAPRDELYARPL 250
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-249 |
2.79e-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: 142.00 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 32 EVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKgvDVAELRR 111
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKL--PLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQkpnpfpksiyenvvyglriqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTIAVE 191
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGK 249
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
41-254 |
1.12e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDgcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKP 120
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-PT----SGRILIDGVDI--RDLTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPE 193
Cdd:COG1132 424 FLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 194 VLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHnmqqaaRVS-----DYTAFMYMGKLIEFG 254
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVEQG 556
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
25-259 |
1.27e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 150.29 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 25 ASESVELEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKG 103
Cdd:COG4988 331 AAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 104 VDVAELRRRVGMVFQKPNPFPKSIYENvvygLRIQGINkkrVLDEAVEWALKGAALWEEVKD-------RLHESALGLSG 176
Cdd:COG4988 404 LDPASWRRQIAWVPQNPYLFAGTIREN----LRLGRPD---ASDEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 177 GQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDT 256
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
...
gi 15600559 257 DTL 259
Cdd:COG4988 556 EEL 558
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
31-272 |
7.72e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.15 E-value: 7.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDgcrvEGEIRLDGHNIFAkgvDVAELR 110
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK-PD----SGSILIDGEDVRK---EPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKpNPFPK--SIYENVVYGLRIQGINKKRvLDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTI 188
Cdd:COG4555 74 RQIGVLPDE-RGLYDrlTVRENIRYFAELYGLFDEE-LKKRIEELIELLGLEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELK-SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQ 267
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
....*
gi 15600559 268 TEDYI 272
Cdd:COG4555 228 LEDAF 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
47-264 |
4.33e-40 |
|
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: 142.16 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 47 FDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlVDG-CRV-EGEIRLDGHNIF--AKGVDVAELRRRVGMVFQKPNP 122
Cdd:COG4148 16 LDVDFTLPGRGVTALFGPSGSGKTTLLRA-------IAGlERPdSGRIRLGGEVLQdsARGIFLPPHRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FP-KSIYENVVYGLRIQGINKKRV-LDEAVEWaLKGAALweevkdrLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:COG4148 89 FPhLSVRGNLLYGRKRAPRAERRIsFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 201 CSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
31-240 |
5.46e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 138.85 E-value: 5.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGA-KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNI-FAKGVDVAE 108
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDInKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGlRIQGINKKRVL-----DEAVEWALkgAALwEEV--KDRLHESALGLSGGQQQ 180
Cdd:cd03256 76 LRRQIGMIFQQFNLIERlSVLENVLSG-RLGRRSTWRSLfglfpKEEKQRAL--AAL-ERVglLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSD 240
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYAD 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
31-261 |
5.58e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHnifakgvDVAELR 110
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVRLFGK-------PPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPN---PFPKSIYENVVYGL-RIQGINK--KRVLDEAVEWALK--GAalwEEVKDRLhesaLG-LSGGQQQR 181
Cdd:COG1121 75 RRIGYVPQRAEvdwDFPITVRDVVLMGRyGRRGLFRrpSRADREAVDEALErvGL---EDLADRP----IGeLSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMyMGKLIEFGDTDTLF 260
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
.
gi 15600559 261 T 261
Cdd:COG1121 227 T 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
31-259 |
5.80e-40 |
|
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: 138.34 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDvAELR 110
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDITGLPPH-ERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQginKKRVLDEAVEWALkgaALWEEVKDRLHESALGLSGGQQQRLVIARTIA 189
Cdd:cd03224 75 AGIGYVPEGRRIFPElTVEENLLLGAYAR---RRAKRKARLERVY---ELFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-264 |
9.93e-40 |
|
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: 137.95 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMN--DlvdgcrvEGEIRLDGHNIfaKGVDVAE 108
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrpT-------SGSVLFDGEDI--TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRR-VGMVFQKPNPFPK-SIYENVVYGLRIQG---------INKKRVLDEAVEWALKGAALWeevkDRLHESALGLSGG 177
Cdd:cd03219 72 IARLgIGRTFQIPRLFPElTVLENVMVAAQARTgsglllaraRREEREARERAEELLERVGLA----DLADRPAGELSYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDT 256
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
....*...
gi 15600559 257 DTLFTNPA 264
Cdd:cd03219 228 DEVRNNPR 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
42-265 |
1.30e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 139.38 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 42 AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnRMNDLVDgcRVEGEIRLDGHNIFA--KGVDVAELRRRVGMVFQK 119
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQ---HLNGLLQ--PTSGTVTIGERVITAgkKNKKLKPLRKKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNP--FPKSIYENVVYGLRIQGINKKRVLDEAVEWaLKGAALWEEVkdrLHESALGLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PRK13634 94 PEHqlFEETVEKDICFGPMNFGVSEEDAKQKAREM-IELVGLPEEL---LARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 198 DEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAK 265
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
31-272 |
1.44e-39 |
|
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: 137.85 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQaLFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAEL- 109
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLET------------IAGFIKPDSGKILLNGKDITNLp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 --RRRVGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEWA--LKGAALweevkdrLHESALGLSGGQQQRLVI 184
Cdd:cd03299 68 peKRDISYVPQNYALFPhMTVYKNIAYGLKKRKVDKKEIERKVLEIAemLGIDHL-------LNRKPETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPistlKIEE-LIYELK-----SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDV----RTKEkLREELKkirkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
250
....*....|....
gi 15600559 259 LFTNPAKKQTEDYI 272
Cdd:cd03299 217 VFKKPKNEFVAEFL 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
41-272 |
1.54e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 140.71 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgcR-VEGEIRLDGHNIFAkgVDVAEL---RRRVGMV 116
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE------RpTSGRVLVDGQDLTA--LSEKELrkaRRQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 117 FQKPNPFP-KSIYENVVYGLRIQGINK----KRVLD--EAVEWALKgaalweevKDRLHESalgLSGGQQQRLVIARTIA 189
Cdd:PRK11153 88 FQHFNLLSsRTVFDNVALPLELAGTPKaeikARVTEllELVGLSDK--------ADRYPAQ---LSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQ 267
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
....*
gi 15600559 268 TEDYI 272
Cdd:PRK11153 237 TREFI 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
31-277 |
4.26e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 136.66 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYG-AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNI-FAKGVDVAE 108
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDItKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFP-KSIYENVVYGlRIQGINKKRVL-----DEAVEWALkgaALWEEV--KDRLHESALGLSGGQQQ 180
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVLHG-RLGYKPTWRSLlgrfsEEDKERAL---SALERVglADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDytafmymgKLIEFGDTDT 258
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYAD--------RIVGLKAGEI 224
|
250
....*....|....*....
gi 15600559 259 LFTNPAKKQTEDYITGRYG 277
Cdd:TIGR02315 225 VFDGAPSELDDEVLRHIYG 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
32-254 |
7.16e-39 |
|
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: 134.10 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 32 EVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAELRR 111
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQkpnpfpksiyenVVYGLRIQGInKKRVLDEavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTIAVE 191
Cdd:cd03214 74 KIAYVPQ------------ALELLGLAHL-ADRPFNE-------------------------LSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
30-264 |
1.23e-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: 135.54 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAEL 109
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRL------------IAGLERPDSGTILFGGEDATDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 ---RRRVGMVFQKPNPFPK-SIYENVVYGLRIQgiNKKRVLDEAvewalkgaalweEVKDRLHE-------SALG----- 173
Cdd:cd03296 70 pvqERNVGFVFQHYALFRHmTVFDNVAFGLRVK--PRSERPPEA------------EIRAKVHEllklvqlDWLAdrypa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 -LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:cd03296 136 qLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
250
....*....|....
gi 15600559 251 IEFGDTDTLFTNPA 264
Cdd:cd03296 216 EQVGTPDEVYDHPA 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
42-262 |
2.10e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.33 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 42 AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnRMNDLVDGcrVEGEIRLDGHNIFAKGVDVAELRRRVGMVFQKP- 120
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQ---HLNGLLKP--TSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 -NPFPKSIYENVVYGLRIQGINKKRVLDEAVEwALKGAAL-WEEVKDRlheSALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:PRK13637 94 yQLFEETIEKDIAFGPINLGLSEEEIENRVKR-AMNIVGLdYEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 199 EPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
39-238 |
3.11e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.64 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMnDLVDgcrvEGEIRLDGHNIFA-KGVDVAELRRRVGMVF 117
Cdd:COG2884 11 YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE-ERPT----SGQVLVNGQDLSRlKRREIPYLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QK----PNpfpKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPE 193
Cdd:COG2884 86 QDfrllPD---RTVYENVALPLRVTGKSRKEI-RRRVREVLDLVGLSDKAKALPHE----LSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600559 194 VLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNM----QQAARV 238
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLelvdRMPKRV 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
31-254 |
4.69e-38 |
|
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: 133.15 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRM------------IAGLEEPTSGRIYIGGRDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 ---RRVGMVFQKPNPFP-KSIYENVVYGLRIQGInKKRVLDEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVIAR 186
Cdd:cd03301 69 pkdRDIAMVFQNYALYPhMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQI-EHLLDRKPKQ---LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 187 TIAVEPEVLLLDEPCSALDpiSTLKIEELIyELKS-----KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLD--AKLRVQMRA-ELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
31-272 |
6.61e-38 |
|
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: 136.71 E-value: 6.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAEL- 109
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRI------------IAGLERQTAGTIYQGGRDITRLp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 --RRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEW----ALKGAAlweevkdRLHESALglSGGQQQRL 182
Cdd:TIGR03265 73 pqKRDYGIVFQSYALFPNlTVADNIAYGLKNRGMGRAEVAERVAELldlvGLPGSE-------RKYPGQL--SGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLgvTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
250
....*....|..
gi 15600559 261 TNPAKKQTEDYI 272
Cdd:TIGR03265 224 RHPATPFVADFV 235
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
40-259 |
8.23e-38 |
|
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: 135.21 E-value: 8.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndlvdgcrvegeIRLDGHNIFAKGVDV----AELRRRVGM 115
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL------------LRPTSGTARVAGYDVvrepRKVRRSIGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 116 VFQKPNPFPK-SIYENVVYGLRIQGInKKRVLDEAVEWALKGAALWEEVKDRLHesalGLSGGQQQRLVIARTIAVEPEV 194
Cdd:TIGR01188 71 VPQYASVDEDlTGRENLEMMGRLYGL-PKDEAEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 195 LLLDEPCSALDPISTLKIEELIYELK-SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
40-264 |
1.37e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.62 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFAKGVDvaelRRRVGMVF 117
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDVTHRSIQ----QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKPNPFPK-SIYENVVYGLRIQGINKkrvldeavewalkgaalwEEVKDRLHEsALGL--------------SGGQQQRL 182
Cdd:PRK11432 85 QSYALFPHmSLGENVGYGLKMLGVPK------------------EERKQRVKE-ALELvdlagfedryvdqiSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
....
gi 15600559 261 TNPA 264
Cdd:PRK11432 226 RQPA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
55-254 |
1.78e-37 |
|
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: 131.65 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 55 KQRVTAFIGPSGCGKSTLLRCFNRMnDLVDGcrveGEIRLDGHNIF--AKGVDVAELRRRVGMVFQKPNPFPK-SIYENV 131
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGL-EKPDG----GTIVLNGTVLFdsRKKINLPPQQRKIGLVFQQYALFPHlNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 132 VYGLRIQGINKKRVLDEAVEWALKgaalWEEVKDRlheSALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLK 211
Cdd:cd03297 97 AFGLKRKRNREDRISVDELLDLLG----LDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600559 212 IEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03297 170 LLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
31-264 |
3.14e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 132.08 E-value: 3.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcFNrmndLVDGcrV----EGEIRLDGHNIfaKGVDV 106
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTL---FN----LITG--FyrptSGRILFDGRDI--TGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRvGMV--FQKPNPFPK-SIYENVVYGLRIQ-GINKKRVLDEAVEWALKGAALWEEV---------KDRLHESALG 173
Cdd:COG0411 74 HRIARL-GIArtFQNPRLFPElTVLENVLVAAHARlGRGLLAALLRLPRARREEREARERAeellervglADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
250
....*....|...
gi 15600559 252 EFGDTDTLFTNPA 264
Cdd:COG0411 233 AEGTPAEVRADPR 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-272 |
4.88e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.03 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDvrMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCrvegeIRLDGHNIFAKGVDVAEL- 109
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLL-------NLIAGF-----LPPDSGRILWNGQDLTALp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 --RRRVGMVFQKPNPFPK-SIYENVvyGLriqGINKKRVLDEA----VEWALKGAALwEEVKDRLHESalgLSGGQQQRL 182
Cdd:COG3840 68 paERPVSMLFQENNLFPHlTVAQNI--GL---GLRPGLKLTAEqraqVEQALERVGL-AGLLDRLPGQ---LSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPIstLKIE--ELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....
gi 15600559 259 LFTNPAKKQTEDYI 272
Cdd:COG3840 217 LLDGEPPPALAAYL 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
31-259 |
4.99e-37 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 130.57 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndlvdgCRVE-GEIRLDGHNIFAkgvDVAEL 109
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL------LKPTsGRATVAGHDVVR---EPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNPFPK-SIYENVVYGLRIQGInKKRVLDEAVEWALKGAALWEeVKDRLhesALGLSGGQQQRLVIARTI 188
Cdd:cd03265 72 RRRIGIVFQDLSVDDElTGWENLYIHARLYGV-PGAERRERIDELLDFVGLLE-AADRL---VKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-274 |
6.30e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 6.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRV--EGEIRL----DGHNIFAKG 103
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvnGQTINLvrdkDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 104 VDVAELRRRVGMVFQKPNPFPK-SIYENVVYG-LRIQGINKKRVLDEAVEWaLKGAALWEEVKDRLhesALGLSGGQQQR 181
Cdd:PRK10619 85 NQLRLLRTRLTMVFQHFNLWSHmTVLENVMEApIQVLGLSKQEARERAVKY-LAKVGIDERAQGKY---PVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPI---STLKI-EELIYELKskfTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTD 257
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElvgEVLRImQQLAEEGK---TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
250
....*....|....*..
gi 15600559 258 TLFTNPAKKQTEDYITG 274
Cdd:PRK10619 238 QLFGNPQSPRLQQFLKG 254
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-267 |
7.97e-37 |
|
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: 130.49 E-value: 7.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNdLVDgcRVEGEIRLDGHNIfaKGVDVAELR 110
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SG-LLP--PRSGSIRFDGEDI--TGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RR-VGMVFQKPNPFPK-SIYENVVYGLRIQGinKKRVLDEAVEWALkgaALWEEVKDRLHESALGLSGGQQQRLVIARTI 188
Cdd:COG0410 77 RLgIGYVPEGRRIFPSlTVEENLLLGAYARR--DRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQ 267
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVRE 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
44-259 |
3.10e-36 |
|
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: 129.20 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPNPF 123
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 124 PKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:cd03249 90 DGTIAENIRYG-------KPDATDEEVEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 197 LDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMqQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
62-264 |
3.23e-36 |
|
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: 131.46 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 62 IGPSGCGKSTLLRC---FNRMNdlvdgcrvEGEIRLDGHNIfakgVDVAELRRRVGMVFQKPNPFPK-SIYENVVYGLRI 137
Cdd:TIGR01187 2 LGPSGCGKTTLLRLlagFEQPD--------SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHmTVEENVAFGLKM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 138 QGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPistlKIEELI- 216
Cdd:TIGR01187 70 RKVPRAEI-KPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDK----KLRDQMq 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600559 217 YELKS-----KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:TIGR01187 141 LELKTiqeqlGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-259 |
2.71e-35 |
|
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: 132.97 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 25 ASESVELEVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaK 102
Cdd:COG4987 328 APGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDL--R 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 GVDVAELRRRVGMVFQKPNPFPKSIYENvvygLRIQginKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLS 175
Cdd:COG4987 401 DLDEDDLRRRIAVVPQRPHLFDTTLREN----LRLA---RPDATDEELWAALERVGLGDWLAAlpdgldtWLGEGGRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 176 GGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYE-LKSKfTIVIVTHNMQQAARVsDYTAFMYMGKLIEFG 254
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR-TVLLITHRLAGLERM-DRILVLEDGRIVEQG 551
|
....*
gi 15600559 255 DTDTL 259
Cdd:COG4987 552 THEEL 556
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-259 |
2.91e-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: 126.08 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQ--ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndLVdgcrveGEIRLDGHNIFAKGVDVA- 107
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKM------LT------GELRPTSGTAYINGYSIRt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ---ELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKDRLhesALGLSGGQQQRLV 183
Cdd:cd03263 69 drkAARQSLGYCPQFDALFDElTVREHLRFYARLKGLPKSEI-KEEVELLLRVLGL-TDKANKR---ARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-232 |
3.67e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.19 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCrvegeIRLDGHNIfaKGVDVAELRRRVGMVFQKPNP 122
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGS-----ILIDGQDI--REVTLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPEVL 195
Cdd:cd03253 87 FNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRfpdgydtIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNM 232
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
31-235 |
4.06e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 126.90 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYG----AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRMNdlvdgcrvEGEIRLDGHNIFAKG 103
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLiagFLAPS--------SGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 104 VDvaelrrRvGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEW----ALKGAAlweevKDRLHEsalgLSGGQ 178
Cdd:COG4525 76 AD------R-GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELlalvGLADFA-----RRRIWQ----LSGGM 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 179 QQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQA 235
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEA 198
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-259 |
7.80e-35 |
|
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: 126.39 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndLVDgcrVEGEIRLDGHNIfakgVDVA- 107
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLP---TSGKVTVDGLDT----LDEEn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 --ELRRRVGMVFQKP-NPFPKSIYEN-VVYGLRIQGIN----KKRVldeavEWALKGAALWEEvkdRLHESALgLSGGQQ 179
Cdd:TIGR04520 72 lwEIRKKVGMVFQNPdNQFVGATVEDdVAFGLENLGVPreemRKRV-----DEALKLVGMEDF---RDREPHL-LSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARvSDYTAFMYMGKLIE----- 252
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAegtpr 221
|
....*....
gi 15600559 253 --FGDTDTL 259
Cdd:TIGR04520 222 eiFSQVELL 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
31-264 |
9.70e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 127.27 E-value: 9.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQ-----ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFN----------RMNDLVDGCRVEGEIRLD 95
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNglikskygtiQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 96 GHNIfAKGVDVAELRRRVGMVFQKP--NPFPKSIYENVVYGLRIQGINKKRVLDEAvEWALKGAALWEEVKDRlheSALG 173
Cdd:PRK13631 102 NPYS-KKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLA-KFYLNKMGLDDSYLER---SPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELK-SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIE 252
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|..
