|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-253 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 587.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDV 82
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIAR 162
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDR 242
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
250
....*....|.
gi 123770551 243 RTEDYITGRFG 253
Cdd:COG1117 248 RTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-252 |
0e+00 |
|
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: 500.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVEL 85
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTE 245
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 123770551 246 DYITGRF 252
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-235 |
1.58e-156 |
|
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: 433.92 E-value: 1.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVELR 86
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHkpATGLSGGQQQRLCIARALAI 166
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVI 235
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-253 |
1.64e-146 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 409.94 E-value: 1.64e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDV 82
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKrkLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIAR 162
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFF---------LNGELIEMDRTE 233
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250 260
....*....|....*....|
gi 123770551 234 VIFTKPRDRRTEDYITGRFG 253
Cdd:PRK14243 245 KIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-253 |
2.58e-145 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 406.47 E-value: 2.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVELR 86
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAI 166
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTED 246
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 123770551 247 YITGRFG 253
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-253 |
3.14e-106 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 308.12 E-value: 3.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVELR 86
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAI 166
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQ--ELKKKYTIVIVTHNMQQAARISDRTAFFLN-----GELIEMDRTEVIFTKP 239
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 123770551 240 RDRRTEDYITGRFG 253
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-253 |
8.55e-103 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 299.06 E-value: 8.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVELR 86
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGL-KDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARAL 164
Cdd:PRK14267 85 REVGMVFQYPNPFPHlTIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRT 244
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 123770551 245 EDYITGRFG 253
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-251 |
1.76e-102 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 297.98 E-value: 1.76e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKenFDVVEL 85
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK--MDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPK-SVYENVAYAPKIHGL-KDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARA 163
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRR 243
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*...
gi 123770551 244 TEDYITGR 251
Cdd:PRK14247 241 TEKYVTGR 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-248 |
1.93e-88 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 261.85 E-value: 1.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRI-EGSILFDGVDIYKENFDVVEL 85
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL------EEPdSGTITVDGEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFP-KSVYENVAYAPKIHGlkdKRKLDEIVEkslRGAALWDEV--KDRLHK-PATgLSGGQQQRLCIA 161
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLAPIKVK---KMSKAEAEE---RAMELLERVglADKADAyPAQ-LSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
....*...
gi 123770551 241 DRRTEDYI 248
Cdd:COG1126 229 HERTRAFL 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
5.95e-86 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 256.51 E-value: 5.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPG-VRIEGSILFDGVDIYKenFDVVELRK 87
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIFQ--IDAIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAI 166
Cdd:PRK14246 91 EVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTED 246
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
....*
gi 123770551 247 YITGR 251
Cdd:PRK14246 251 YVIGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-253 |
7.39e-81 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 244.24 E-value: 7.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 11 DLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENfDVVELRKRVG 90
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 91 MVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEV 170
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYITG 250
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
...
gi 123770551 251 RFG 253
Cdd:PRK14271 265 LSG 267
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-240 |
1.22e-71 |
|
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: 218.74 E-value: 1.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY-GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfdVVEL 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDITKKN--LREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQspNP----FPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDevkdRLHKPATGLSGGQQQRLCIA 161
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEH----LADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-226 |
4.92e-71 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 216.63 E-value: 4.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRI-EGSILFDGVDIYKENFDVVEL 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL------EEPdSGTIIIDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFP-KSVYENVAYAP-KIHGlKDKRKLDEIVEKSLRGAALwDEVKDrlHKPATgLSGGQQQRLCIARA 163
Cdd:cd03262 75 RQKVGMVFQQFNLFPhLTVLENITLAPiKVKG-MSKAEAEERALELLEKVGL-ADKAD--AYPAQ-LSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-241 |
7.92e-71 |
|
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: 225.55 E-value: 7.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY-----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPgvRIEGSILFDGVDIYKEN-F 80
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG---LLR--PTSGSILFDGKDLTKLSrR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSP----NPFpKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLhkPATgLSGGQQQ 156
Cdd:COG1123 336 SLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRY--PHE-LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEV 234
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....*..