gi 15600559 253 FGDTDTLFTNPA 264
Cdd:PRK13631 257 TGTPYEIFTDQH 268
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
32-243 |
1.10e-34 |
|
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: 124.18 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 32 EVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGCRveGEIRLDGhnifakgVDVAELRR 111
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKA---ILGLLKPTS--GSIRVFG-------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQKPN---PFPKSIYENVVYGLR-----IQGINKKRvlDEAVEWALKGAALwEEVKDRLhesaLG-LSGGQQQRL 182
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGLYghkglFRRLSKAD--KAKVDEALERVGL-SELADRQ----IGeLSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTA 243
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
41-239 |
2.80e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 123.13 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFA-KGVDVAELRRRVGMVF 117
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLK-------LLYGALTpsRGQVRIAGEDVNRlRGRQLPLLRRRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKPNPFP-KSIYENVVYGLRIQGInKKRVLDEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:TIGR02673 86 QDFRLLPdRTVYENVALPLEVRGK-KEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600559 197 LDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVS 239
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVA 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-260 |
2.91e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 125.24 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgCRVEGEIRLDGHNIFA--KGVDVAELRRRVGMVFQKPNP 122
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLITStsKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 --FPKSIYENVVYGLRIQGINKKrvldEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFGVSQE----EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 201 CSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
43-263 |
3.69e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.94 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndLVDGcrvEGEIRLDGHNIFAK--GVDVAELRRRVGMVFQKP 120
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHITPEtgNKNLKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NP--FPKSIYENVVYGLRIQGINKKRVLDEAVEWaLKGAALWEEVKDRlheSALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:PRK13641 95 EAqlFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 199 EPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
31-259 |
4.53e-34 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 123.40 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGCRveGEIRLDGHNIfakGVDVAELR 110
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKT---LMGLLPVKS--GSIRLDGEDI---TKLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGM--VFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEwalkgaaLWEEVKDRLHESALGLSGGQQQRLVIART 187
Cdd:TIGR03410 73 ARAGIayVPQGREIFPRlTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-263 |
4.67e-34 |
|
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: 129.03 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALF-----------DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgcRVEGEIRLDGHNI 99
Cdd:COG4172 276 LEARDLKVWFPIKRGLFrrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 100 FA-KGVDVAELRRRVGMVFQkpNPF----PK-SIYENVVYGLRIQGINKKRV-LDEAVEWALKGAALWEEVKDRL-HEsa 171
Cdd:COG4172 350 DGlSRRALRPLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGLSAAeRRARVAEALEEVGLDPAARHRYpHE-- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 172 lgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpISTLK-IEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMG 248
Cdd:COG4172 426 --FSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDG 502
|
250
....*....|....*
gi 15600559 249 KLIEFGDTDTLFTNP 263
Cdd:COG4172 503 KVVEQGPTEQVFDAP 517
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-259 |
6.88e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.45 E-value: 6.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLV--DgcrvEGEIRLDGHNIfakgvdVAE 108
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRI---ILGILapD----SGEVLWDGEPL------DPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVG-MvfqkpnP-----FPK-SIYENVVYGLRIQGINKKRVLDEAVEW----ALKGAAlweevKDRLHEsalgLSGG 177
Cdd:COG4152 69 DRRRIGyL------PeerglYPKmKVGEQLVYLARLKGLSKAEAKRRADEWlerlGLGDRA-----NKKVEE----LSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIV-THNMQQAARVSDYTAFMYMGKLIEFGDT 256
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
...
gi 15600559 257 DTL 259
Cdd:COG4152 214 DEI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
45-259 |
2.26e-33 |
|
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: 121.57 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDgcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPNPFP 124
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYD-VD----SGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:cd03251 90 DTVAENIAYG-------RPGATREEVEEAARAANAHEFIMElpegydtVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 198 DEPCSALDPISTLKIEELIYEL-KSKFTIVIvthnmqqAARVS-----DYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03251 163 DEATSALDTESERLVQAALERLmKNRTTFVI-------AHRLStienaDRIVVLEDGKIVERGTHEEL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
27-267 |
4.54e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 122.26 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 27 ESVELEVPGLNLFYG-AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVD 105
Cdd:PRK13636 2 EDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-----PSSGRILFDGKPIDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRRVGMVFQKPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKdrlHESALGLSGGQQQRLV 183
Cdd:PRK13636 77 LMKLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDEV-RKRVDNALKRTGI-EHLK---DKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFt 261
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF- 230
|
....*.
gi 15600559 262 npAKKQ 267
Cdd:PRK13636 231 --AEKE 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-252 |
6.14e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.90 E-value: 6.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIfakgVDVAE 108
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGFETpdSGRIMLDGQDI----THVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGIN----KKRVLDeavewALKGAALwEEVKDRlheSALGLSGGQQQRLV 183
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHmTVFENVAFGLRMQKTPaaeiTPRVME-----ALRMVQL-EEFAQR---KPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 184 IARTIAVEPEVLLLDEPCSALDpistLKI-EELIYELKS-----KFTIVIVTHNMQQAARVSDYTAFMYMGKlIE 252
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD----YKLrKQMQNELKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDGR-IE 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-261 |
7.27e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 7.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDgcrveGEIRLDGHNIFAKGVDvaEL 109
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS-----GTVFLGDKPISMLSSR--QL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPnPFPK--SIYENVVYG----LRIQGinKKRVLDEA-VEWALKGAALwEEVKDRLHESalgLSGGQQQRL 182
Cdd:PRK11231 75 ARRLALLPQHH-LTPEgiTVRELVAYGrspwLSLWG--RLSAEDNArVNQAMEQTRI-NHLADRRLTD---LSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
31-264 |
7.64e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 123.27 E-value: 7.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRLDGHnifakgvDVAE 108
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLehQTSGHIRFHGT-------DVSR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LR---RRVGMVFQKPNPFPK-SIYENVVYGLRIQginKKRVLDEAVEWALKGAALWEEVK-DRLHES-ALGLSGGQQQRL 182
Cdd:PRK10851 69 LHardRKVGFVFQHYALFRHmTVFDNIAFGLTVL---PRRERPNAAAIKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKS--KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
....
gi 15600559 261 TNPA 264
Cdd:PRK10851 226 REPA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-264 |
9.03e-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: 125.57 E-value: 9.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGA----KQALFDVRMNIPKQRVTAFIGPSGCGKS----TLLRcfnrmndLV--DGCRVEGEIRLDGHNIF 100
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILR-------LLpdPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 akGVDVAELRR----RVGMVFQKP----NPFpKSIYENVVYGLRI-QGINKKRVLDEAVEWalkgaaLwEEV-----KDR 166
Cdd:COG4172 80 --GLSERELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLhRGLSGAAARARALEL------L-ERVgipdpERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 167 L----HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSD 240
Cdd:COG4172 150 LdaypHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFAD 225
|
250 260
....*....|....*....|....
gi 15600559 241 YTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-264 |
1.54e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.61 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdLVDgcrvEGEIRLDGHNIFAKgvDVAEL 109
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQ----RGRVKVMGREVNAE--NEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWeevkDRLHESALGLSGGQQQRLVIART 187
Cdd:PRK13647 78 RSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLDKDEV-ERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTdTLFTNPA 264
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDED 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
42-260 |
2.84e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.22 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 42 AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHnifAKGVDVAELRRRVGMVFQKPN 121
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSST---SKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 P--FPKSIYENVVYGLRIQGINKK---RVLDEAVEWALKGAALWEEvkdrlheSALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNFGIPKEkaeKIAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 197 LDEPCSALDP---ISTLKIEELIYELKSkfTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13643 168 LDEPTAGLDPkarIEMMQLFESIHQSGQ--TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
48-264 |
2.97e-32 |
|
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: 121.37 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIF--AKGVDVAELRRRVGMVFQKPNPFPK 125
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPD-----EGEIVLNGRTLFdsRKGIFLPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 126 -SIYENVVYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLhesalglSGGQQQRLVIARTIAVEPEVLLLDEPCSAL 204
Cdd:TIGR02142 90 lSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRL-------SGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 205 DPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-230 |
3.12e-32 |
|
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: 123.94 E-value: 3.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 24 LASESVELEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaK 102
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPL--A 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 GVDVAELRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKDR-------LHESALGLS 175
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIRLA-------RPDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 176 GGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTH 230
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-254 |
1.21e-31 |
|
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: 116.52 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQrVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFAKGVdvaE 108
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMR-------ILATLTppSSGTIRIDGQDVLKQPQ---K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWeevkDRLHESALGLSGGQQQRLVIART 187
Cdd:cd03264 70 LRRRIGYLPQEFGVYPNfTVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLG----DRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-272 |
1.24e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIfakgVDVAE 108
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLR-------MLAGFEqpTAGQIMLDGVDL----SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEaVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIART 187
Cdd:PRK11607 89 YQRPINMMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAK 265
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
....*..
gi 15600559 266 KQTEDYI 272
Cdd:PRK11607 244 RYSAEFI 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-254 |
2.44e-31 |
|
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: 115.46 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdLVDgcrvEGEIRLDGhnifaKGVDvAELR 110
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII-LPD----SGEVLFDG-----KPLD-IAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEWaLKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIA 189
Cdd:cd03269 70 NRIGYLPEERGLYPKmKVIDQLVYLAQLKGLKKEEARRRIDEW-LERLELSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-252 |
2.75e-31 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 115.39 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLV--DgcrvEGEIRLDGHNIfakgVDVAE 108
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIkpD----SGEITFDGKSY----QKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVlDEAVewalkgaalwEEV--KDRLHESALGLSGGQQQRLVIA 185
Cdd:cd03268 70 ALRRIGALIEAPGFYPNlTARENLRLLARLLGIRKKRI-DEVL----------DVVglKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 186 RTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIE 252
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
44-263 |
4.46e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.72 E-value: 4.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDVAELRRRVGMVFQKPNP- 122
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-----PTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDDq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 -FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPC 201
Cdd:PRK13639 91 lFAPTVEEDVAFGPLNLGLSKEEV-EKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 202 SALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
45-231 |
8.27e-31 |
|
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: 114.43 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFA-KGVDVAELRRRVGMVFQKPNPF 123
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL-----PTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 124 PK-SIYENVVYGLRIQGINKKrvldeavEWALKGAALWEEV--KDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:cd03292 91 PDrNVYENVAFALEVTGVPPR-------EIRKRVPAALELVglSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 15600559 201 CSALDPISTLKIEELIYEL-KSKFTIVIVTHN 231
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-260 |
8.64e-31 |
|
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: 114.63 E-value: 8.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAE 108
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGIDI--RDISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKDR-------LHESALGLSGGQQQR 181
Cdd:cd03254 75 LRSMIGVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMqQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
48-240 |
1.52e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 117.05 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDghnifakgvDVAELRRRVGMVFQKPNPFPK-S 126
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN---------DVPPAERGVGMVFQSYALYPHlS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 127 IYENVVYGLRIQGINK----KRVldEAVEWALKGAALWE-EVKDrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDEPC 201
Cdd:PRK11000 92 VAENMSFGLKLAGAKKeeinQRV--NQVAEVLQLAHLLDrKPKA--------LSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600559 202 SALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSD 240
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLAD 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
31-268 |
1.63e-30 |
|
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: 113.79 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTllrCFNRMNDLVdgcRV-EGEIRLDGHNIFAKGVDVael 109
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLV---KPdSGKILLDGQDITKLPMHK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVF--QKPNPFPK-SIYENVVYGLRIQGINKKrvldeavEWALKGAALWEE-----VKDRLhesALGLSGGQQQR 181
Cdd:cd03218 72 RARLGIGYlpQEASIFRKlTVEENILAVLEIRGLSKK-------EREEKLEELLEEfhithLRKSK---ASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
....*...
gi 15600559 261 TNPAKKQT 268
Cdd:cd03218 222 ANELVRKV 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
39-251 |
3.18e-30 |
|
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: 112.35 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKgvdvaELRRRVGMVFQ 118
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAK-----ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNP--FPKSIYENVVYGLRIQGINKkrvldEAVEWALKGAALWEEvKDRlHesALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:cd03226 79 DVDYqlFTDSVREELLLGLKELDAGN-----EQAETVLKDLDLYAL-KER-H--PLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 197 LDEPCSALDPISTLKIEELIYELKS-KFTIVIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
31-263 |
3.20e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.09 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFA-KGVDVA 107
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLR-------LIGGQIApdHGEILFDGENIPAmSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLD-------EAVewALKGAAlweevkdRLHESAlgLSGGQQ 179
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDmNVFDNVAYPLREHTQLPAPLLHstvmmklEAV--GLRGAA-------KLMPSE--LSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTD 257
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
....*.
gi 15600559 258 TLFTNP 263
Cdd:PRK11831 230 ALQANP 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-260 |
7.18e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHNIFakgvdvaE 108
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW-------D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKP-NPFPKSIYEN-VVYGLRIQGINKKRVLdEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIAR 186
Cdd:PRK13635 79 VRRQVGMVFQNPdNQFVGATVQDdVAFGLENIGVPREEMV-ERVDQALRQVGM----EDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELK--SKFTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
44-205 |
9.73e-30 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 117.75 E-value: 9.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRmndlvdgcRVEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKP 120
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLllgFET--------PESGSVFYDGQDL--AGLDVQAVRRQLGVVLQNG 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NPFPKSIYENVVYGLRIqginkkrVLDEAVEwALKGAALWEEVKDR---LH----ESALGLSGGQQQRLVIARTIAVEPE 193
Cdd:TIGR03797 537 RLMSGSIFENIAGGAPL-------TLDEAWE-AARMAGLAEDIRAMpmgMHtvisEGGGTLSGGQRQRLLIARALVRKPR 608
|
170
....*....|..
gi 15600559 194 VLLLDEPCSALD 205
Cdd:TIGR03797 609 ILLFDEATSALD 620
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
39-235 |
9.74e-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: 110.98 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmndlvDGCRVE-GEIRLDGHNIFAKGVDVAELRRRVGMVF 117
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN------GLLRPQsGAVLIDGEPLDYSRKGLLERRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALkgAALweEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVL 195
Cdd:TIGR01166 75 QDPDDqlFAADVDQDVAFGPLNLGLSEAEV-ERRVREAL--TAV--GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQA 235
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
38-251 |
1.08e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 111.43 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 38 LFYGAKQALFDVrmNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEIRLDGhnifakgVDVAEL---RRR 112
Cdd:cd03298 8 FSYGEQPMHFDL--TFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLING-------VDVTAAppaDRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 113 VGMVFQKPNPFPK-SIYENVVYGlRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVE 191
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
44-262 |
1.46e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLDGHniFAKGVDVAELRRRVGMVFQKP--N 121
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN--LKKIKEVKRLRKEIGLVFQFPeyQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWEEVKDRlheSALGLSGGQQQRLVIARTIAVEPEVLLLDEPC 201
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGENKQEAYKKVPE-LLKLVQLPEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 202 SALDPISTLKIEELIYELKSKFT--IVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-231 |
1.72e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 116.31 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 14 ALGRDRQSLDLASESVELEVPGLNLFY-GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEI 92
Cdd:TIGR02868 318 AEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG-----EV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 93 RLDGhnIFAKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKDR------ 166
Cdd:TIGR02868 393 TLDG--VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-------RPDATDEELWAALERVGLADWLRALpdgldt 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 167 -LHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHN 231
Cdd:TIGR02868 464 vLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
31-267 |
3.19e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 110.83 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTllrCFNRMNDLVDgcRVEGEIRLDGHNIFAKGVDvaeLR 110
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHLPMH---ER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVF--QKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEwalkgaALWEE--VKDRLHESALGLSGGQQQRLVIA 185
Cdd:TIGR04406 74 ARLGIGYlpQEASIFRKlTVEENIMAVLEIRKDLDRAEREERLE------ALLEEfqISHLRDNKAMSLSGGERRRVEIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 186 RTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERgIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
...
gi 15600559 265 KKQ 267
Cdd:TIGR04406 228 VRR 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
44-256 |
3.23e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 112.49 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRM-------------NDLVDGCRVEGEIRLDGHNI----FAKGVDV 106
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIqktrFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQ--KPNPFPKSIYENVVYGLRIQGINKKrvldEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVI 184
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDT 256
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-254 |
7.52e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 109.38 E-value: 7.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDV----AELRRRVGMVFQK 119
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRM------------LAGLLEPDAGFATVDGFDVvkepAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPK-SIYENVVYGLRIQGInKKRVLDEAVEWALKGAalweEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:cd03266 87 TGLYDRlTARENLEYFAGLYGL-KGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 199 EPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
40-238 |
7.85e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 108.86 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrMNDLVDGcrveGEIRLDGHNIFA-KGVDVAELRR-RVGMVF 117
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIG-LLEKFDS----GQVYLNGQETPPlNSKKASKFRReKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKpnpFP----KSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPE 193
Cdd:TIGR03608 83 QN---FAlienETVEENLDLGLKYKKLSKKEKREKKKE-ALEKVGLNLKLKQKIYE----LSGGEQQRVALARAILKPPP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600559 194 VLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNM---QQAARV 238
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
32-261 |
8.81e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.79 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 32 EVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLvdgcrVEGEIRLDGHNIfaKGVDVAELRR 111
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPP-----DSGEVLVDGLDV--ATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQKPNPFPK-SIYENVVYGlRI---QG-INK--KRVLDEAVEW-ALkgaalwEEVKDR-LHEsalgLSGGQQQRL 182
Cdd:COG4604 76 RLAILRQENHINSRlTVRELVAFG-RFpysKGrLTAedREIIDEAIAYlDL------EDLADRyLDE----LSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
.
gi 15600559 261 T 261
Cdd:COG4604 225 T 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
45-232 |
1.56e-28 |
|
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: 108.45 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPN 121
Cdd:cd03245 19 ALDNVSLTIrAGEKV-AIIGRVGSGKSTLLK-------LLAGLYKptSGSVLLDGTDI--RQLDPADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENVVYGLRIqginkkrVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPEV 194
Cdd:cd03245 89 LFYGTLRDNITLGAPL-------ADDERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600559 195 LLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNM 232
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-274 |
2.58e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.66 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 26 SESVELEVPGLNLfyGAKqalfDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRmndLVDGCRveGEIRLDGHNIfAKGVD 105
Cdd:PRK10070 30 SKEQILEKTGLSL--GVK----DASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDI-AKISD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 vAELR----RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEwALKGAALweevKDRLHESALGLSGGQQQ 180
Cdd:PRK10070 98 -AELRevrrKKIAMVFQSFALMPHmTVLDNTAFGMELAGINAEERREKALD-ALRQVGL----ENYAHSYPDELSGGMRQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:PRK10070 172 RVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDE 251
|
250
....*....|....*.