gi 123770551 235 IFTKPRD 241
Cdd:COG1123 492 VFANPQH 498
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-225 |
4.74e-70 |
|
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: 212.82 E-value: 4.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlipgVRIEGSILFDGVDIYKENFDVVELR 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFP-KSVYENVAYapkihglkdkrkldeivekslrgaalwdevkdrlhkpatGLSGGQQQRLCIARALA 165
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIAL---------------------------------------GLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGE 225
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-237 |
2.00e-67 |
|
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: 208.29 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENFD- 81
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRP---DSGEILVDGQDITGLSEKe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPF-PKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALwDEVKDRLhkPAtGLSGGQQQRLCI 160
Cdd:COG1127 77 LYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKM--PS-ELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-242 |
1.79e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 209.57 E-value: 1.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPG-VRI-EGSILFDGVDIykenFDV-V 83
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-------MIAGfETPdSGRILLDGRDV----TGLpP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRkRVGMVFQSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIAR 162
Cdd:COG3842 75 EKR-NVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGL-EGLADR--YPHQ-LSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDP--ISTMRIE--ELIQELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAklREEMREElrRLQRELGI--TFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
....
gi 123770551 239 PRDR 242
Cdd:COG3842 227 PATR 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-237 |
2.33e-66 |
|
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: 205.43 E-value: 2.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTlnrMNDLIPGVRieGSILFDGVDIYKENF-DVVEL 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPDS--GEVLIDGEDISGLSEaELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPF-PKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARAL 164
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-226 |
1.35e-65 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 202.74 E-value: 1.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGVriEGSILFDGVDIykENFDVVELR 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA---DLDPPT--SGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPKSVYENVAYAPKIHGLK-DKRKLDEIVEKSLRGAALwdevkdrLHKPATGLSGGQQQRLCIARALA 165
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDI-------LDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-251 |
5.02e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.22 E-value: 5.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIYKENfdvVELR 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML--LGLLRPT---SGEVRVLGEDVARDP---AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDevkdRLHKPATGLSGGQQQRLCIARALA 165
Cdd:COG1131 73 RRIGYVPQEPALYPDlTVRENLRFFARLYGL-PRKEARERIDELLELFGLTD----AADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIftkpRDRRT 244
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL----KARLL 223
|
250
....*....|
gi 123770551 245 ED---YITGR 251
Cdd:COG1131 224 EDvflELTGE 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-248 |
4.02e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 203.39 E-value: 4.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndlipgvrIE----GSILFDGVDI--Y 76
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------LErptsGSVLVDGVDLtaL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 77 KENfDVVELRKRVGMVFQSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKslrgaaLWDEV--KDRLHK-PATgLSG 152
Cdd:COG1135 73 SER-ELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGV-PKAEIRKRVAE------LLELVglSDKADAyPSQ-LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMD 230
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
250
....*....|....*...
gi 123770551 231 RTEVIFTKPRDRRTEDYI 248
Cdd:COG1135 224 PVLDVFANPQSELTRRFL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-230 |
8.77e-64 |
|
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: 198.13 E-value: 8.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykenFDVVELR 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFP-KSVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKK--KYTIVIVTHNMQQAARISDRTAFFLNGELIEMD 230
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-225 |
1.39e-63 |
|
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: 197.69 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNF--QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENfdVVEL 85
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGP---TSGEVLVDGKDLTKLS--LKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDevkdRLHKPATGLSGGQQQRLCIARA 163
Cdd:cd03225 74 RRKVGLVFQNPDDqfFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGE 225
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-226 |
2.22e-63 |
|
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: 197.33 E-value: 2.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYK--ENF 80
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PT---SGEVRVDGTDISKlsEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKrkldeivEKSLRGAALWDEV--KDRLHKPATGLSGGQQQR 157
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKK-------ERRERAEELLERVglGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMqQAARISDRTAFFLNGEL 226
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-217 |
4.70e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.00 E-value: 4.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGVriEGSILFDGVDiyke 78
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKPT--SGEVLVDGKP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 nfdVVELRKRVGMVFQSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLrgaalwDEV--KDRLHK-PATgLSGGQ 154
Cdd:COG1116 75 ---VTGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGV-PKAERRERARELL------ELVglAGFEDAyPHQ-LSGGM 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDR 217
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADR 208
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-248 |
5.31e-63 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 199.16 E-value: 5.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQ-ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgvrIE---GSILFDGVDIYKenFDV 82
Cdd:COG1125 2 IEFENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRL--------IEptsGRILIDGEDIRD--LDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFP-KSVYENVAYAPKIHGlKDKRKLDEIVEKSLRGAALW-DEVKDRlhKPATgLSGGQQQRLCI 160
Cdd:COG1125 72 VELRRRIGYVIQQIGLFPhMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDpEEYRDR--YPHE-LSGGQQQRVGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRI-EELI---QELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIF 236
Cdd:COG1125 148 ARALAADPPILLMDEPFGALDPITREQLqDELLrlqRELGK--TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEIL 225
|
250
....*....|..