gi 15600559 259 LFTNPAKKQTEDYITG 274
Cdd:PRK10070 252 ILNNPANDYVRTFFRG 267
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
43-271 |
3.06e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVD--VAELRRRVGMVFQKP 120
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK-----PTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NP--FPKSIYENVVYGLRIQGINKKRVLDEAVEWALK-GAAlweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PRK13646 95 ESqlFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDlGFS-----RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 198 DEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNpaKKQTEDY 271
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
40-259 |
3.28e-28 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 113.30 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKqALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndLVDGCRVE-GEIRLDGHNIfaKGVDVAELRRRVGMVFQ 118
Cdd:TIGR01193 485 YGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKL------LVGFFQARsGEILLNGFSL--KDIDRHTLRQFINYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPFPKSIYENVVYGlriqgiNKKRVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVE 191
Cdd:TIGR01193 556 EPYIFSGSILENLLLG------AKENVSQDEIWAACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSKfTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-259 |
6.68e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.36 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIfaKGVDVAELRRRVGMVF 117
Cdd:PRK13657 344 YDNSRQGVEDVSFEAkPGQTV-AIVGPTGAGKSTLINLLQRVFD-----PQSGRILIDGTDI--RTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKPNPFPKSIYENvvygLRIqgiNKKRVLDEAVEWALKGAALWEEVKDRLH-------ESALGLSGGQQQRLVIARTIAV 190
Cdd:PRK13657 416 QDAGLFNRSIEDN----IRV---GRPDATDEEMRAAAERAQAHDFIERKPDgydtvvgERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMqQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
31-240 |
6.88e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.84 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGcrvegeirLD---GHNIFAKGVDVA 107
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-------LLAG--------LEtpsAGELLAGTAPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFP-KSIYENVVYGLRiqgiNKKRvlDEAVEwALKGAALweevKDRLHESALGLSGGQQQRLVIAR 186
Cdd:PRK11247 78 EAREDTRLMFQDARLLPwKKVIDNVGLGLK----GQWR--DAALQ-ALAAVGL----ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSD 240
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMAD 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
31-236 |
1.40e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfNRMN-DLVDGCRVEGEIRLDGHNIfakgVDVAEL 109
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLL---AAIAgTLSPAFSASGEVLLNGRRL----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNPFPK-SIYENVVYGL--RIQGINKKrvldEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVIAR 186
Cdd:COG4136 75 QRRIGILFQDDLLFPHlSVGENLAFALppTIGRAQRR----ARVEQALEEAGL-AGFADRDPAT---LSGGQRARVALLR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAA 236
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAP 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
49-260 |
1.47e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 49 VRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRLDGHNIFAKgvDVAELRRRVGMVFQKP-NPF-P 124
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTAR-------LIDGLfeEFEGKVKIDGELLTAE--NVWNLRRKIGMVFQNPdNQFvG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVVYGLRIQGINKKRVLDEAVEwalkgAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSAL 204
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDE-----ALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 205 DPISTLKIEELIYELKSKF--TIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
39-263 |
2.67e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKgvDVAELRRRVGMVFQ 118
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-----PTSGSVLIRGEPITKE--NIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNP--FPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:PRK13652 86 NPDDqiFSPTVEQDIAFGPINLGLDEETV-AHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 197 LDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-254 |
6.91e-27 |
|
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: 104.11 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFY--GAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDV 106
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIkPGEKV-GIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDI--SKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPKSIYENV----VYGlriqginkkrvlDEAVEWALKGAALWEEVK-------DRLHESALGLS 175
Cdd:cd03244 74 HDLRSRISIIPQDPVLFSGTIRSNLdpfgEYS------------DEELWQALERVGLKEFVEslpggldTVVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 176 GGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHnmqqaaRV-----SDYTAFMYMGKL 250
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRV 215
|
....
gi 15600559 251 IEFG 254
Cdd:cd03244 216 VEFD 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
43-262 |
9.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.17 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndLVDgcrVEGEIRLDGHNIFAKGvDVAELRRRVGMVFQKP-N 121
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDTSDEE-NLWDIRNKAGMVFQNPdN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYE-NVVYGLRIQGINKKRVlDEAVEWALKGAALWEEvkdRLHESALgLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PRK13633 97 QIVATIVEeDVAFGPENLGIPPEEI-RERVDESLKKVGMYEY---RRHAPHL-LSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 201 CSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
42-237 |
1.14e-26 |
|
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: 103.70 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 42 AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIFAkgVDVAELRRRVGMVFQKPN 121
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG-----QVLLDGKPISQ--YEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENVVYGLriQGINkkrvLDEAVEWALKGAA----------LWEEVKdrlhESALGLSGGQQQRLVIARTIAVE 191
Cdd:cd03248 99 LFARSLQDNIAYGL--QSCS----FECVKEAAQKAHAhsfiselasgYDTEVG----EKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAAR 237
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-263 |
1.60e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.43 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 38 LFYGAK--QALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfNRMNDLVDgCRVEGEIRLDGHNI-FAKGVDVAELRRRVG 114
Cdd:PRK11308 21 LFKPERlvKALDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTMIE-TPTGGELYYQGQDLlKADPEAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 115 MVFQKP----NPFPK--SIYENVVYglriqgINKKRVLDEAVEWALKGAA---LWEEVKDRL-HEsalgLSGGQQQRLVI 184
Cdd:PRK11308 96 IVFQNPygslNPRKKvgQILEEPLL------INTSLSAAERREKALAMMAkvgLRPEHYDRYpHM----FSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
.
gi 15600559 263 P 263
Cdd:PRK11308 246 P 246
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-256 |
1.74e-26 |
|
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: 103.02 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 37 NLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCR--VEGEIRLDGHNIfakgVDVAELRRRVG 114
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLL-------NLIAGFIepASGSIKVNDQSH----TGLAPYQRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 115 MVFQKPNPFPK-SIYENVVYG----LRIQGINKKRVLDEAVEWALkgaalwEEVKDRLHESalgLSGGQQQRLVIARTIA 189
Cdd:TIGR01277 74 MLFQENNLFAHlTVRQNIGLGlhpgLKLNAEQQEKVVDAAQQVGI------ADYLDRLPEQ---LSGGQRQRVALARCLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKS--KFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDT 256
Cdd:TIGR01277 145 RPNPILLLDEPFSALDPLLREEMLALVKQLCSerQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-277 |
1.80e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.30 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 36 LNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgCRVEGEIRLDGHNI--FAKgvdvAELRRRV 113
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHIqhYAS----KEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 114 GMVFQKP-NPFPKSIYENVVYGLRIQG--INKKRVLDE-AVEWALKGAAlweeVKDRLHESALGLSGGQQQRLVIARTIA 189
Cdd:PRK10253 84 GLLAQNAtTPGDITVQELVARGRYPHQplFTRWRKEDEeAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGdtdtlftNPAKKQ 267
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIV 232
|
250
....*....|
gi 15600559 268 TEDYITGRYG 277
Cdd:PRK10253 233 TAELIERIYG 242
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
43-262 |
1.82e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 104.30 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrmNDLVDGC--RVEGEIRLDGHNIFAKGVDvaELRRRVGMVFQKP 120
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTI-------SKILTGLlkPQSGEIKIDGITISKENLK--EIRKKIGIIFQNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 -NPFPKSIYE-NVVYGLRIQGINKKRVLDEAVEWALKgaalwEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:PRK13632 93 dNQFIGATVEdDIAFGLENKKVPPKKMKDIIDDLAKK-----VGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 199 EPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-260 |
2.09e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFAKgvDVAELRRRVGMVFQKP-N 121
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIGIEKvkSGEIFYNNQAITDD--NFEKLRKHIGIVFQNPdN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYE-NVVYGLRIQGINKKRvLDEAVEWALKGAALWEEVKDRLHesalGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PRK13648 95 QFVGSIVKyDVAFGLENHAVPYDE-MHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 201 CSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
45-259 |
2.55e-26 |
|
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: 102.95 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIFAkgVDVAELRRRVGMVFQKPNPFP 124
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG-----RVLVDGHDLAL--ADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVvyGLRIQGINKKRVLDEAvewALKGA-----ALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDE 199
Cdd:cd03252 90 RSIRDNI--ALADPGMSMERVIEAA---KLAGAhdfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 200 PCSALDPISTLKIEELIYELKSKFTIVIVTHNMqQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
43-263 |
2.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMndLVDGCRVEGEIRLDGHNIFAKgvDVAELRRRVGMVFQKP-N 121
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAK--TVWDIREKVGIVFQNPdN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PF-PKSIYENVVYGLRIQGINKKRVLdEAVEWALKGAALWEEVKDrlhESAlGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PRK13640 96 QFvGATVGDDVAFGLENRAVPRPEMI-KIVRDVLADVGMLDYIDS---EPA-NLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 201 CSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAArVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
30-233 |
4.31e-26 |
|
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: 107.26 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFY-GAKQ-ALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDV 106
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIrPGEKV-AIIGRIGSGKSTLLKLLLGLYQPT-----EGSVLLDGVDI--RQIDP 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPKSIYENVVYGLRiqGINkkrvlDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQ 179
Cdd:TIGR03375 535 ADLRRNIGYVPQDPRLFYGTLRDNIALGAP--YAD-----DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQR 607
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQ 233
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-237 |
4.46e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.13 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFY----GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFAKGV 104
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLG-------LLAGLDRptSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 D-VAELRRR-VGMVFQK----PNpfpKSIYENVVYGLRIQGinkkrvLDEAVEWAlkgAALWEEV--KDRLHESALGLSG 176
Cdd:COG4181 82 DaRARLRARhVGFVFQSfqllPT---LTALENVMLPLELAG------RRDARARA---RALLERVglGHRLDHYPAQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 177 GQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAAR 237
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
31-254 |
5.01e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmNDLVDGCrveGEIRLDGHNIfaKGVDVAELR 110
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPDS---GEVRLNGRPL--ADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPN-PFPKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWeEVKDRLHESalgLSGGQQQRLVIARTIA 189
Cdd:PRK13548 76 RRRAVLPQHSSlSFPFTVEEVVAMGRAPHGLSRAED-DALVAAALAQVDLA-HLAGRDYPQ---LSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 190 ------VEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
30-254 |
5.10e-26 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 101.33 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAK--QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCrvegeIRLDGHNIfaKGVDVA 107
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGK-----IEIDGIDI--STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFPKSIYENV-VYGlriqginkkRVLDEAVEWALkgaalweevkdRLHESALGLSGGQQQRLVIAR 186
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNLdPFD---------EYSDEEIYGAL-----------RVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQaarVSDYTAF--MYMGKLIEFG 254
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRT---IIDYDKIlvMDAGEVKEYD 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-235 |
1.61e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEIRLDGHNIFAKGvdvAE 108
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL-------NLIAGFVPyqHGSITLDGKPVEGPG---AE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LrrrvGMVFQKPNPFP-KSIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWEEVKDRLHEsalgLSGGQQQRLVIART 187
Cdd:PRK11248 72 R----GVVFQNEGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQ-MLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQA 235
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEA 192
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
31-238 |
2.92e-25 |
|
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: 98.44 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQA--LFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFAkgVDV 106
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLAR-------LILGLLrpTSGRVRLDGADISQ--WDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPKSIYENVvyglriqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIAR 186
Cdd:cd03246 72 NELGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNM---QQAARV 238
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
35-267 |
3.30e-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: 100.65 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 35 GLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegeirldghNIFAKGVDVAEL----- 109
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQG------------TVSFRGQDLYQLdrkqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 ---RRRVGMVFQKP----NPfPKSIYENVVYGLR-IQGINKKRVLDEAVEwALKGAALWEEVKDRLHESalgLSGGQQQR 181
Cdd:TIGR02769 84 rafRRDVQLVFQDSpsavNP-RMTVRQIIGEPLRhLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQ---LSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|
gi 15600559 260 FT--NPAKKQ 267
Cdd:TIGR02769 239 LSfkHPAGRN 248
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-230 |
5.26e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.95 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFYGAKQ--ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDgcrvEGEIRLDGHNIfaKGVDVA 107
Cdd:PRK11176 341 DIEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD-ID----EGEILLDGHDL--RDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFPKSIYENVVYGlriqgiNKKRVLDEAVEWALKGA---ALWEEVKDRLH----ESALGLSGGQQQ 180
Cdd:PRK11176 414 SLRNQVALVSQNVHLFNDTIANNIAYA------RTEQYSREQIEEAARMAyamDFINKMDNGLDtvigENGVLLSGGQRQ 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTH 230
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
31-263 |
8.98e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTllrCFNrMndlvdgcrVEGEIRLDGHNIFAKGVDVAEL- 109
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFY-M--------IVGLVKPDSGRIFLDGEDITHLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 ---RRRVGMVF--QKPNPFPK-SIYENVVYGLRIQGINKKrvldeavEWALKGAALWEE-----VKDRLhesALGLSGGQ 178
Cdd:COG1137 72 mhkRARLGIGYlpQEASIFRKlTVEDNILAVLELRKLSKK-------EREERLEELLEEfgithLRKSK---AYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 179 QQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTD 257
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
....*.
gi 15600559 258 TLFTNP 263
Cdd:COG1137 222 EILNNP 227
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
44-250 |
1.13e-24 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 98.25 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrMNDLVDgcrvEGEIRLDGHNIfaKGVDVAE---LRRR-VGMVFQK 119
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEV--TNLSYSQkiiLRRElIGYIFQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPK-SIYENVVYGLRIQGINKKRVLdEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:NF038007 92 FNLIPHlSIFDNVALPLKYRGVAKKERI-ERVNQVLNLFGI----DNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600559 199 EPCSALDPISTLKI-EELIYELKSKFTIVIVTHNmQQAARVSDYTAFMYMGKL 250
Cdd:NF038007 167 EPTGNLDSKNARAVlQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-251 |
1.36e-24 |
|
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: 96.34 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNrmndlvdGCRV--EGEIRLDGHNIFAKGVDVAe 108
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLYKpdSGEILVDGKEVSFASPRDA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQkpnpfpksiyenvvyglriqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTI 188
Cdd:cd03216 73 RRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
31-268 |
1.90e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 98.62 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLfYGAKQALFDVRMNIPKQRVTAFIGPSGCGKStlLRCFNRMNDLVDGCR-VEGEIRLDGhnifaKGVDVAEL 109
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGRVLLDG-----KPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 R-RRVGMVFQKP----NPFpKSIYENVVYGLRIQGinKKRVLDEAVEwALKGAALwEEVKDRLHESALGLSGGQQQRLVI 184
Cdd:PRK10418 77 RgRKIATIMQNPrsafNPL-HTMHTHARETCLALG--KPADDATLTA-ALEAVGL-ENAARVLKLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
....*.
gi 15600559 263 PAKKQT 268
Cdd:PRK10418 232 PKHAVT 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
43-254 |
4.28e-24 |
|
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: 95.46 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRmnDLVDGcrvEGEIRLDGHNIFAKGvdvAELRRRVGMVFQKPN 121
Cdd:cd03247 15 QQVLKNLSLELkQGEKI-ALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLE---KALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENVvyGLRiqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDEPC 201
Cdd:cd03247 86 LFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600559 202 SALDPISTLKIEELIYE-LKSKfTIVIVTHNMQQAARVsDYTAFMYMGKLIEFG 254
Cdd:cd03247 127 VGLDPITERQLLSLIFEvLKDK-TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
31-250 |
6.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.49 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQ---ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFAKgvD 105
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDGLLEaeSGQIIIDGDLLTEE--N 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRRVGMVFQKP-NPFPKSIYEN-VVYGLRIQGIN----KKRVlDEAVEwaLKGAalwEEVKDRlhESALgLSGGQQ 179
Cdd:PRK13650 76 VWDIRHKIGMVFQNPdNQFVGATVEDdVAFGLENKGIPheemKERV-NEALE--LVGM---QDFKER--EPAR-LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAArVSDYTAFMYMGKL 250
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
31-263 |
7.46e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.98 E-value: 7.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRMNDlvdgcrveGEIRLDGHNIFAK-GVDV 106
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCltgFYKPTG--------GTILLRGQHIEGLpGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AelrrRVGMV--FQKPNPFPK-SIYENVVY--------GLrIQGINKKRVLDEAVEWALKGAALWEEV---KDRLHESAL 172
Cdd:PRK11300 78 A----RMGVVrtFQHVRLFREmTVIENLLVaqhqqlktGL-FSGLLKTPAFRRAESEALDRAATWLERvglLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 173 GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTP 232
|
250
....*....|...
gi 15600559 251 IEFGDTDTLFTNP 263
Cdd:PRK11300 233 LANGTPEEIRNNP 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-254 |
9.47e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 94.93 E-value: 9.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 28 SVELEVPGLN------LFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGCRVEGEIRLDGHNIFA 101
Cdd:cd03213 1 GVTLSFRNLTvtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNA---LAGRRTGLGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 102 KgvdvaELRRRVGMVFQkpnpfpksiyENVVYG-LRIQginkkrvldEAVEWAlkgAALweevkdRlhesalGLSGGQQQ 180
Cdd:cd03213 78 R-----SFRKIIGYVPQ----------DDILHPtLTVR---------ETLMFA---AKL------R------GLSGGERK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHnmqqAARVSDYTAF-----MYMGKLIEFG 254
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIH----QPSSEIFELFdklllLSQGRVIYFG 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
60-263 |
9.96e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.31 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 60 AFIGPSGCGKSTLLRCFNRmndLVDGcrVEGEIRLDGHNI-FAKGVDVAELRRRVGMVFQKP----NPfPKSIYENVVYG 134
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLR---LVES--QGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQDPyaslDP-RQTVGDSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGINKKRVLDEAVEWALKGAALWEEVKDRL-HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIE 213
Cdd:PRK10261 428 LRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 214 ELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK10261 504 NLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-254 |
1.93e-23 |
|
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: 99.41 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGA--KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIfaKGVDVAE 108
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-----SGQILLDGHDL--ADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKPNPFPKSIYENVVYGLRIQginkkrVLDEAVEWALKGAALWEEVkDRLH--------ESALGLSGGQQQ 180
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQ------ADRAEIERALAAAYAQDFV-DKLPlgldtpigENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNM---QQAARVsdytAFMYMGKLIEFG 254
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKADRI----VVMDDGRIVERG 549
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
47-261 |
2.66e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.03 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 47 FDVRMNiPKQRVtAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEIRLDGHNifakGVDVAELRRRVGMVFQKPNPFP 124
Cdd:PRK10771 18 FDLTVE-RGERV-AILGPSGAGKSTLL-------NLIAGFLTpaSGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 K-SIYENVVYG----LRIQGINKKRVLDEAVEWALkgaalwEEVKDRL-HEsalgLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:PRK10771 85 HlTVAQNIGLGlnpgLKLNAAQREKLHAIARQMGI------EDLLARLpGQ----LSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 199 EPCSALDPisTLKIE--ELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:PRK10771 155 EPFSALDP--ALRQEmlTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
46-248 |
3.49e-23 |
|
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: 94.45 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCR--VEGEIRLDGHNIFAKGVDvaelrRRVgmVFQKPNPF 123
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL-------NLISGLAqpTSGGVILEGKQITEPGPD-----RMV--VFQNYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 124 P-KSIYENVvyGLRIQGINKKRVLDEA---VEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLDE 199
Cdd:TIGR01184 67 PwLTVRENI--ALAVDRVLPDLSKSERraiVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600559 200 PCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMG 248
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
58-263 |
6.35e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKST---LLRCFNRMNdlvdgcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYG 134
Cdd:TIGR00958 509 VVALVGPSGSGKSTvaaLLQNLYQPT--------GGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRiqginkkRVLDEAVEWALKGAALWEEVKDRLH-------ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpi 207
Cdd:TIGR00958 579 LT-------DTPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD-- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 208 stLKIEELIYELKSK--FTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:TIGR00958 650 --AECEQLLQESRSRasRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-263 |
1.03e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.22 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 13 DALGRDRQSLDlASESVELEVPGLNLF-YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmNDLVDGCRVEGE 91
Cdd:PRK11174 333 AHPQQGEKELA-SNDPVTIEAEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 92 IRLDGHNIfaKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKDRLH--- 168
Cdd:PRK11174 406 LKINGIEL--RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-------NPDASDEQLQQALENAWVSEFLPLLPQgld 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 169 ----ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVsDYTAF 244
Cdd:PRK11174 477 tpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWV 555
|
250
....*....|....*....
gi 15600559 245 MYMGKLIEFGDTDTLFTNP 263
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQAG 574
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
31-230 |
1.11e-22 |
|
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: 92.54 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRmndlvdgcRVEGEIRLDGHNIfakGVDVA 107
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIlagLLP--------PSAGEVLWNGEPI---RDARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGInkkRVLDEAVEWALKGAALweevKDRLHESALGLSGGQQQRLVIAR 186
Cdd:COG4133 72 DYRRRLAYLGHADGLKPElTVRENLRFWAALYGL---RADREAIDEALEAVGL----AGLADLPVRQLSAGQKRRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYE-LKSKFTIVIVTH 230
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
44-227 |
1.36e-22 |
|
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: 96.81 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDGcrveGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPNPF 123
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD-VTS----GRILIDGQDI--RDVTQASLRAAIGIVPQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 124 PKSIYENVVYGlRIQginkkrVLDEAVEWALKGAALWEEVKD-------RLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:COG5265 445 NDTIAYNIAYG-RPD------ASEEEVEAAARAAQIHDFIESlpdgydtRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190
....*....|....*....|....*....|..
gi 15600559 197 LDEPCSALDPISTLKIEELIYEL-KSKFTIVI 227
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVaRGRTTLVI 549
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
40-237 |
1.93e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlVDGCR--VEGEIRLDGHnifakgvdvaelrRRVGMVF 117
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKV-------LAGVLrpTSGTVRRAGG-------------ARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QK---PNPFPKSIYENVVYG-------LRIQGINKKRVLDEAVEwALKGAALweeVKDRLHEsalgLSGGQQQRLVIART 187
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGrwarrglWRRLTRDDRAAVDDALE-RVGLADL---AGRQLGE----LSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAAR 237
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRR 184
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
35-267 |
2.12e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 35 GLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFA-KGVDVAELRR 111
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLAR-------LLVGLEspSQGNVSWRGEPLAKlNRAQRKAFRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQKP----NPfPKSIYENVVYGLR-IQGINKKRVLDEAVEwALKGAALWEEVKDRLHESalgLSGGQQQRLVIAR 186
Cdd:PRK10419 90 DIQMVFQDSisavNP-RKTVREIIREPLRhLLSLDKAERLARASE-MLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIE---FGDTDTlFT 261
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVEtqpVGDKLT-FS 243
|
....*.
gi 15600559 262 NPAKKQ 267
Cdd:PRK10419 244 SPAGRV 249
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
29-261 |
2.49e-22 |
|
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: 92.84 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 29 VELEvpGLNLFYGAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRMNDLVDGCRVE--GEIRldghnifaKGVD 105
Cdd:COG1119 4 LELR--NVTVRRGGKTILDDISWTVkPGEHW-AILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGERR--------GGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRRVGMV---FQkpNPFPKSI-YENVVY-------GLRiqginkKRVLDEAVEWALKGAALW--EEVKDRLHESal 172
Cdd:COG1119 73 VWELRKRIGLVspaLQ--LRFPRDEtVLDVVLsgffdsiGLY------REPTDEQRERARELLELLglAHLADRPFGT-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 173 gLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:COG1119 143 -LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
250
....*....|.
gi 15600559 251 IEFGDTDTLFT 261
Cdd:COG1119 222 VAAGPKEEVLT 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
62-264 |
3.78e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.64 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 62 IGPSGCGKSTllRCFNRMNDLVDGCRVEGEIRLDGHNIFakGVDVAELRR----RVGMVFQKP----NPFPKsIYENVVY 133
Cdd:PRK09473 48 VGESGSGKSQ--TAFALMGLLAANGRIGGSATFNGREIL--NLPEKELNKlraeQISMIFQDPmtslNPYMR-VGEQLME 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 134 GLRI-QGINKKRVLDEAVEwaLKGAALWEEVKDRL----HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPIS 208
Cdd:PRK09473 123 VLMLhKGMSKAEAFEESVR--MLDAVKMPEARKRMkmypHE----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTV 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 209 TLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:PRK09473 197 QAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-240 |
4.57e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.09 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC---FNRMNdlvdgcrvEGEIRLDGHNIFAKGVDVA 107
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKIlsgVYQPD--------SGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 ElRRRVGMVFQKPNPFPK-SIYENVVYGLRIQG---INKKRVLDEAVEwALK--GAAL--WEEVKDrlhesalgLSGGQQ 179
Cdd:COG1129 77 Q-AAGIAIIHQELNLVPNlSVAENIFLGREPRRgglIDWRAMRRRARE-LLArlGLDIdpDTPVGD--------LSVAQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSD 240
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIAD 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
44-240 |
4.58e-22 |
|
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: 91.34 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRmNDLVDGcrveGEIRLDGHNifaKGVDVA--------ELRRR-VG 114
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPDS----GSILVRHDG---GWVDLAqaspreilALRRRtIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 115 MVFQkpnpFPKSI-----YENVVYGLRIQGINKKRVLDEAVEWaLkgAALweEVKDRLHESA-LGLSGGQQQRLVIARTI 188
Cdd:COG4778 97 YVSQ----FLRVIprvsaLDVVAEPLLERGVDREEARARAREL-L--ARL--NLPERLWDLPpATFSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFT-IVIVTHNMQQAARVSD 240
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVAD 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
47-264 |
6.97e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 47 FDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEIRLDGHNIF--AKGVDVAELRRRVGMVFQKPNP 122
Cdd:PRK11144 15 LTVNLTLPAQGITAIFGRSGAGKTSLI-------NAISGLTRpqKGRIVLNGRVLFdaEKGICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPK-SIYENVVYGLRiqgiNKKRVL-DEAVEwaLKGAalwEEVKDRLHESalgLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PRK11144 88 FPHyKVRGNLRYGMA----KSMVAQfDKIVA--LLGI---EPLLDRYPGS---LSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 201 CSALD-PistLKIEELIY--ELKSKFTIVI--VTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPA 264
Cdd:PRK11144 156 LASLDlP---RKRELLPYleRLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
31-263 |
1.38e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.95 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRmnDLVDGcrvEGEIRLDGHNIfaKGVDVAELR 110
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPN-PFPKSIYENVVYGlRIQGINKKRVLDEAVEWALKGAALWEeVKDRLHESalgLSGGQQQRLVIARTIA 189
Cdd:COG4559 75 RRRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQT---LSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 190 -------VEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRgGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
..
gi 15600559 262 NP 263
Cdd:COG4559 230 DE 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
40-267 |
6.43e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.80 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTllrCFNRMNDLVDgcRVEGEIRLDGHNIFAKGVDvAELRRRVGMVFQK 119
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDISLLPLH-ARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPK-SIYENVVYGLRI-QGINKKRVLDEAVEwalkgaaLWEE-----VKDRLHESalgLSGGQQQRLVIARTIAVEP 192
Cdd:PRK10895 87 ASIFRRlSVYDNLMAVLQIrDDLSAEQREDRANE-------LMEEfhiehLRDSMGQS---LSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 193 EVLLLDEPCSALDPISTLKIEELIYELK-SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQ 267
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
60-237 |
7.45e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 60 AFIGPSGCGKSTLLRCfnrMNDLVDGCrvEGEIRLDGHNIFAKGVDV-AELR-RRVGMVFQKPNPFPK-SIYENVVYGLR 136
Cdd:PRK10584 40 ALIGESGSGKSTLLAI---LAGLDDGS--SGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQSFMLIPTlNALENVELPAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 137 IQGINKKRVLDEAVEwALKGAALWEevkdRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELI 216
Cdd:PRK10584 115 LRGESSRQSRNGAKA-LLEQLGLGK----RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180
....*....|....*....|...
gi 15600559 217 YELKSKF--TIVIVTHNMQQAAR 237
Cdd:PRK10584 190 FSLNREHgtTLILVTHDLQLAAR 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-257 |
8.30e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 91.73 E-value: 8.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 12 FDALGRDRQSLDLASESVELEVPGLNLFY-GAKQALF-DVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndLVDGCR-V 88
Cdd:COG4618 312 LAAVPAEPERMPLPRPKGRLSVENLTVVPpGSKRPILrGVSFSLEPGEVLGVIGPSGSGKSTLARL------LVGVWPpT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 89 EGEIRLDGHNIFAkgVDVAELRRRVGMVFQKPNPFPKSIYENVVyglRIQGINkkrvlDEAVEWALKGAAlweeVKD--- 165
Cdd:COG4618 386 AGSVRLDGADLSQ--WDREELGRHIGYLPQDVELFDGTIAENIA---RFGDAD-----PEKVVAAAKLAG----VHEmil 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 166 --------RLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKS-KFTIVIVTHNMqQAA 236
Cdd:COG4618 452 rlpdgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP-SLL 530
|
250 260
....*....|....*....|.
gi 15600559 237 RVSDYTAFMYMGKLIEFGDTD 257
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRD 551
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
39-237 |
1.00e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdgCRVE----GEIRLDGHNIFA-KGVDVAELRRRV 113
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLI---------CGIErpsaGKIWFSGHDITRlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 114 GMVFQKPNPF-PKSIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDrlheSALGLSGGQQQRLVIARTIAVEP 192
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLIIAGASGDDI-RRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600559 193 EVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAAR 237
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISR 202
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
31-265 |
1.04e-20 |
|
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: 87.84 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVdvaelr 110
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILR-----PTSGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVLDeavewALKGAALWEEVKDRLHESALGLsggqQQRLVIARTIA 189
Cdd:TIGR03740 70 HKIGSLIESPPLYENlTARENLKVHTTLLGLPDSRIDE-----VLNIVDLTNTGKKKAKQFSLGM----KQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG------DTDTLFTN 262
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGYQGkinkseNLEKLFVE 220
|
...
gi 15600559 263 PAK 265
Cdd:TIGR03740 221 VVK 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-251 |
1.29e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.22 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAELR-----RRVGMVF 117
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA------------IAGSLPPDSGSILIDGKDVTKLPeykraKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QkpNPF----PK-SIYENVV--------YGLRIqGINKKRVldeavewalkgaalwEEVKDRLHESALG----------- 173
Cdd:COG1101 87 Q--DPMmgtaPSmTIEENLAlayrrgkrRGLRR-GLTKKRR---------------ELFRELLATLGLGlenrldtkvgl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQ--RLVIArTIaVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSDYTAFMYMGK 249
Cdd:COG1101 149 LSGGQRQalSLLMA-TL-TKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
..
gi 15600559 250 LI 251
Cdd:COG1101 227 II 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
40-205 |
1.39e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.90 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAK-QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC-RV-EGEIRLDGhnifaKGVDVAELRRR-VGM 115
Cdd:PRK11650 13 YDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-------MVAGLeRItSGEIWIGG-----RVVNELEPADRdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 116 VFQKPNPFPK-SIYENVVYGLRIQGINK----KRVLDeavewalkgAALWEEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:PRK11650 81 VFQNYALYPHmSVRENMAYGLKIRGMPKaeieERVAE---------AARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 15600559 191 EPEVLLLDEPCSALD 205
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-237 |
1.43e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnRMNDLVDGCR-VEGEIRLDGHNIFAKGV---DV 106
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKsAGSHIELLGRTVQREGRlarDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPK-SIYENVVYG-----------LR-IQGINKKRVLDEAVEWALKGAAlweevkdrlHESALG 173
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRlSVLENVLIGalgstpfwrtcFSwFTREQKQRALQALTRVGMVHFA---------HQRVST 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAAR 237
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
43-229 |
1.93e-20 |
|
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: 86.94 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvDGCRVEGEIRLDGhnifaKGVDVAELRRRVGMVFQKPNP 122
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNG-----QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPK-SIYENVVYG--LRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHEsalGLSGGQQQRLVIARTIAVEPEVLLLDE 199
Cdd:cd03234 93 LPGlTVRETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVK---GISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|
gi 15600559 200 PCSALDPISTLKIEELIYELKSKFTIVIVT 229
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
31-263 |
2.14e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 87.58 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCF-NRMndLVDGCRVEGEIRLDG-HNIFAkgvdVAE 108
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLaGRL--APDHGTATYIMRSGAeLELYQ----LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRV------GMVFQKPNPFPK---SIYENVvyGLRIQGINKK---RVLDEAVEWAlkgaalwEEVK---DRLHESALG 173
Cdd:TIGR02323 78 AERRRlmrtewGFVHQNPRDGLRmrvSAGANI--GERLMAIGARhygNIRATAQDWL-------EEVEidpTRIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250
....*....|..
gi 15600559 252 EFGDTDTLFTNP 263
Cdd:TIGR02323 229 ESGLTDQVLDDP 240
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
63-231 |
2.82e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.69 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRCfnrMNDLVDGCRveGEIRLDGHnifakgvDVAEL-----RRRVGMVFQKPNPFPKSIYENVV--YGL 135
Cdd:PRK10247 40 GPSGCGKSTLLKI---VASLISPTS--GTLLFEGE-------DISTLkpeiyRQQVSYCAQTPTLFGDTVYDNLIfpWQI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 136 RIQGINKKRVLDEAVEWALKGAALWEEVKDrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEEL 215
Cdd:PRK10247 108 RNQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170
....*....|....*...
gi 15600559 216 IYELKSKFTIVI--VTHN 231
Cdd:PRK10247 180 IHRYVREQNIAVlwVTHD 197
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
45-266 |
8.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrmndlvdGCRVEGEIRLDGHNIFAKGVD------VAELRRRVGMVFQ 118
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTL------------ALHLNGLLRPQKGKVLVSGIDtgdfskLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNP--FPKSIYENVVYG---LRIQGINKKRVLDEAV-EWALKgaalweevKDRlHESALGLSGGQQQRLVIARTIAVEP 192
Cdd:PRK13644 85 NPETqfVGRTVEEDLAFGpenLCLPPIEIRKRVDRALaEIGLE--------KYR-HRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 193 EVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQaARVSDYTAFMYMGKLIEFGDTDTLFTNPAKK 266
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-264 |
1.08e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.32 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 27 ESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdgCrveGEIRLDGHNIFAKGVDV 106
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL---------C---GDPRATSGRIVFDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AE------LRRRVGMVFQKPNPFPK-SIYENVVYGlriQGINKKRVLDEAVEWALkgaALWEEVKDRLHESALGLSGGQQ 179
Cdd:PRK11614 70 TDwqtakiMREAVAIVPEGRRVFSRmTVEENLAMG---GFFAERDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDT 258
Cdd:PRK11614 144 QMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDA 223
|
....*.
gi 15600559 259 LFTNPA 264
Cdd:PRK11614 224 LLANEA 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
62-263 |
2.37e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 62 IGPSGCGKSTLLRCFNRmndLVDGcrVEGEIRLDGHNIF-AKGVDVAELRRRVGMVFQKP----NPfPKSIYENVVYGLR 136
Cdd:PRK15079 53 VGESGCGKSTFARAIIG---LVKA--TDGEVAWLGKDLLgMKDDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 137 I--QGINKKRVLDEAVEWALKgAALWEEVKDRL-HEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIE 213
Cdd:PRK15079 127 TyhPKLSRQEVKDRVKAMMLK-VGLLPNLINRYpHE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVV 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 214 ELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK15079 202 NLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
31-255 |
3.82e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.96 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCF-NRMNDLVdgcrVEGEIRLDGHNIFAKGVDVaEL 109
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKYEV----TEGEILFKGEDITDLPPEE-RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPnpfpksiyenvvygLRIQGINkkrvldeavewalkgaalweeVKDRLHESALGLSGGQQQRLVIARTIA 189
Cdd:cd03217 76 RLGIFLAFQYP--------------PEIPGVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 190 VEPEVLLLDEPCSALDpISTLK-IEELIYELKS-KFTIVIVTHNMQQAARV-SDYTAFMYMGKLIEFGD 255
Cdd:cd03217 121 LEPDLAILDEPDSGLD-IDALRlVAEVINKLREeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-262 |
5.78e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 23 DLASESVELEVPGLNLFY--GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlVDgcrvEGEIRLDGHNIf 100
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD-PQ----QGEILLNGQPI- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 aKGVDVAELRRRVGMVFQKPNPFPKSIYENVVyglriqgINKKRVLDEAVEWAL------------KGAALWeevkdrLH 168
Cdd:PRK11160 405 -ADYSEAALRQAISVVSQRVHLFSATLRDNLL-------LAAPNASDEALIEVLqqvgleklleddKGLNAW------LG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 169 ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVsDYTAFMYMG 248
Cdd:PRK11160 471 EGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNG 549
|
250
....*....|....
gi 15600559 249 KLIEFGDTDTLFTN 262
Cdd:PRK11160 550 QIIEQGTHQELLAQ 563
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-259 |
7.04e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 1 MQNETASHGINFdalgrdrqsldlASESVELEVPGLNLfygakqaLFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMN 80
Cdd:PRK10575 1 MQEYTNHSDTTF------------ALRNVSFRVPGRTL-------LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 81 DlvdgcRVEGEIRLDGHNI-------FAKgvDVAELRRrvgmvfQKPNPFPKSIYENVVYG-------LRIQGINKKRVL 146
Cdd:PRK10575 62 P-----PSEGEILLDAQPLeswsskaFAR--KVAYLPQ------QLPAAEGMTVRELVAIGrypwhgaLGRFGAADREKV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 147 DEAVewALKGAalwEEVKDRLHESalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FT 224
Cdd:PRK10575 129 EEAI--SLVGL---KPLAHRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLT 200
|
250 260 270
....*....|....*....|....*....|....*
gi 15600559 225 IVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:PRK10575 201 VIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-259 |
9.45e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 9.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 21 SLDLASESVELEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgCRVEGEIRLDGHNIF 100
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-----SPDAGKITVLGVPVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 AKgvdvAEL-RRRVGMVFQKPNPFPK-SIYEN-VVYGlRIQGInKKRVLDEAVEWALKGAALWEEVKDRLHEsalgLSGG 177
Cdd:PRK13536 107 AR----ARLaRARIGVVPQFDNLDLEfTVRENlLVFG-RYFGM-STREIEAVIPSLLEFARLESKADARVSD----LSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDT 256
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
...