gi 123770551 237 TKPRDRRTEDYI 248
Cdd:COG1125 226 ANPANDFVADFV 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-241 |
7.68e-63 |
|
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: 196.95 E-value: 7.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYG----NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMN--DlipgvriEGSILFDGVDIYKEnf 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErpW-------SGEVTFDGRPVTRR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSP----NPFpKSVYENVAYAPKIHGLKDKrklDEIVEKSLRGAALWDEVKDRlhKPATgLSGGQQQ 156
Cdd:COG1124 73 RRKAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDR--YPHQ-LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEV 234
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
....*..
gi 123770551 235 IFTKPRD 241
Cdd:COG1124 226 LLAGPKH 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-228 |
2.81e-62 |
|
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: 195.03 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKENFDV 82
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELR-KRVGMVFQSP----NPFpKSVYENVAYAPKIHG-LKDKRKLDEIVEKSLRGAALwdeVKDRLHKPATGLSGGQQQ 156
Cdd:cd03257 77 RKIRrKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGL---PEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-228 |
2.64e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 192.18 E-value: 2.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYK--E 78
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-------ILGGLDRptSGEVLIDGQDISSlsE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 NfDVVELR-KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKrkldeivEKSLRGAALWDEV--KDRLHKPATGLSGGQ 154
Cdd:COG1136 78 R-ELARLRrRHIGFVFQFFNLLPElTALENVALPLLLAGVSRK-------ERRERARELLERVglGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIE 228
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-217 |
7.19e-61 |
|
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: 191.15 E-value: 7.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPG-VRI-EGSILFDGVDIykenf 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLR-------IIAGlERPtSGEVLVDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvVELRKRVGMVFQSPNPFP-KSVYENVAYAPKIHGLKDKRKLDeivekslRGAALWDEV--KDRLHK-PATgLSGGQQQ 156
Cdd:cd03293 69 --TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARE-------RAEELLELVglSGFENAyPHQ-LSGGMRQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDR 217
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-237 |
1.29e-60 |
|
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: 191.41 E-value: 1.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPgvRIEGSILFDGVDIykENFDVVELR 86
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG---LLK--PSSGEVLLDGRDL--ASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPN-PFPKSVYENVAY--APKIHGLKDKRKLD-EIVEKSLRGAALWDevkdrL-HKPATGLSGGQQQRLCIA 161
Cdd:COG1120 75 RRIAYVPQEPPaPFGLTVRELVALgrYPHLGLFGRPSAEDrEAVEEALERTGLEH-----LaDRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-240 |
3.01e-60 |
|
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: 190.10 E-value: 3.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYK-ENFD 81
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PT---SGSVLVDGTDLTLlSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPF-PKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDEVKdrlHKPATgLSGGQQQRLCI 160
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKAD---AYPAQ-LSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 123770551 239 PR 240
Cdd:cd03258 232 PQ 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-240 |
1.06e-59 |
|
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: 191.42 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGVRIEGSILFDGVDIYKenFDV 82
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLLK--LSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELR----KRVGMVFQSP----NPFpKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALwDEVKDRLHKPATGLSGGQ 154
Cdd:COG0444 78 KELRkirgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRT 232
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
....*...
gi 123770551 233 EVIFTKPR 240
Cdd:COG0444 236 EELFENPR 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-239 |
1.74e-59 |
|
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: 189.58 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYG-----NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIY-KENF 80
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITaKKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLKDKrKLDEIVEKSLRGAALWDEVKDRlhKPATgLSGGQQQRL 158
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEE-EAEERVKEALELVGLDEEYLER--SPFE-LSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIF 236
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 123770551 237 TKP 239
Cdd:TIGR04521 232 SDV 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-240 |
1.35e-58 |
|
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: 193.58 E-value: 1.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIP-GVRIEGSILFDGVDIYKenFDVV 83
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPhGGRISGEVLLDGRDLLE--LSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSP--NPFPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIA 161
Cdd:COG1123 80 LRGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
.
gi 123770551 240 R 240
Cdd:COG1123 235 Q 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
15-248 |
1.81e-58 |
|
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: 185.58 E-value: 1.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIykENFDVVELRKRVGMVFQ 94
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--IEP---TSGEIFIDGEDI--REQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFP-KSVYENVAYAPKIHGLKDKRKlDEIVEKSLRGAALWD-EVKDRLhkPATgLSGGQQQRLCIARALAIEPEVLL 172
Cdd:cd03295 83 QIGLFPhMTVEENIALVPKLLKWPKEKI-RERADELLALVGLDPaEFADRY--PHE-LSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 173 MDEPTSALDPISTMRIEE----LIQELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYI 248
Cdd:cd03295 159 MDEPFGALDPITRDQLQEefkrLQQELGK--TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-242 |
6.43e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 185.28 E-value: 6.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV-RI-EGSILFDGVDIYKenfdvVE 84
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-------MIAGLeDPtSGEILIGGRDVTD-----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIAR 162
Cdd:COG3839 72 PKDRnIAMVFQSYALYPhMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGL-EDLLDR--KPKQ-LSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPIS--TMRIE--ELIQELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLrvEMRAEikRLHRRLGT--TTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR 224
|
....
gi 123770551 239 PRDR 242
Cdd:COG3839 225 PANL 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-240 |
3.50e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 183.04 E-value: 3.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGvrIE----GSILFDGVDIYkenFDV 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-------IIAG--LEtpdsGRIVLNGRDLF---TNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIA 161
Cdd:COG1118 71 PPRERRVGFVFQHYALFPHmTVAENIAFGLRVRPP-SKAEIRARVEELLELVQL-EGLADR--YPSQ-LSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
.
gi 123770551 240 R 240
Cdd:COG1118 226 A 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
3.87e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 177.20 E-value: 3.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTlnrMNDLIPgvRIEGSILFDGVDIYKEnf 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVRLFGKPPRRA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvvelRKRVGMVFQSPN---PFPKSVYENVA--YAPKIHGLKDKRKLD-EIVEKSLR--GAAlwdevkDRLHKPATGLSG 152
Cdd:COG1121 74 -----RRRIGYVPQRAEvdwDFPITVRDVVLmgRYGRRGLFRRPSRADrEAVDEALErvGLE------DLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAfFLNGELIEMDR 231
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGP 221
|
250
....*....|...
gi 123770551 232 TEVIFTKPRDRRT 244
Cdd:COG1121 222 PEEVLTPENLSRA 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-226 |
3.21e-54 |
|
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: 172.58 E-value: 3.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIYKENfdvVELR 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDIKKEP---EEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYapkihglkdkrkldeivekslrgaalwdevkdrlhkpatglSGGQQQRLCIARALA 165
Cdd:cd03230 73 RRIGYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKKY-TIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-246 |
4.70e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.47 E-value: 4.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNL-YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRI-EGSILFDGVDIYKENF-DVV 83
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL------VEPtSGEILVDGQDVTALRGrALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPK-SVYENV-----AYAPKIHGL------KDKRkldeivekslRGAALWDEV--KDRLHKPATG 149
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRlSVLTNVlagrlGRTSTWRSLlglfppEDRE----------RALEALERVglADKAYQRADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 150 LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRtafflngeLI 227
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRYADR--------II 218
|
250
....*....|....*....