gi 15600559 257 DTL 259
Cdd:PRK13536 257 HAL 259
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-257 |
1.92e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.71 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 24 LASESVELEVPGlnlfyGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRLDGHNIfa 101
Cdd:TIGR01842 317 LSVENVTIVPPG-----GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLAR-------LIVGIwpPTSGSVRLDGADL-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 102 KGVDVAELRRRVGMVFQKPNPFPKSIYENVVyglRIqginKKRVLDEAVEWALKGAALwEEVKDRL---HESALG----- 173
Cdd:TIGR01842 383 KQWDRETFGKHIGYLPQDVELFPGTVAENIA---RF----GENADPEKIIEAAKLAGV-HELILRLpdgYDTVIGpggat 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKS-KFTIVIVTHNMqQAARVSDYTAFMYMGKLIE 252
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRP-SLLGCVDKILVLQDGRIAR 533
|
....*
gi 15600559 253 FGDTD 257
Cdd:TIGR01842 534 FGERD 538
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-233 |
2.05e-18 |
|
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: 80.98 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLVdgcRVEGEIRLDGhnifakgvdvaelrrRVGMVFQKPNPFP 124
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSVSVPG---------------SIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVVYGLRIqgiNKKRVLDeavewALKGAALweeVKD----------RLHESALGLSGGQQQRLVIARTIAVEPEV 194
Cdd:cd03250 80 GTIRENILFGKPF---DEERYEK-----VIKACAL---EPDleilpdgdltEIGEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600559 195 LLLDEPCSALDPistlKIEELIYE------LKSKFTIVIVTHNMQ 233
Cdd:cd03250 149 YLLDDPLSAVDA----HVGRHIFEncilglLLNNKTRILVTHQLQ 189
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-230 |
2.27e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 16 GRDRQSLdlasESVELEVPGLNLFYGA-KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEI 92
Cdd:PRK10790 330 GNDDRPL----QSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLA-------SLLMGYYPltEGEI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 93 RLDGHNIfaKGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLdEAVEWALKGAALWEEVKDRLHESAL 172
Cdd:PRK10790 399 RLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQLAELARSLPDGLYTPLGEQGN 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 173 GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTH 230
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-269 |
3.48e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 20 QSLDLASESVeLEVPGLNLFYGAKQ----ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGCRVEGEIRLD 95
Cdd:PRK10261 3 HSDELDARDV-LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 96 GHN---IFAKGVDVAELRRRVG----MVFQKP----NP-FPksIYENVVYGLRI-QGINKKRVLDEAvewalkgAALWEE 162
Cdd:PRK10261 82 RRSrqvIELSEQSAAQMRHVRGadmaMIFQEPmtslNPvFT--VGEQIAESIRLhQGASREEAMVEA-------KRMLDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 163 VKDRLHESALG-----LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFT--IVIVTHNMQQA 235
Cdd:PRK10261 153 VRIPEAQTILSryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVV 232
|
250 260 270
....*....|....*....|....*....|....
gi 15600559 236 ARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTE 269
Cdd:PRK10261 233 AEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-259 |
5.43e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.31 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMND-------------LVDGCRVEGEIRLDGH 97
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvaLCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 98 NIFAKG-------VDV--------AELRRRVGMVFQKPNPF--PKSIYENVVYGLRIQGINKKRVLDEAVEwalkgaaLW 160
Cdd:TIGR03269 81 PCPVCGgtlepeeVDFwnlsdklrRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD-------LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 161 EEVK--DRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAA 236
Cdd:TIGR03269 154 EMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 15600559 237 RVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
90-244 |
6.76e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 90 GEIRLDGHNIFakGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKD--RL 167
Cdd:PTZ00265 1277 GKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREDVKRACKFAAIDEFIESlpNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 168 HESALG-----LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSD 240
Cdd:PTZ00265 1348 YDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDK 1427
|
....
gi 15600559 241 YTAF 244
Cdd:PTZ00265 1428 IVVF 1431
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
31-263 |
7.10e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndLVDGCRV-EGEIRLDGHNifAKGVDVAEL 109
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNA------LSARLAPdAGEVHYRMRD--GQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 ----RRRV-----GMVFQKPNPfpksiyenvvyGLRIQ---GIN-KKRVLdeAVEWALKG-----AALW-EEVK---DRL 167
Cdd:PRK11701 79 seaeRRRLlrtewGFVHQHPRD-----------GLRMQvsaGGNiGERLM--AVGARHYGdiratAGDWlERVEidaARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 168 HESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFM 245
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVM 225
|
250
....*....|....*...
gi 15600559 246 YMGKLIEFGDTDTLFTNP 263
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDP 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
46-269 |
1.06e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.46 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrMNDLvdGC---RVEGEIRLDGHNIFAKGVD-VAELRRR-VGMVFQKP 120
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTL------MNIL--GCldkPTSGTYRVAGQDVATLDADaLAQLRREhFGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 NPFPK-SIYENV----VYGlriqGINKKRVLDEAVEWALKGAalweeVKDRLHESALGLSGGQQQRLVIARTIAVEPEVL 195
Cdd:PRK10535 96 HLLSHlTAAQNVevpaVYA----GLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSdytafmymgKLIEFGDTDTLFTNPAKKQTE 269
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAE---------RVIEIRDGEIVRNPPAQEKVN 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
46-239 |
1.76e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNI-----FAKgvdvAELR-RRVGMVFQK 119
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT-----PTSGDVIFNGQPMsklssAAK----AELRnQKLGFIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPK-SIYENVVYGLRIQGINKKRVLDEAVEwALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:PRK11629 96 HHLLPDfTALENVAMPLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSE----LSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15600559 199 EPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVS 239
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLqgTAFLVVTHDLQLAKRMS 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
57-261 |
2.03e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 57 RVTAFIGPSGCGKSTLLrcfNRMNDLVDGcrvEGEIRLDGHNIfaKGVDVAELRRRVGMVFQK-PNPFPKSIYEnvvY-G 134
Cdd:COG4138 23 ELIHLIGPNGAGKSTLL---ARMAGLLPG---QGEILLNGRPL--SDWSAAELARHRAYLSQQqSPPFAMPVFQ---YlA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGInkkrVLDEAVEWALkgAALWEEVK--DRLHESALGLSGGQQQRLVIARTI-----AVEPE--VLLLDEPCSALD 205
Cdd:COG4138 92 LHQPAG----ASSEAVEQLL--AQLAEALGleDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 206 PISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFT 261
Cdd:COG4138 166 VAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-268 |
3.23e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALF-----------DVRMNIPKQRVTAFIGPSGCGKST----LLRCFNRmndlvdgcrvEGEIRLD 95
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvvvkNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS----------QGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 96 G---HNIFAKgvDVAELRRRVGMVFQKPNPF--PK-SIYENVVYGLRIQginkkrvldeavEWALKGAALWEEVKDRLHE 169
Cdd:PRK15134 346 GqplHNLNRR--QLLPVRHRIQVVFQDPNSSlnPRlNVLQIIEEGLRVH------------QPTLSAAQREQQVIAVMEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 170 SALG----------LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAAR 237
Cdd:PRK15134 412 VGLDpetrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRA 491
|
250 260 270
....*....|....*....|....*....|.
gi 15600559 238 VSDYTAFMYMGKLIEFGDTDTLFTNPAKKQT 268
Cdd:PRK15134 492 LCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
45-261 |
3.92e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAELRRR--VGMVFQKPN- 121
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKA------------LMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 --PFPkSIYENVV----YG----LRIQGINKKRVLDEAVEWAlkgaalweEVKDRLHESALGLSGGQQQRLVIARTIAVE 191
Cdd:PRK15056 90 dwSFP-VLVEDVVmmgrYGhmgwLRRAKKRDRQIVTAALARV--------DMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAfMYMGKLIEFGDTDTLFT 261
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFT 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-260 |
4.29e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcFNRMNDLVDgcRVEGEIRLDGHNIFAKGVDVAELR 110
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTL---FMNLSGLLR--PQKGAVLWQGKPLDYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNP--FPKSIYENVVYGLRIQGINKK---RVLDEAVEWAlkgaalweEVKDRLHESALGLSGGQQQRLVIA 185
Cdd:PRK13638 77 QQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPEAeitRRVDEALTLV--------DAQHFRHQPIQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 186 RTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFT-IVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-263 |
4.91e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHNIFAkgVDVAELR 110
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA---INGTLT--PTAGTVLVAGDDVEA--LSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPN-PFPKSIYENVVYGlRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIA 189
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMG-RTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 190 VEPEVLLLDEPCSALD---PISTLK-IEELIYELKskfTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK09536 156 QATPVLLLDEPTASLDinhQVRTLElVRRLVDDGK---TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
43-269 |
5.22e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKS----TLLRcfnrmndLVDGCRVE---GEIRLDGHNIFAkgVDVAELRR---- 111
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILR-------LLPSPPVVypsGDIRFHGESLLH--ASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQKP----NPF---PKSIYEnvVYGLRiQGINKKRVLDEAVEwALKGAALwEEVKDRLHESALGLSGGQQQRLVI 184
Cdd:PRK15134 93 KIAMIFQEPmvslNPLhtlEKQLYE--VLSLH-RGMRREAARGEILN-CLDRVGI-RQAAKRLTDYPHQLSGGERQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSA 247
|
....*..
gi 15600559 263 PAKKQTE 269
Cdd:PRK15134 248 PTHPYTQ 254
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
46-233 |
7.38e-17 |
|
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: 77.37 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrMNDLVDGCRVEGEIRLDGHNIFAKGVDVAELRRR--VGMVFQKPNPF 123
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL-----LAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 124 PKSIYENVVYGlriQGINKKRVldEAVewaLKGAALWEEV-------KDRLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:cd03290 92 NATVEENITFG---SPFNKQRY--KAV---TDACSLQPDIdllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600559 197 LDEPCSALD-PISTLKIEELIYEL--KSKFTIVIVTHNMQ 233
Cdd:cd03290 164 LDDPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
31-277 |
1.44e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLV-----DGCRVEGEIRLDGHNIFAkgVD 105
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTgggapRGARVTGDVTLNGEPLAA--ID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAELRRRVGMVFQKPNP-FPKSIYENVVYG----LRIQGINKKR---VLDEAVEWALKGAALWEEVKDrlhesalgLSGG 177
Cdd:PRK13547 78 APRLARLRAVLPQAAQPaFAFSAREIVLLGryphARRAGALTHRdgeIAWQALALAGATALVGRDVTT--------LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIA---------VEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVT--HNMQQAARVSDYTAFMY 246
Cdd:PRK13547 150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLA 229
|
250 260 270
....*....|....*....|....*....|.
gi 15600559 247 MGKLIEFGdtdtlftNPAKKQTEDYITGRYG 277
Cdd:PRK13547 230 DGAIVAHG-------APADVLTPAHIARCYG 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
35-230 |
2.85e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 35 GLNLFYGAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIF-AKGVdvaelrrR 112
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSInPGDRI-GLVGRNGAGKSTLLKI------------LAGELEPDSGEVSiPKGL-------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 113 VGMVFQKPNPFP-KSIYENVVYGLR--IQGINKKRVLDEAVEWALKGAALWEEVKDRLHE--------------SALG-- 173
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGDAelRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilSGLGfp 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 174 ----------LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIyeLKSKFTIVIVTH 230
Cdd:COG0488 143 eedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL--KNYPGTVLVVSH 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
50-250 |
4.84e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.13 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 50 RMNIP--KQRVTAFIGPSGCGKSTLLRCfnrMNDLVDgcRVEGEIRLDGHNIfAKGVDVaeLRRRVGMVFQKPNPFPK-S 126
Cdd:TIGR01257 948 RLNITfyENQITAFLGHNGAGKTTTLSI---LTGLLP--PTSGTVLVGGKDI-ETNLDA--VRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 127 IYENVVYGLRIQGinkkRVLDEAvewALKGAALWEE--VKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSAL 204
Cdd:TIGR01257 1020 VAEHILFYAQLKG----RSWEEA---QLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600559 205 DPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
31-254 |
5.01e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNdlvdgCRVEGEIRLDGHNIFAKGvdvAELR 110
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-----HPDAGSISLCGEPVPSRA---RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQGINKKRVlDEAVEWALKGAALWEEVKDRLHEsalgLSGGQQQRLVIARTIA 189
Cdd:PRK13537 80 QRVGVVPQFDNLDPDfTVRENLLVFGRYFGLSAAAA-RALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 190 VEPEVLLLDEPCSALDPistlKIEELIYE-LKSKF----TIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDP----QARHLMWErLRSLLargkTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
43-263 |
5.64e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.45 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIFAKGVDvaELRRRVGMVFQKPNP 122
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-----DIRFHDIPLTKLQLD--SWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPKSIYENVVYGlriqginKKRVLDEAVEWALKGAALWEEVKdRL---HESALG-----LSGGQQQRLVIARTIAVEPEV 194
Cdd:PRK10789 401 FSDTVANNIALG-------RPDATQQEIEHVARLASVHDDIL-RLpqgYDTEVGergvmLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 195 LLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMqQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
48-227 |
5.91e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.76 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRL-DGHNIfaKGVDVAELRRRVGMVFQKPNPFPKS 126
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIInDSHNL--KDINLKWWRSKIGVVSQDPLLFSNS 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 127 IYENVVYGL-------------RIQGINKKRVLDEAVEWALKGAAL-------------------WEEVKDR-------- 166
Cdd:PTZ00265 476 IKNNIKYSLyslkdlealsnyyNEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknYQTIKDSevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 167 --LHE--SAL-------------GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELK---SKFTIV 226
Cdd:PTZ00265 556 vlIHDfvSALpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITII 635
|
.
gi 15600559 227 I 227
Cdd:PTZ00265 636 I 636
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
31-263 |
1.16e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQ----RVTAFIGPSGCGKStlLRCFNRMNdLVD-GCRVEGE-IRLDGHNIFAkgv 104
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSvkqgEVVGIVGESGSGKS--VSSLAIMG-LIDyPGRVMAEkLEFNGQDLQR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 dVAELRRR------VGMVFQKP----NPFPKSIYEnVVYGLRI-QGINKKRVLDEAVEwalkgaaLWEEV-----KDRLH 168
Cdd:PRK11022 78 -ISEKERRnlvgaeVAMIFQDPmtslNPCYTVGFQ-IMEAIKVhQGGNKKTRRQRAID-------LLNQVgipdpASRLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 169 ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK--FTIVIVTHNMQQAARVSDYTAFMY 246
Cdd:PRK11022 149 VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAHKIIVMY 228
|
250
....*....|....*..
gi 15600559 247 MGKLIEFGDTDTLFTNP 263
Cdd:PRK11022 229 AGQVVETGKAHDIFRAP 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
40-240 |
1.96e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.52 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGhniFAKGVDVAELRRRVGMVF 117
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLK-------ILSGLLQptSGEVRVAG---LVPWKRRKKFLRRIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 -QKPN-----PFPKSIYENVvyglRIQGINK---KRVLDEAVEwalkgaALweEVKDRLHESALGLSGGQQQRLVIARTI 188
Cdd:cd03267 101 gQKTQlwwdlPVIDSFYLLA----AIYDLPParfKKRLDELSE------LL--DLEELLDTPVRQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600559 189 AVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVSD 240
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrERGTTVLLTSHYMKDIEALAR 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
41-257 |
6.82e-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: 74.07 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvEGEIRL--DGHNIFAKGVDV-AELRRRVGMVF 117
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG---EVNVRVgdEWVDMTKPGPDGrGRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 118 QKPNPFP-KSIYENVVYGLRIQgINKKRVLDEAVeWALKGAALWEE-VKDRLHESALGLSGGQQQRLVIARTIAVEPEVL 195
Cdd:TIGR03269 372 QEYDLYPhRTVLDNLTEAIGLE-LPDELARMKAV-ITLKMVGFDEEkAEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 196 LLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTD 257
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
34-254 |
3.33e-14 |
|
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: 69.87 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 34 PGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMnDLVDgcrvEGEIRLDGhnifakgvDVAELrRRV 113
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI-YPPD----SGTVTVRG--------RVSSL-LGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 114 GMVFQkPNpfpKSIYENVVYGLRIQGINKKR---VLDEAVEWAlkgaalweEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:cd03220 92 GGGFN-PE---LTGRENIYLNGRLLGLSRKEideKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVI-VTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
44-277 |
3.74e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDGcrvegEIRLDGHNIfAKGvDVAELRRRVGMVFQKP--- 120
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-----ELLIDDHPL-HFG-DYSYRSQRIRMIFQDPsts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 -NPfPKSIYENVVYGLRIQGINKKRVLDEAVEWALKGAALweeVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDE 199
Cdd:PRK15112 100 lNP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 200 PCSALDPISTLKIEELIYELKSKFTI--VIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYITGRYG 277
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFG 255
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-230 |
1.02e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 25 ASESVELEVPGLNLFYGAKQALF-DVRMNI-PKQRVtAFIGPSGCGKSTLLRCfnrmndlvdgcrvegeirLDGHNIFAK 102
Cdd:COG4178 357 TSEDGALALEDLTLRTPDGRPLLeDLSLSLkPGERL-LITGPSGSGKSTLLRA------------------IAGLWPYGS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 103 G-VDVAELRRrvgMVF--QKPnpfpksiY-------ENVVYGLRIQGINkkrvlDEAVEWALKGAALwEEVKDRLHESAL 172
Cdd:COG4178 418 GrIARPAGAR---VLFlpQRP-------YlplgtlrEALLYPATAEAFS-----DAELREALEAVGL-GHLAERLDEEAD 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 173 ---GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPIStlkiEELIYE-LKSKF---TIVIVTH 230
Cdd:COG4178 482 wdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN----EAALYQlLREELpgtTVISVGH 542
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
31-255 |
1.04e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTL---LrcfnrMNDlvDGCRV-EGEIRLDGHNIFAKGVDv 106
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLakvL-----MGH--PKYEVtSGSILLDGEDILELSPD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 aElRRRVG--MVFQKPNPFP--------KSIYENVvyglRIQGINKKRVLDEAVEWAlkgaalwEEVKdrLHESAL---- 172
Cdd:COG0396 73 -E-RARAGifLAFQYPVEIPgvsvsnflRTALNAR----RGEELSAREFLKLLKEKM-------KELG--LDEDFLdryv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 173 --GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpISTLKI-EELIYELKSK-FTIVIVTHNmqqaAR-----VSDYTA 243
Cdd:COG0396 138 neGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-IDALRIvAEGVNKLRSPdRGILIITHY----QRildyiKPDFVH 212
|
250
....*....|..
gi 15600559 244 FMYMGKLIEFGD 255
Cdd:COG0396 213 VLVDGRIVKSGG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
40-240 |
1.74e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrMN--------DlvdgcrvEGEIRLDGHNIFAKGVDVAeLRR 111
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDGKPVRIRSPRDA-IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 112 RVGMVFQKPNPFPK-SIYENVVYGLRIqgiNKKRVLDeavewalkgaalWEEVKDRLHE--SALG-----------LSGG 177
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLEP---TKGGRLD------------RKAARARIRElsERYGldvdpdakvedLSVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPistLKIEEL---IYELKSK-FTIVIVTHNMQQAARVSD 240
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTP---QEADELfeiLRRLAAEgKSIIFITHKLREVMAIAD 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
46-254 |
1.78e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 70.36 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndLVDGCRVEGEIRLDGhnifakgvdvaelrrRVGMVFQKPNPFPK 125
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHMKG---------------SVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 126 SIYENVVYGLRIQGINKKRVLDeavewalkGAALWEEVK-----DR--LHESALGLSGGQQQRLVIARTIAVEPEVLLLD 198
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLE--------ACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 199 EPCSALDPistlKIEELIYE--------LKSKfTIVIVTHNMQQAARVsDYTAFMYMGKLIEFG 254
Cdd:TIGR00957 786 DPLSAVDA----HVGKHIFEhvigpegvLKNK-TRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
31-230 |
3.12e-13 |
|
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: 65.55 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLVDgcrVEGEIRLDGHNifakgvdvaelr 110
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEP---DEGIVTWGSTV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 rRVGMVFQkpnpfpksiyenvvyglriqginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQQRLVIARTIAV 190
Cdd:cd03221 64 -KIGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSkfTIVIVTH 230
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-254 |
5.60e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 34 PGLNLfygakqALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDvaELRRRV 113
Cdd:TIGR00957 1296 EDLDL------VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNIAKIGLH--DLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 114 GMVFQKPNPFPKSiyenvvygLRIQGINKKRVLDEAVEWALKGAALWEEVK---DRL-HESALG---LSGGQQQRLVIAR 186
Cdd:TIGR00957 1363 TIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWWALELAHLKTFVSalpDKLdHECAEGgenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 187 TIAVEPEVLLLDEPCSALDpistLKIEELIYE-LKSKF---TIVIVTHNMQQaarVSDYTAFMYM--GKLIEFG 254
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVD----LETDNLIQStIRTQFedcTVLTIAHRLNT---IMDYTRVIVLdkGEVAEFG 1501
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
61-263 |
6.22e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 61 FIGPSGCGKSTLLrcfNRMNDLVDGcrvEGEIRLDGHNIfaKGVDVAEL-RRRVGMVFQKPNPFPKSIYEnvvY------ 133
Cdd:PRK03695 27 LVGPNGAGKSTLL---ARMAGLLPG---SGSIQFAGQPL--EAWSAAELaRHRAYLSQQQTPPFAMPVFQ---Yltlhqp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 134 -GLRIQGINKkrVLDEAVEwALKgaalweeVKDRLHESALGLSGGQQQR-------LVIARTIAVEPEVLLLDEPCSALD 205
Cdd:PRK03695 96 dKTRTEAVAS--ALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 206 PISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTNP 263
Cdd:PRK03695 166 VAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
54-248 |
8.64e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 68.27 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 54 PKQRVtAFIGPSGCGKSTLLRCFNRMndlVDGCrvEGEIRLDGHNIFAKGvdVAELRRRVGMVFQKP-----------NP 122
Cdd:PTZ00243 1335 PREKV-GIVGRTGSGKSTLLLTFMRM---VEVC--GGEIRVNGREIGAYG--LRELRRQFSMIPQDPvlfdgtvrqnvDP 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPKSIYENVVYGLRIQGInKKRVLDEAvewalkgaalwEEVKDRLHESALGLSGGQQQRLVIARTIAVEPE-VLLLDEPC 201
Cdd:PTZ00243 1407 FLEASSAEVWAALELVGL-RERVASES-----------EGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 202 SALDPISTLKIEELIYELKSKFTIVIVTHNMQQAAR-----VSDYTAFMYMG 248
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQydkiiVMDHGAVAEMG 1526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
31-255 |
1.08e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPK-QRVtAFIGPSGCGKSTLLRCFnrMNDL-VDgcrvEGEIRLdGHNI----FAKgv 104
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRgDRI-GLIGPNGAGKSTLLKLL--AGELePD----SGTVKL-GETVkigyFDQ-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 DVAELRrrvgmvfqkPNpfpKSIYENVvyglriqginkKRVLDEAVEWAL---------KGAALWEEVKDrlhesalgLS 175
Cdd:COG0488 386 HQEELD---------PD---KTVLDEL-----------RDGAPGGTEQEVrgylgrflfSGDDAFKPVGV--------LS 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 176 GGQQQRLVIARTIAVEPEVLLLDEPCSALDPIStlkIEELIYELKSkF--TIVIVTHNMQQAARVSDytafmymgKLIEF 253
Cdd:COG0488 435 GGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---LEALEEALDD-FpgTVLLVSHDRYFLDRVAT--------RILEF 502
|
..
gi 15600559 254 GD 255
Cdd:COG0488 503 ED 504
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
48-258 |
1.90e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKST-------LLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVaelRRRVGMVFQKp 120
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPA------------SEGEAWLFGQPVDAGDIAT---RRRVGYMSQA- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 121 npFpkSIYE------NVVYGLRIQGINKKRVlDEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVIArtIAV--EP 192
Cdd:NF033858 348 --F--SLYGeltvrqNLELHARLFHLPAAEI-AARVAEMLERFDL-ADVADALPDS---LPLGIRQRLSLA--VAVihKP 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 193 EVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVsDYTAFMYMGKLIefgDTDT 258
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHAGRVL---ASDT 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-233 |
6.13e-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: 65.70 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 30 ELEVPGLNLFY--GAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFNRMndlvdgCRVEGEIRLDGhnIFAKGVDV 106
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVeGGQRV-GLLGRTGSGKSTLLSALLRL------LSTEGEIQIDG--VSWNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGINKKRVLDEAvewALKgaALWEEVKDRLH----ESALGLSGGQQQRL 182
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEV---GLK--SVIEQFPDKLDfvlvDGGYVLSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600559 183 VIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQ 233
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-259 |
1.47e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.38 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 29 VELEvpGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLrcfnrmnDLVDGCRV--EGEIR-LDGhnifakgvD 105
Cdd:NF033858 2 ARLE--GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEvLGG--------D 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 106 VAE--LRRRVG-----MvfqkP-----NPFPK-SIYENVVYGLRIQGINK---KRVLDEavewALKGAALwEEVKDRLhe 169
Cdd:NF033858 65 MADarHRRAVCpriayM----PqglgkNLYPTlSVFENLDFFGRLFGQDAaerRRRIDE----LLRATGL-APFADRP-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 170 sALGLSGGQQQRL-----VIArtiavEPEVLLLDEPCSALDPISTLKIEELIYELKSK---FTIVIVTHNMQQAARVsDY 241
Cdd:NF033858 134 -AGKLSGGMKQKLglccaLIH-----DPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAERF-DW 206
|
250
....*....|....*...
gi 15600559 242 TAFMYMGKLIEFGDTDTL 259
Cdd:NF033858 207 LVAMDAGRVLATGTPAEL 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-272 |
1.53e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 22 LDLASESVELEVPGlnlfyGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvDGCRVEGE-IRLDGhnif 100
Cdd:PRK15093 4 LDIRNLTIEFKTSD-----GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--DNWRVTADrMRFDD---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 akgVDVAEL----RRR-----VGMVFQKP----NPfPKSIYENVVYGlrIQGINKKRVLDEAVEWALKGA-ALWEEV--- 163
Cdd:PRK15093 73 ---IDLLRLspreRRKlvghnVSMIFQEPqsclDP-SERVGRQLMQN--IPGWTYKGRWWQRFGWRKRRAiELLHRVgik 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 164 --KDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAARVS 239
Cdd:PRK15093 147 dhKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQWA 226
|
250 260 270
....*....|....*....|....*....|...
gi 15600559 240 DYTAFMYMGKLIEFGDTDTLFTNPAKKQTEDYI 272
Cdd:PRK15093 227 DKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
54-233 |
2.21e-11 |
|
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: 62.56 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 54 PKQRVtAFIGPSGCGKSTLLRCFNRMndlvdgCRVEGEIRLDGHNifAKGVDVAELRRRVGMVFQKPNPFPKSIYENV-V 132
Cdd:cd03289 29 PGQRV-GLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS--WNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLdP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 133 YGLRiqgiNKKRVLDEAVEWALKgaALWEEVKDRLH----ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPIS 208
Cdd:cd03289 100 YGKW----SDEEIWKVAEEVGLK--SVIEQFPGQLDfvlvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180
....*....|....*....|....*
gi 15600559 209 TLKIEELIYELKSKFTIVIVTHNMQ 233
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
59-231 |
3.33e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 59 TAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFAKGV--DVAELRRRVGMvfqKPNpfpKSIYENVVYG 134
Cdd:PRK13539 31 LVLTGPNGSGKTTLLR-------LIAGLLppAAGTIKLDGGDIDDPDVaeACHYLGHRNAM---KPA---LTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGiNKKRVLDEAVE-WALKGAAlweevkdrlHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIE 213
Cdd:PRK13539 98 AAFLG-GEELDIAAALEaVGLAPLA---------HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170
....*....|....*....
gi 15600559 214 ELIYE-LKSKFTIVIVTHN 231
Cdd:PRK13539 168 ELIRAhLAQGGIVIAATHI 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
60-259 |
4.76e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 60 AFIGPSGCGKSTLLR--CFNRMNDLVdgcrVEGEIRLDGHNIFAKgvdvaELRRRVGMVFQKPNPFPK-SIYENVVYG-- 134
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNalAFRSPKGVK----GSGSVLLNGMPIDAK-----EMRAISAYVQQDDLFIPTlTVREHLMFQah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESAL--GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKI 212
Cdd:TIGR00955 126 LRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600559 213 EELIYELKSKFTIVIVT-HnmQQAARVS---DYTAFMYMGKLIEFGDTDTL 259
Cdd:TIGR00955 206 VQVLKGLAQKGKTIICTiH--QPSSELFelfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-216 |
5.92e-11 |
|
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: 60.33 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 37 NLFY------GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCF-NRMNDLVdgcrVEGEIRLDGHNIfakgvdVAEL 109
Cdd:cd03232 8 NLNYtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGV----ITGEILINGRPL------DKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 RRRVGMVFQKPNPFPKSiyenvvyglriqginkkrvldeavewalkgaalweEVKDRLHESAL--GLSGGQQQRLVIART 187
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL-----------------------------------TVREALRFSALlrGLSVEQRKRLTIGVE 122
|
170 180
....*....|....*....|....*....
gi 15600559 188 IAVEPEVLLLDEPCSALDPISTLKIEELI 216
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
46-237 |
1.50e-10 |
|
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: 61.46 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLVDGcrvEGEIRLDGhnifakgvdvaelrrRVGMVFQKPNPFPK 125
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSG---------------RISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 126 SIYENVVYGL-----RIQGINKKRVLDEAVewalkgAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:TIGR01271 502 TIKDNIIFGLsydeyRYTSVIKACQLEEDI------ALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600559 201 CSALDPISTLKI-EELIYELKSKFTIVIVTHNMQQAAR 237
Cdd:TIGR01271 576 FTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
46-230 |
1.77e-10 |
|
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: 58.32 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 46 LFDVRMNI-PKQRVTaFIGPSGCGKSTLLRCFNRMNDLVDGcRVegeIRLDGHNIFakgvdvaelrrrvgMVFQKPNPFP 124
Cdd:cd03223 17 LKDLSFEIkPGDRLL-ITGPSGTGKSSLFRALAGLWPWGSG-RI---GMPEGEDLL--------------FLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVVYglriqginkkrvldeavewalkgaaLWEEVkdrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSAL 204
Cdd:cd03223 78 GTLREQLIY-------------------------PWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 15600559 205 DPistlKIEELIYE-LKSKFTIVI-VTH 230
Cdd:cd03223 123 DE----ESEDRLYQlLKELGITVIsVGH 146
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-250 |
1.79e-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: 58.60 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLnlfyGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNI--------F 100
Cdd:cd03215 5 LEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAE-------ALFGLRppASGEITLDGKPVtrrsprdaI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 101 AKGVD-VAELRRRVGMVFQKpnpfpkSIYENVVygLRIQginkkrvldeavewalkgaalweevkdrlhesalgLSGGQQ 179
Cdd:cd03215 74 RAGIAyVPEDRKREGLVLDL------SVAENIA--LSSL-----------------------------------LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 180 QRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-200 |
2.04e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.80 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRmnipKQRVTAFIGPSGCGKSTLLRC-FnrmndlvdGCR--VEGEIRLDGHNIFAKGVDVA 107
Cdd:COG1129 257 LEVEGLSVGGVVRDVSFSVR----AGEILGIAGLVGAGRTELARAlF--------GADpaDSGEIRLDGKPVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 eLRRRVGMV---------FQkpnpfPKSIYENVVYGlRIQGINKKRVLDEAVEwalkgAALWEEVKDRL-------HESA 171
Cdd:COG1129 325 -IRAGIAYVpedrkgeglVL-----DLSIRENITLA-SLDRLSRGGLLDRRRE-----RALAEEYIKRLriktpspEQPV 392
|
170 180
....*....|....*....|....*....
gi 15600559 172 LGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
48-250 |
2.89e-10 |
|
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: 60.22 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrMNDLVDGcRVEGEIRLDGHN---------IFAKGVDVAELRRRVGMVFQ 118
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQA---LFGAYPG-KFEGNVFINGKPvdirnpaqaIRAGIAMVPEDRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KpnpfpkSIYENVVYGLrIQGINKKRVLDEAVEWALKGAALweevkDRLHESAL-------GLSGGQQQRLVIARTIAVE 191
Cdd:TIGR02633 354 L------GVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAI-----QRLKVKTAspflpigRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
45-269 |
4.31e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrmNDLVDGC--RVEGEIRLDGhnifakgvDVAELRRRVGMVFQKPNp 122
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTL-------SNIIGGSlsPTVGKVDRNG--------EVSVIAISAGLSGQLTG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 fpksiYENVVYGLRIQGINKKRV---LDEAVEWALKGAALWEEVKDrlhesalgLSGGQQQRLVIARTIAVEPEVLLLDE 199
Cdd:PRK13546 103 -----IENIEFKMLCMGFKRKEIkamTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 200 PCSALDPISTLKIEELIYELK-SKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL------FTNPAKKQTE 269
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkyeaFLNDFKKKSK 246
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
48-230 |
4.86e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRC-FNRMNDLVDGCRVEgeirldghnifakgvdvaelrrrvgmvfQKPNPFP-- 124
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLlAGALKGTPVAGCVD----------------------------VPDNQFGre 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 KSIYENVvygLRIQGIN-KKRVLDEAvewALKGAALWeevKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSA 203
Cdd:COG2401 100 ASLIDAI---GRKGDFKdAVELLNAV---GLSDAVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 15600559 204 LDP----ISTLKIEELIYELKSkfTIVIVTH 230
Cdd:COG2401 167 LDRqtakRVARNLQKLARRAGI--TLVVATH 195
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
37-237 |
5.36e-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: 58.71 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 37 NLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrMNDLVDGcrvEGEIRLDGhnifakgvdvaelrrRVGMV 116
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSG---------------RISFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 117 FQKPNPFPKSIYENVVYGLRIQGINKKRVLdEAVEWALKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:cd03291 104 SQFSWIMPGTIKENIIFGVSYDEYRYKSVV-KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15600559 197 LDEPCSALDPISTLKI-EELIYELKSKFTIVIVTHNMQQAAR 237
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-272 |
1.15e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLVDgcrVEGEIRLDGHNIFAKGVDVAElR 110
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGT---WDGEIYWSGSPLKASNIRDTE-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQKPNPFPK-SIYENVVYGLRIQgINKKRVLDEAVewALKGAALWEEVK---DRLHESALGLSGGQQQRLVIAR 186
Cdd:TIGR02633 78 AGIVIIHQELTLVPElSVAENIFLGNEIT-LPGGRMAYNAM--YLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 187 TIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEfgdtdtlfTNPAK 265
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCDTICVIRDGQHVA--------TKDMS 226
|
....*..
gi 15600559 266 KQTEDYI 272
Cdd:TIGR02633 227 TMSEDDI 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
87-250 |
1.22e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 87 RVEGEIRLDGHNI------------FAKgvdVAELRRRVGMVFQKPNPFpKSIYENVVYGLRIQGINKKRVLDEAVEWAL 154
Cdd:PRK10982 300 KSAGTITLHGKKInnhnaneainhgFAL---VTEERRSTGIYAYLDIGF-NSLISNIRNYKNKVGLLDNSRMKSDTQWVI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 155 KGAalweEVKDRLHESALG-LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFT-IVIVTHNM 232
Cdd:PRK10982 376 DSM----RVKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEM 451
|
170
....*....|....*...
gi 15600559 233 QQAARVSDYTAFMYMGKL 250
Cdd:PRK10982 452 PELLGITDRILVMSNGLV 469
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
43-233 |
1.32e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLDGHNIFAkgvDVAELRRRVGMVF-QK 119
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIK-------MLTGILVptSGEVRVLGYVPFK---RRKEFARRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFP-----------KSIYE--NVVYglriqginKKRvLDEAVEwalkgaALweEVKDRLHESALGLSGGQQQRLVIAr 186
Cdd:COG4586 105 SQLWWdlpaidsfrllKAIYRipDAEY--------KKR-LDELVE------LL--DLGELLDTPVRQLSLGQRMRCELA- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 187 tiAV---EPEVLLLDEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNMQ 233
Cdd:COG4586 167 --AAllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-253 |
1.89e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 5 TASHGINFDALGRDRQSLDLASESVELEVPGLNLFYG--AKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDL 82
Cdd:PTZ00243 633 SASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFElePKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 83 VDGcRVEGEirldghnifakgvdvaelrRRVGMVFQKPNPFPKSIYENVVY-----GLRIQgiNKKRVLDEAVEWALKGA 157
Cdd:PTZ00243 713 SEG-RVWAE-------------------RSIAYVPQQAWIMNATVRGNILFfdeedAARLA--DAVRVSQLEADLAQLGG 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 158 ALWEEVKdrlhESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDP-ISTLKIEELIY-ELKSKfTIVIVTHNMQQA 235
Cdd:PTZ00243 771 GLETEIG----EKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEECFLgALAGK-TRVLATHQVHVV 845
|
250
....*....|....*...
gi 15600559 236 ARvSDYTAFMYMGKlIEF 253
Cdd:PTZ00243 846 PR-ADYVVALGDGR-VEF 861
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
54-258 |
2.56e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 54 PKQRVtAFIGPSGCGKSTLLRCFNrmndlvdgcrveGEIRLD-GHNIFAKGVDVAELRrrvgmvfQKPnpfPK----SIY 128
Cdd:PRK11147 28 DNERV-CLVGRNGAGKSTLMKILN------------GEVLLDdGRIIYEQDLIVARLQ-------QDP---PRnvegTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 129 ENVVYGLRIQGINKKR-------VLDEAVEWALKGAALWEEVKD---------RLHE--SALG---------LSGGQQQR 181
Cdd:PRK11147 85 DFVAEGIEEQAEYLKRyhdishlVETDPSEKNLNELAKLQEQLDhhnlwqlenRINEvlAQLGldpdaalssLSGGWLRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDpISTlkIEELIYELKS-KFTIVIVTH------NMqqAARVSDytafMYMGKLIEF- 253
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirNM--ATRIVD----LDRGKLVSYp 235
|
....*
gi 15600559 254 GDTDT 258
Cdd:PRK11147 236 GNYDQ 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
58-262 |
2.66e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLRCfnrMNDLV--DGcrveGEIRLDGHNiFAKGVDVAELRRRVGMVFQKPNPFPK-SIYENVVYG 134
Cdd:PRK15439 39 VHALLGGNGAGKSTLMKI---IAGIVppDS----GTLEIGGNP-CARLTPAKAHQLGIYLVPQEPLLFPNlSVKENILFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGINKKRVldeavewalkgAALWEE--VKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKI 212
Cdd:PRK15439 111 LPKRQASMQKM-----------KQLLAAlgCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15600559 213 EELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK15439 180 FSRIRELLAQgVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
58-238 |
2.67e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLrcfNRMNDLVDGCRVEGEIRLDGHNIfakgvdVAELRRRVGMVFQKPNPFPK-SIYENVVYG-- 134
Cdd:PLN03211 96 ILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKP------TKQILKRTGFVTQDDILYPHlTVRETLVFCsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 LRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHESAL-GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIE 213
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180
....*....|....*....|....*
gi 15600559 214 ELIYELKSKFTiVIVTHNMQQAARV 238
Cdd:PLN03211 247 LTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-230 |
2.78e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGCRV--EGEIRLdghnifakGVDVae 108
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR-------MITGQEQpdSGTIEI--------GETV-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 lrrRVGMVFQK-----PNpfpKSIYENVVYGLRIQGINKKRVLDEAV--EWALKGAALWEEVKDrlhesalgLSGGQQQR 181
Cdd:TIGR03719 386 ---KLAYVDQSrdaldPN---KTVWEEISGGLDIIKLGKREIPSRAYvgRFNFKGSDQQKKVGQ--------LSGGERNR 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15600559 182 LVIARTIAVEPEVLLLDEPCSALDpISTLK-IEELIYELKSkfTIVIVTH 230
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD-VETLRaLEEALLNFAG--CAVVISH 498
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-251 |
2.88e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKqALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDVAElRRRVGMVFQ 118
Cdd:PRK10762 14 FPGVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSILYLGKEVTFNGPKSSQ-EAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPFPK-SIYENVVYGL----RIQGINKKRVLDEAvewalkgAALWEE--VKDRLHESALGLSGGQQQRLVIARTIAVE 191
Cdd:PRK10762 87 ELNLIPQlTIAENIFLGRefvnRFGRIDWKKMYAEA-------DKLLARlnLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLI 251
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-232 |
4.38e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 35 GLNLFygakqALFdvRMNIPKQ-RVTAFIGPSGCGKSTLLRCFNrmndlvdgcrveGEIR--LdghNIFAKGVDVAE-LR 110
Cdd:PRK13409 84 GVNGF-----KLY--GLPIPKEgKVTGILGPNGIGKTTAVKILS------------GELIpnL---GDYEEEPSWDEvLK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQkpNPFpKSIYEN---VVYglRIQGINK-KRVLDEAVEWALKGA---ALWEEVKDRLH-ESALG-----LSGG 177
Cdd:PRK13409 142 RFRGTELQ--NYF-KKLYNGeikVVH--KPQYVDLiPKVFKGKVRELLKKVderGKLDEVVERLGlENILDrdiseLSGG 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNM 232
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
31-255 |
6.78e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdGCRVEGEIrlDGHNIFAKGVDVAEL- 109
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL--------AGREDYEV--TGGTVEFKGKDLLELs 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 110 -RRRVG----MVFQKP-------NPFPKSIYENVVYGLRIQGINKKRVLDEAVEwalKGAALWEEVKDRLHESA-LGLSG 176
Cdd:PRK09580 72 pEDRAGegifMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLME---EKIALLKMPEDLLTRSVnVGFSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 177 GQQQRLVIARTIAVEPEVLLLDEPCSALDpISTLKI-EELIYELKS-KFTIVIVTHNMQQAARVS-DYTAFMYMGKLIEF 253
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIvADGVNSLRDgKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKS 227
|
..
gi 15600559 254 GD 255
Cdd:PRK09580 228 GD 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
44-240 |
7.73e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 44 QALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDLvdgcrVEGEIRLDGHNI-FAKGVDVaeLRRRVGMVFQKPNP 122
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQP-----DAGSILIDGQEMrFASTTAA--LAAGVAIIYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPK-SIYENVVYGlriQGINKKRVLDEavewalkgAALWEEVKDRLHEsaLG-----------LSGGQQQRLVIARTIAV 190
Cdd:PRK11288 91 VPEmTVAENLYLG---QLPHKGGIVNR--------RLLNYEAREQLEH--LGvdidpdtplkyLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600559 191 EPEVLLLDEPCSALdpiSTLKIEEL---IYELKSKFTIVI-VTHNMQQAARVSD 240
Cdd:PRK11288 158 NARVIAFDEPTSSL---SAREIEQLfrvIRELRAEGRVILyVSHRMEEIFALCD 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
40-232 |
9.19e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDghnifaKGVDVAELRRRVGMVFQK 119
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRV------------VLGLVAPD------EGVIKRNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 120 PNPFPkSIYENVVYGLRIQ-GINKKRVLdeavewalkgAALWEEVKDRLHESAL-GLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PRK09544 76 LYLDT-TLPLTVNRFLRLRpGTKKEDIL----------PALKRVQAGHLIDAPMqKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600559 198 DEPCSALDPISTLKIEELIYELKSKF--TIVIVTHNM 232
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-230 |
1.16e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 36 LNLFYGAKQALfdvrmnipkqrvtafIGPSGCGKSTLLRcfnrmndLVDGcrVEGEIrlDGHNIFAKGVdvaelrrRVGM 115
Cdd:TIGR03719 26 LSFFPGAKIGV---------------LGLNGAGKSTLLR-------IMAG--VDKDF--NGEARPQPGI-------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 116 VFQKPNPFP-KSIYENVVYGLRiqgiNKKRVLDEAVEWALKGA-------ALWEE---VKDRL-------HESAL----- 172
Cdd:TIGR03719 73 LPQEPQLDPtKTVRENVEEGVA----EIKDALDRFNEISAKYAepdadfdKLAAEqaeLQEIIdaadawdLDSQLeiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 173 ------------GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSkfTIVIVTH 230
Cdd:TIGR03719 149 alrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
47-262 |
1.36e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 47 FDVRmniPKQRVtAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIFAKGVdvAELRRRVGMVFQKPNPFPKS 126
Cdd:PLN03130 1260 FEIS---PSEKV-GIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDISKFGL--MDLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 127 IYENvvyglriqginkkrvLDEAVEWalKGAALWE-----EVKDRLHESALGL-----------SGGQQQRLVIARTIAV 190
Cdd:PLN03130 1329 VRFN---------------LDPFNEH--NDADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600559 191 EPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
31-257 |
1.83e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDG----CRVEGEIRLDGHNIFAKGvdv 106
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSK-------VIAGhpayKILEGDILFKGESILDLE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 107 AELRRRVG--MVFQKPNPFPKSIYENVvygLRIqGINKKRVLDEAVEwaLKGAALWEEVKDRLH-----ESAL------G 173
Cdd:CHL00131 78 PEERAHLGifLAFQYPIEIPGVSNADF---LRL-AYNSKRKFQGLPE--LDPLEFLEIINEKLKlvgmdPSFLsrnvneG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpISTLK-IEELIYELK-SKFTIVIVTHNMQQAARVS-DYTAFMYMGKL 250
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKiIAEGINKLMtSENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
....*..
gi 15600559 251 IEFGDTD 257
Cdd:CHL00131 231 IKTGDAE 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
54-262 |
2.53e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 54 PKQRVtAFIGPSGCGKSTLLRCFNRMNDLVdgcrvEGEIRLDGHNIFAKGVdvAELRRRVGMVFQKPNPFPKSIYENvvy 133
Cdd:PLN03232 1261 PSEKV-GVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDVAKFGL--TDLRRVLSIIPQSPVLFSGTVRFN--- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 134 glriqginkkrvLDEAVEWalKGAALWE-----EVKDRLHESALGL-----------SGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PLN03232 1330 ------------IDPFSEH--NDADLWEaleraHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 198 DEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVsDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-246 |
4.04e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 35 GLNLFygakqALFdvRMNIPKQ-RVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIR--LdghNIFAKGVDVAE-LR 110
Cdd:COG1245 84 GENGF-----RLY--GLPVPKKgKVTGILGPNGIGKSTALKI------------LSGELKpnL---GDYDEEPSWDEvLK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 RRVGMVFQkpNPFpKSIYEN---VVYglRIQGINK-KRVLDEAVEWALKGA---ALWEEVKDRLH-ESALG-----LSGG 177
Cdd:COG1245 142 RFRGTELQ--DYF-KKLANGeikVAH--KPQYVDLiPKVFKGTVRELLEKVderGKLDELAEKLGlENILDrdiseLSGG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMY 246
Cdd:COG1245 217 ELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-272 |
5.25e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdgCRV------EGEIRLDGHNIFAKGV 104
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL---------SGVyphgtyEGEIIFEGEELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 105 DVAElRRRVGMVFQKPNPFPK-SIYENVVYGLRIQG---INKKRVLDEAVEWaLKGAALWEEVKDRLHEsalgLSGGQQQ 180
Cdd:PRK13549 77 RDTE-RAGIAIIHQELALVKElSVLENIFLGNEITPggiMDYDAMYLRAQKL-LAQLKLDINPATPVGN----LGLGQQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEfgdtdtl 259
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISDTICVIRDGRHIG------- 223
|
250
....*....|...
gi 15600559 260 fTNPAKKQTEDYI 272
Cdd:PRK13549 224 -TRPAAGMTEDDI 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
48-272 |
6.65e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 48 DVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNI--------FAKGVD-VAELRRRVGMvfq 118
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDIsprspldaVKKGMAyITESRRDNGF--- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 kpnpFPK-SIYENV-------------VYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDrlhesalgLSGGQQQRLVI 184
Cdd:PRK09700 353 ----FPNfSIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALKCHSVNQNITE--------LSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 185 ARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYMGKLIEfgdtdtLFTNp 263
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ------ILTN- 493
|
....*....
gi 15600559 264 AKKQTEDYI 272
Cdd:PRK09700 494 RDDMSEEEI 502
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
85-200 |
7.69e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 85 GCRVEGEIRLDGHNIFAKGVD---------VAELRRRVGMVFqkpnpfPKSIYENVVYGlRIQGINKKRVLDEAVEwaLK 155
Cdd:NF040905 312 GRNISGTVFKDGKEVDVSTVSdaidaglayVTEDRKGYGLNL------IDDIKRNITLA-NLGKVSRRGVIDENEE--IK 382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15600559 156 GAalwEEVKDRLH-------ESALGLSGGQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:NF040905 383 VA---EEYRKKMNiktpsvfQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
50-246 |
7.82e-08 |
|
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: 51.98 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 50 RMNIPKQ-RVTAFIGPSGCGKSTLLRcfnrmndLVDG------CRVEGEIRLDG----------HNIFAKGVDvAELRrr 112
Cdd:cd03236 19 RLPVPREgQVLGLVGPNGIGKSTALK-------ILAGklkpnlGKFDDPPDWDEildefrgselQNYFTKLLE-GDVK-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 113 vgmVFQKP---NPFPKSIYENVvyGLRIQGINKKRVLDEAVEwalkgAALWEEVKDRLHESalgLSGGQQQRLVIARTIA 189
Cdd:cd03236 89 ---VIVKPqyvDLIPKAVKGKV--GELLKKKDERGKLDELVD-----QLELRHVLDRNIDQ---LSGGELQRVAIAAALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMY 246
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-242 |
7.83e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNiFAK--GVDVAE 108
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNIN-YNKldHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRrrVGMVFQKPNPFPK-SIYENVVYGL----RIQGINkkrvldeAVEWA---LKGAALWEEV--KDRLHESALGLSGGQ 178
Cdd:PRK09700 80 LG--IGIIYQELSVIDElTVLENLYIGRhltkKVCGVN-------IIDWRemrVRAAMMLLRVglKVDLDEKVANLSISH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 179 QQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFT-IVIVTHNMQQAARVSD-YT 242
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDrYT 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
54-260 |
9.43e-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: 51.83 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 54 PKQRVtAFIGPSGCGKSTLLRCFNRMNDLVDgcrveGEIRLDGHNIfaKGVDVAELRRRVGMVFQKPNPFPKSIyenvvy 133
Cdd:cd03288 46 PGQKV-GICGRTGSGKSSLSLAFFRMVDIFD-----GKIVIDGIDI--SKLPLHTLRSRLSIILQDPILFSGSI------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 134 glRIQGINKKRVLDEAVEWALKGAALWEEVKDR-------LHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDP 206
Cdd:cd03288 112 --RFNLDPECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15600559 207 ISTLKIEELIYELKSKFTIVIVTHNMQQAARvSDYTAFMYMGKLIEFGDTDTLF 260
Cdd:cd03288 190 ATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-274 |
1.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKqALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCFNRMNDlvdgcRVEGEIRLDGHNIFAKGVDVAeLRRRVGMVFQ 118
Cdd:PRK10982 8 FPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEIDFKSSKEA-LENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPF-PKSIYENV---VYGLRIQGINKKRVLDEAvewalkgAALWEEVKDRL--HESALGLSGGQQQRLVIARTIAVEP 192
Cdd:PRK10982 81 ELNLVlQRSVMDNMwlgRYPTKGMFVDQDKMYRDT-------KAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 193 EVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEfgdtdtlfTNPAKKQTEDY 271
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDK 225
|
...
gi 15600559 272 ITG 274
Cdd:PRK10982 226 IIA 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
63-229 |
1.07e-07 |
|
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: 51.21 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIfAKGVD-----VAELRRRVGMvfqKPNpfpKSIYENVVYGL 135
Cdd:TIGR01189 33 GPNGIGKTTLLR-------ILAGLLrpDSGEVRWNGTPL-AEQRDephenILYLGHLPGL---KPE---LSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 136 RIQGINKKRVLDEAVEWALKGAAlweevkdrlHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEEL 215
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAVGLTGFE---------DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....
gi 15600559 216 IYELKSKFTIVIVT 229
Cdd:TIGR01189 170 LRAHLARGGIVLLT 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
174-250 |
1.07e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 1.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKL 250
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-233 |
1.49e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 43 KQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRC-FNRMNDLVDGCRVegeirldghnifakgvdvaeLRRRVGMVFQKPN 121
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVV--------------------IRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENVVYGLRIQGINKKRVLD-EAVEWALK---GAALWEevkdrLHESALGLSGGQQQRLVIARTIAVEPEVLLL 197
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYWRAIDvTALQHDLDllpGRDLTE-----IGERGVNISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190
....*....|....*....|....*....|....*...
gi 15600559 198 DEPCSALDPISTLKIEE--LIYELKSKfTIVIVTHNMQ 233
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDscMKDELKGK-TRVLVTNQLH 801
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-240 |
1.76e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLfygakQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndlvDGCRVEGEIRLdghnifakgvdvaelr 110
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARL---------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 111 rrvgmvfqkpNPFPKSIYENVVygLRIQGInkKRVLDEAVEWAlkgaalweevkdRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:cd03238 51 ----------ISFLPKFSRNKL--IFIDQL--QFLIDVGLGYL------------TLGQKLSTLSGGELQRVKLASELFS 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 191 EPE--VLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHN---MQQAARVSD 240
Cdd:cd03238 105 EPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
87-259 |
1.80e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 87 RVEGEIRLDGHNIFAKGVD---------VAELRRRVGMVfqkPNpfpKSIYENVVYG-LRIQGINKKRVLD--EAVEWAl 154
Cdd:COG3845 310 PASGSIRLDGEDITGLSPRerrrlgvayIPEDRLGRGLV---PD---MSVAENLILGrYRRPPFSRGGFLDrkAIRAFA- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 155 kgaalwEEVKDR-------LHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIV 226
Cdd:COG3845 383 ------EELIEEfdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVL 456
|
170 180 190
....*....|....*....|....*....|...
gi 15600559 227 IVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTL 259
Cdd:COG3845 457 LISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
57-254 |
3.18e-07 |
|
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: 49.57 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 57 RVTAFIGPSGCGKSTLLRCFNrmNDLVDGCRVEGEIRLDGHN--IFAKgvdvaELRRRVGMVFQKPNPFPKsiyenvvyg 134
Cdd:cd03233 34 EMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIPykEFAE-----KYPGEIIYVSEEDVHFPT--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 lriqgINKKRVLDEAVEwaLKGaalweevkdrlHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTL---- 210
Cdd:cd03233 98 -----LTVRETLDFALR--CKG-----------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALeilk 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600559 211 KIEELIYELKSKfTIVIVTHNMQQAARVSDYTAFMYMGKLIEFG 254
Cdd:cd03233 160 CIRTMADVLKTT-TFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
87-250 |
3.80e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 87 RVEGEIRLDGHNI--------FAKGVD-VAELRRRVGMVFQKpnpfpkSIYENVVYGLrIQGINKKRVLDEAVEWAlkga 157
Cdd:PRK13549 315 RWEGEIFIDGKPVkirnpqqaIAQGIAmVPEDRKRDGIVPVM------GVGKNITLAA-LDRFTGGSRIDDAAELK---- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 158 ALWEEVKdRLH------ESALG-LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVT 229
Cdd:PRK13549 384 TILESIQ-RLKvktaspELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVIS 462
|
170 180
....*....|....*....|.
gi 15600559 230 HNMQQAARVSDYTAFMYMGKL 250
Cdd:PRK13549 463 SELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
63-206 |
3.93e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRCfnrmndLVDGCRVE-GEIRLDGHNifakgVDVAELRRRVGMVFQKPNPFPK-SIYENVVYGLRIQGI 140
Cdd:PRK13543 44 GDNGAGKTTLLRV------LAGLLHVEsGQIQIDGKT-----ATRGDRSRFMAYLGHLPGLKADlSTLENLHFLCGLHGR 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 141 NKKRVLDEAVewALKGAALWEEVKDRlhesalGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDP 206
Cdd:PRK13543 113 RAKQMPGSAL--AIVGLAGYEDTLVR------QLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
63-216 |
4.11e-07 |
|
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: 49.41 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRLDGHNIFAKGVDVAElrrrvGMVFQKPNPFPK---SIYENVVYGLRI 137
Cdd:cd03231 33 GPNGSGKTTLLR-------ILAGLspPLAGRVLLNGGPLDFQRDSIAR-----GLLYLGHAPGIKttlSVLENLRFWHAD 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 138 QGinkkrvlDEAVEWALKGAALwEEVKDRLHESalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELI 216
Cdd:cd03231 101 HS-------DEQVEEALARVGL-NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-262 |
4.87e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 41 GAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEI--RLDGHNIfakgvdvaeLRRRVGMVFQ 118
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISA------------MLGELppRSDASVV---------IRGTVAYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 KPNPFPKSIYENVVYGLRIQGINKKRVLDEAvewALK-------GAALWEevkdrLHESALGLSGGQQQRLVIARTIAVE 191
Cdd:PLN03130 687 VSWIFNATVRDNILFGSPFDPERYERAIDVT---ALQhdldllpGGDLTE-----IGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 192 PEVLLLDEPCSALDPISTLKIEE--LIYELKSKfTIVIVTHNMQQAARVsDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK-TRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
62-229 |
5.36e-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: 50.52 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 62 IGPSGCGKSTLLRcfnrmndlvdgcrVEGEIrldgHNIFAkGVDVAELRRRVGMVFQKPNPFPKSIYENVVYGLRIQGIN 141
Cdd:TIGR00954 484 CGPNGCGKSSLFR-------------ILGEL----WPVYG-GRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 142 KKRVLDEAVEWALKGAAL---------WEEVKDRLHEsalgLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPistlKI 212
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVQLthilereggWSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DV 617
|
170
....*....|....*..
gi 15600559 213 EELIYELKSKFTIVIVT 229
Cdd:TIGR00954 618 EGYMYRLCREFGITLFS 634
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
58-219 |
6.11e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLRCfnrMNDLVDGCRVEGEIRL-DGHnifakGVDvAELRRRVGMVFQKPNPFPKS-IYENVVYGL 135
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLvNGR-----PLD-SSFQRSIGYVQQQDLHLPTStVRESLRFSA 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 136 RIQGINK--KRVLDEAVEWALKGAALwEEVKDRL-HESALGLSGGQQQRLVIARTIAVEPEVLL-LDEPCSALDPISTLK 211
Cdd:TIGR00956 862 YLRQPKSvsKSEKMEYVEEVIKLLEM-ESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
....*...
gi 15600559 212 IEELIYEL 219
Cdd:TIGR00956 941 ICKLMRKL 948
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
123-254 |
6.60e-07 |
|
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: 48.12 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 123 FPKSIYENVVYGLR-----IQGIN---KKRVLDeAVEWALKGAALWEEVKD-------------RLHESALGLSGGQQQR 181
Cdd:cd03227 7 FPSYFVPNDVTFGEgsltiITGPNgsgKSTILD-AIGLALGGAQSATRRRSgvkagcivaavsaELIFTRLQLSGGEKEL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 182 LVIA-----RTIAVEPeVLLLDEPCSALDPISTLKIEELIYE-LKSKFTIVIVTHNMQQAARvsdYTAFMYMGKLIEFG 254
Cdd:cd03227 86 SALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL---ADKLIHIKKVITGV 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
31-244 |
7.11e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC-RVE-GEIRLDGHNIfakGVDVAE 108
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLK-------LIAGLlNPEkGEILFERQSI---KKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 LRRRVGMVFQKP--NPFpKSIYENVVYGLRIQGINKKrvLDEAVEWALKGAALweevkdrlhESALG-LSGGQQQRLVIA 185
Cdd:PRK13540 72 YQKQLCFVGHRSgiNPY-LTLRENCLYDIHFSPGAVG--ITELCRLFSLEHLI---------DYPCGlLSSGQKRQVALL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 186 RTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSKFTIVIVTHNMQQAARVSDYTAF 244
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEY 198
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
58-231 |
1.14e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLRCF----------------NRMNDLVDGCRVEGEIRLDGHNIfakgvdvaELRRRVGMVFQKPN 121
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEASVELEFEHGGKRY--------RIERRQGEFAEFLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 122 PFPKSIYENV--VYGLRI--QGINKKRVLDEAVEWALKGAALWEEVKDRLH------ESALGLSGGQQQRLVIARTIAve 191
Cdd:COG0419 97 AKPSERKEALkrLLGLEIyeELKERLKELEEALESALEELAELQKLKQEILaqlsglDPIETLSGGERLRLALADLLS-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600559 192 pevLLLDEpcSALDPISTLKIEELIYELKskftivIVTHN 231
Cdd:COG0419 175 ---LILDF--GSLDEERLERLLDALEELA------IITHV 203
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
170-261 |
1.41e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 170 SALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKI-EELIYELKSKFTIVIVTHNMQQAARVSDYTAFMYMG 248
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRG 220
|
90
....*....|...
gi 15600559 249 KLIEFGDTDTLFT 261
Cdd:NF000106 221 RVIADGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-252 |
2.08e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKqALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrMNDLvDGcrV------EGEIRLDGHNIFAKGVDVAElrrR 112
Cdd:NF040905 11 FPGVK-ALDDVNLSVREGEIHALCGENGAGKSTL------MKVL-SG--VyphgsyEGEILFDGEVCRFKDIRDSE---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 113 VGMVF--QKPNPFPK-SIYENVVYGlriqgiNkkrvldeavEWALKGAALWEEVKDR---------LHESA------LGL 174
Cdd:NF040905 78 LGIVIihQELALIPYlSIAENIFLG------N---------ERAKRGVIDWNETNRRarellakvgLDESPdtlvtdIGV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600559 175 sgGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIE 252
Cdd:NF040905 143 --GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-250 |
2.21e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 17 RDRQSLDLASESVELEVPGLnlfygAKQALFDVRmnipKQRVTAFIGPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRL 94
Cdd:PRK11288 249 RPRPLGEVRLRLDGLKGPGL-----REPISFSVR----AGEIVGLFGLVGAGRSELMK-------LLYGAtrRTAGQVYL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 95 DGHNIFAKGVDVA---------ELRRRVGMVfqkpnpfP-KSIYENVVYGLRIQGINKKRVLDEAVEwalkgAALWEE-- 162
Cdd:PRK11288 313 DGKPIDIRSPRDAiragimlcpEDRKAEGII-------PvHSVADNINISARRHHLRAGCLINNRWE-----AENADRfi 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 163 ----VKDRLHESALG-LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAA 236
Cdd:PRK11288 381 rslnIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVL 460
|
250
....*....|....
gi 15600559 237 RVSDYTAFMYMGKL 250
Cdd:PRK11288 461 GVADRIVVMREGRI 474
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
58-230 |
3.02e-06 |
|
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: 46.83 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLRC-----------FNRMNDLVDGCRVEGEIRLDGHNIF--AKGVDVaELRRRVgmvfqkpnpfp 124
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaltgelppNSKGGAHDPKLIREGEVRAQVKLAFenANGKKY-TITRSL----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 125 kSIYENVVYgLRIQGINKkrvldeavewalkgaaLWEEVKDRLhesalglSGGQQQ------RLVIARTIAVEPEVLLLD 198
Cdd:cd03240 92 -AILENVIF-CHQGESNW----------------PLLDMRGRC-------SGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190
....*....|....*....|....*....|....*
gi 15600559 199 EPCSALDPIS-TLKIEELIYELKSK--FTIVIVTH 230
Cdd:cd03240 147 EPTTNLDEENiEESLAEIIEERKSQknFQLIVITH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
175-230 |
3.79e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 3.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600559 175 SGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEEliYELKSKFTIVIVTH 230
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLET--YLLKWPKTFIVVSH 399
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
45-262 |
5.75e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 45 ALFDVRMNIPKQRVTAFIGPSGCGKSTLlrcfnrmNDLVDGCRVEGEIRLD------------GHNIFAKGVDVAELRrr 112
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTL-------SNLIAGVTMPNKGTVDikgsaaliaissGLNGQLTGIENIELK-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 113 vgmvfqkpnpfpksiyenvvyGLrIQGINKKRVLD---EAVEWALKGAALWEEVKDrlhesalgLSGGQQQRLVIARTIA 189
Cdd:PRK13545 110 ---------------------GL-MMGLTKEKIKEiipEIIEFADIGKFIYQPVKT--------YSSGMKSRLGFAISVH 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 190 VEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQAARVSDYTAFMYMGKLIEFGDTDTLFTN 262
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
63-229 |
7.97e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 63 GPSGCGKSTLLRcfnrmndLVDGC--RVEGEIRLDGHNIF---------------AKGVDvAELrrrvgmvfqkpnpfpk 125
Cdd:PRK13538 34 GPNGAGKTSLLR-------ILAGLarPDAGEVLWQGEPIRrqrdeyhqdllylghQPGIK-TEL---------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 126 SIYENVVYGLRIQGinkkrVLDEAVEW-ALKGAALweevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSAL 204
Cdd:PRK13538 90 TALENLRFYQRLHG-----PGDDEALWeALAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*
gi 15600559 205 DPISTLKIEELIYELKSKFTIVIVT 229
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILT 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
169-250 |
1.22e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 169 ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL-KSKFTIVIVTHNMQQAARVSDYTAFMYM 247
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
...
gi 15600559 248 GKL 250
Cdd:PRK15439 479 GEI 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-240 |
1.40e-05 |
|
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: 45.09 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 52 NIPKQRVTAFIGPSGCGKSTLLRCFnrmndlvdgcrvEGEIRLDGHNIFAKGVDVAelrrrvgmvfQKPNpFPKSIYENV 131
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEGDIEIELDTVS----------YKPQ-YIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 132 VYGLrIQGINKKRVLDEAVEWALKGAALWEEVKDRLhesALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLK 211
Cdd:cd03237 78 VRDL-LSSITKDFYTHPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|.
gi 15600559 212 IEELI--YELKSKFTIVIVTHNMQQAARVSD 240
Cdd:cd03237 154 ASKVIrrFAENNEKTAFVVEHDIIMIDYLAD 184
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
57-273 |
1.42e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 57 RVTAFIGPSGCGKSTLLRCFNRMNDLVDGcRVEGEIRLDGHnifakgvDVAELRRR----VGMVFQKPNPFPK-SIYENV 131
Cdd:TIGR00956 88 ELTVVLGRPGSGCSTLLKTIASNTDGFHI-GVEGVITYDGI-------TPEEIKKHyrgdVVYNAETDVHFPHlTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 132 VYGLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLH--------ESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSA 203
Cdd:TIGR00956 160 DFAARCKTPQNRPDGVSREEYAKHIADVYMATYGLSHtrntkvgnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 204 LDPISTLkieELIYELKSKFTIVIVTHNM------QQAARVSDYTAFMYMGKLIEFGDTD---TLFTN-----PAKKQTE 269
Cdd:TIGR00956 240 LDSATAL---EFIRALKTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEGYQIYFGPADkakQYFEKmgfkcPDRQTTA 316
|
....
gi 15600559 270 DYIT 273
Cdd:TIGR00956 317 DFLT 320
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
58-205 |
3.15e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 58 VTAFIGPSGCGKSTLLrcfnrmnDLVDGCR----VEGEIRLDGhniFAKGVDVaeLRRRVGMVFQKPNPFPK-SIYENVV 132
Cdd:PLN03140 908 LTALMGVSGAGKTTLM-------DVLAGRKtggyIEGDIRISG---FPKKQET--FARISGYCEQNDIHSPQvTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 133 YG--LR----IQGINKKRVLDEAVEwalkgaaLWEevKDRLHESALGLSG------GQQQRLVIARTIAVEPEVLLLDEP 200
Cdd:PLN03140 976 YSafLRlpkeVSKEEKMMFVDEVME-------LVE--LDNLKDAIVGLPGvtglstEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 15600559 201 CSALD 205
Cdd:PLN03140 1047 TSGLD 1051
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
57-188 |
4.10e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 57 RVTAFIGPSGCGKSTLLRCFNRMNDLVDGcRVEGEIRLDG--HNIFAKGVDVAELRRRVGMVFQKPNPFPksiyenVVYG 134
Cdd:COG4637 22 PLTVLIGANGSGKSNLLDALRFLSDAARG-GLQDALARRGglEELLWRGPRTITEPIRLELEFAEEDERD------LRYE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 135 LRIQGINKK---RVLDEAVeWALKGAALWEEVKDRLHESALglsGGQQQRLVIARTI 188
Cdd:COG4637 95 LELGLPEPGgrpEVKEERL-WLKRGSGGRPFLDFRPKGRAV---GGEPERLDSPESL 147
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
173-235 |
5.16e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 5.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600559 173 GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLK----IEELIYElkSKFTIVIVTHNMQQA 235
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLvrrfVDVLISE--GETQLLFVSHHAEDA 465
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-230 |
6.46e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 36 LNLFYGAKQALfdvrmnipkqrvtafIGPSGCGKSTLLRC-------FNrmndlvdgcrveGEIRLdghnifAKGVdvae 108
Cdd:PRK11819 28 LSFFPGAKIGV---------------LGLNGAGKSTLLRImagvdkeFE------------GEARP------APGI---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 109 lrrRVGMVFQKP--NPfPKSIYENVVYGLRiqgiNKKRVLDE----AVEWALKGA---ALWEE---VKDRLH-------E 169
Cdd:PRK11819 71 ---KVGYLPQEPqlDP-EKTVRENVEEGVA----EVKAALDRfneiYAAYAEPDAdfdALAAEqgeLQEIIDaadawdlD 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 170 S-------ALG----------LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYELKSkfTIVIVTH 230
Cdd:PRK11819 143 SqleiamdALRcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG--TVVAVTH 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
174-241 |
1.24e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600559 174 LSGGQQQRLVIARTI---AVEPEVLLLDEPCSALdpiSTLKIEELIYELKS----KFTIVIVTHNMqQAARVSDY 241
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQSlthqGHTVVIIEHNM-HVVKVADY 880
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
55-232 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 55 KQRVTAFIGPSGCGKSTLLRCFnrMNDLvdGCRVEGEIRLDGHNIFAkgvdvaelrrrvgmvfqkpnpfpksiyenvvyg 134
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--AREL--GPPGGGVIYIDGEDILE--------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 135 lriqginkkrvldeavewalkgAALWEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEE 214
Cdd:smart00382 44 ----------------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180
....*....|....*....|....
gi 15600559 215 LIY------ELKSKFTIVIVTHNM 232
Cdd:smart00382 102 LEElrllllLKSEKNLTVILTTND 125
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
174-233 |
1.85e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600559 174 LSGGQQQRLVIARTIAVEPEVLLLDEPCSALDpISTLK-IEELIYELKSkfTIVIVTHNMQ 233
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLD-VETLElLEELLDSYQG--TVLLVSHDRQ 498
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
165-205 |
2.22e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 2.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15600559 165 DRLHESALG-LSGGQQQRLVIARTIAVEPEVLLLDEPCSALD 205
Cdd:PRK13409 444 ERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
136-248 |
2.29e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 136 RIQGINKKRVlDEAVEWALKGAALwEEVKDRLhesALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEEL 215
Cdd:TIGR01257 2038 RLRGVPAEEI-EKVANWSIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
90 100 110
....*....|....*....|....*....|....
gi 15600559 216 IYE-LKSKFTIVIVTHNMQQAARVSDYTAFMYMG 248
Cdd:TIGR01257 2113 IVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
165-205 |
2.50e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 2.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 15600559 165 DRLHESAL-GLSGGQQQRLVIARTIAVEPEVLLLDEPCSALD 205
Cdd:COG1245 446 EKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
160-240 |
3.25e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 160 WEEVKDRLHESALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDPISTLKIEELIYEL--KSKFTIVIVTHNMQQAAR 237
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDY 137
|
...
gi 15600559 238 VSD 240
Cdd:cd03222 138 LSD 140
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-199 |
3.40e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 39 FYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRCfnrmndlvdgcrVEGEIRLDGHNIFAKGVDVAELrrrvgmvfq 118
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRM------------IAGIMQPSSGNIYYKNCNINNI--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 119 kPNPFPKSIYENVvyGLRIQginkKRVLDEAVEWA--------LKGAALWEEVKDRLHESALGLSGGQQQRLVIARTIAV 190
Cdd:PRK13541 68 -AKPYCTYIGHNL--GLKLE----MTVFENLKFWSeiynsaetLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIAC 140
|
....*....
gi 15600559 191 EPEVLLLDE 199
Cdd:PRK13541 141 QSDLWLLDE 149
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
166-240 |
4.25e-04 |
|
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: 40.70 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 166 RLHESALGLSGGQQQRLVIARTIAVEPEVLL--LDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHN---MQQAARVS 239
Cdd:cd03270 130 TLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDedtIRAADHVI 209
|
.
gi 15600559 240 D 240
Cdd:cd03270 210 D 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-210 |
1.02e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNIPKQRVTAFIGPSGCGKSTLLRcfnrM---NDLVDGcrveGEIRLdghnifakGVDVa 107
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK----MitgQEQPDS----GTIKI--------GETV- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 108 elrrRVGMVFQ-----KPNpfpKSIYENVVYGLRIQGINKKRVLDEAV--EWALKGAALWEEVKDrlhesalgLSGGQQQ 180
Cdd:PRK11819 388 ----KLAYVDQsrdalDPN---KTVWEEISGGLDIIKVGNREIPSRAYvgRFNFKGGDQQKKVGV--------LSGGERN 452
|
170 180 190
....*....|....*....|....*....|
gi 15600559 181 RLVIARTIAVEPEVLLLDEPCSALDpISTL 210
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLD-VETL 481
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-231 |
1.06e-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: 39.68 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 134 GLRIQGINKKRVLDEAVEWALKGAALWEEVKDRLHE-SALGLSGGQQQ--RLVIA-RTIAVEPEVLLLDEPCSALDPIST 209
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElPAFELSDGTKRllALLAAlLSALPKGGLLLIDEPESGLHPKLL 275
|
90 100
....*....|....*....|...
gi 15600559 210 LKIEELIYELKSKFT-IVIVTHN 231
Cdd:pfam13304 276 RRLLELLKELSRNGAqLILTTHS 298
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
174-240 |
1.55e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600559 174 LSGGQQQRLVIARTIAVEPE--VLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMQQ---AARVSD 240
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIID 549
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
62-206 |
1.80e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 62 IGPSGCGKSTLLRcfnrmndLVDGCR--VEGEIRLDGHNIFAKgvDVAELRRRVGMVFQKPNPFPksiyenvvyglRIQG 139
Cdd:PRK10522 355 IGGNGSGKSTLAM-------LLTGLYqpQSGEILLDGKPVTAE--QPEDYRKLFSAVFTDFHLFD-----------QLLG 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600559 140 INKKRVLDEAVEWALKGAALWEEVKDRLHE-SALGLSGGQQQRLVIARTIAVEPEVLLLDEPCSALDP 206
Cdd:PRK10522 415 PEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
40-257 |
1.99e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 40 YGAKQALFDVRMN-IPKQRVtAFIGPSGCGKSTLLRcfnrmndLVDG--CRVEGEIRLdghnifAKGVdvaelrrRVGMV 116
Cdd:PRK10636 322 YGDRIILDSIKLNlVPGSRI-GLLGRNGAGKSTLIK-------LLAGelAPVSGEIGL------AKGI-------KLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 117 FQKPNPFPKSIYENVVYGLRIqginKKRVLDEAVEWALKGAALWeevKDRLHESALGLSGGQQQRLVIARTIAVEPEVLL 196
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLARL----APQELEQKLRDYLGGFGFQ---GDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600559 197 LDEPCSALDpistLKIEELIYELKSKF--TIVIVTHNMQQAARVSDYTAFMYMGKLIEF-GDTD 257
Cdd:PRK10636 454 LDEPTNHLD----LDMRQALTEALIDFegALVVVSHDRHLLRSTTDDLYLVHDGKVEPFdGDLE 513
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-256 |
3.64e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 31 LEVPGLNLFYGAKQALFDVRMNI-PKQRVtAFIGPSGCGKSTLLRCFnrMNDL-VDgcrvEGEIRL-DGHNI-------- 99
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLeAGERL-AIIGENGVGKTTLLRTL--VGELePD----SGTVKWsENANIgyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 100 --FAKGVDVAELRRRvgmvFQKPNPfpksiyenvvyglriqginkkrvLDEAVEWALkGAALWEEvkDRLHESALGLSGG 177
Cdd:PRK15064 393 ydFENDLTLFDWMSQ----WRQEGD-----------------------DEQAVRGTL-GRLLFSQ--DDIKKSVKVLSGG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 178 QQQRLVIARTIAVEPEVLLLDEPCSALDPIStlkIEELIYELKsKF--TIVIVTHNMQ----QAARVSDYTAfmymGKLI 251
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALE-KYegTLIFVSHDREfvssLATRIIEITP----DGVV 514
|
....*
gi 15600559 252 EFGDT 256
Cdd:PRK15064 515 DFSGT 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
60-205 |
3.97e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 60 AFIGPSGCGKSTLLRcfnrmndLVDGcrvegeirldghnifakgvdvaELRRRVGMVFQKPNpfpksiyenvvygLRIQG 139
Cdd:PLN03073 539 AMVGPNGIGKSTILK-------LISG----------------------ELQPSSGTVFRSAK-------------VRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 140 INKKRV--LDEAVEWALKGAALWE---EVKDRLHESALG------------LSGGQQQRLVIARTIAVEPEVLLLDEPCS 202
Cdd:PLN03073 577 FSQHHVdgLDLSSNPLLYMMRCFPgvpEQKLRAHLGSFGvtgnlalqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
...
gi 15600559 203 ALD 205
Cdd:PLN03073 657 HLD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-241 |
4.55e-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: 38.46 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600559 166 RLHESALGLSGGQQQRLVIARTI---AVEPEVLLLDEPCSALDPISTLKIEELIYELKSK-FTIVIVTHNMqQAARVSDY 241
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL-DVIKTADY 900
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
55-73 |
6.31e-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: 36.99 E-value: 6.31e-03
|
| |