gi 123770551 228 EMDRTEVIFTKPRDRRTED 246
Cdd:COG3638 219 GLRDGRVVFDGPPAELTDA 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-248 |
1.26e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 173.28 E-value: 1.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPG---VRIEGSiLFDGVDIYKENfDVV 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLE--TPDsgqLNIAGH-QFDFSQKPSEK-AIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPK-SVYENVAYAP-KIHGLKDKRKLDEIVE--KSLRgaalWDEVKDR--LHkpatgLSGGQQQR 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHlTVMENLIEAPcKVLGLSKEQAREKAMKllARLR----LTDKADRfpLH-----LSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEvIF 236
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HF 228
|
250
....*....|..
gi 123770551 237 TKPRDRRTEDYI 248
Cdd:COG4161 229 TQPQTEAFAHYL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-249 |
1.27e-53 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 173.28 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPGvriEGSIlfdgvDIYKENFD----- 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLE--MPR---SGTL-----NIAGNHFDfsktp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 ----VVELRKRVGMVFQSPNPFPK-SVYENVAYAP-KIHGLKD---KRKLDEIVEKsLRgaalWDEVKDR--LHkpatgL 150
Cdd:PRK11124 73 sdkaIRELRRNVGMVFQQYNLWPHlTVQQNLIEAPcRVLGLSKdqaLARAEKLLER-LR----LKPYADRfpLH-----L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 151 SGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGELIEM 229
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
250 260
....*....|....*....|.
gi 123770551 230 -DRTEviFTKPRDRRTEDYIT 249
Cdd:PRK11124 223 gDASC--FTQPQTEAFKNYLS 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-225 |
6.94e-53 |
|
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: 170.69 E-value: 6.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNdLIPgvRIEGSILFDGVDI-YKENFDVVel 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MG-LLP--PRSGSIRFDGRDItGLPPHERA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPK-SVYENV---AYAPKIHglKDKRKLDEIVEkslrgaaLWDEVKDRLHKPATGLSGGQQQRLCIA 161
Cdd:cd03224 74 RAGIGYVPEGRRIFPElTVEENLllgAYARRRA--KRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGE 225
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-225 |
9.13e-53 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 168.72 E-value: 9.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNF--QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIykENFDVVE 84
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PT---SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPKSVYENVayapkihglkdkrkldeivekslrgaalwdevkdrlhkpatgLSGGQQQRLCIARAL 164
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGE 225
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-250 |
1.68e-52 |
|
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: 171.29 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 17 GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRieGSILFDGVDIYKENF-DVVELR-KRVGMVFQ 94
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAAMSRkELRELRrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLM 173
Cdd:cd03294 110 SFALLPhRTVLENVAFGLEVQGV-PRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 174 DEPTSALDP-ISTMRIEELIQ---ELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYIT 249
Cdd:cd03294 185 DEAFSALDPlIRREMQDELLRlqaELQK--TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
.
gi 123770551 250 G 250
Cdd:cd03294 263 G 263
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-231 |
2.27e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 169.46 E-value: 2.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmnDLIPgvrIEGSILFDGVDIYK-ENFDVVE 84
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERP---TSGQVLVNGQDLSRlKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQS----PNpfpKSVYENVAYAPKIHGlKDKRKLDEIVEKSLrgaalwDEV--KDRLHKPATGLSGGQQQRL 158
Cdd:COG2884 77 LRRRIGVVFQDfrllPD---RTVYENVALPLRVTG-KSRKEIRRRVREVL------DLVglSDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDR 231
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-248 |
3.41e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 173.75 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRieGSILFDGVDIYKenFDVVEL----RKRVGMVFQSP 96
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNR---LIEPTA--GEVLIDGEDITK--LSKKELrelrRKKMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NPFP-KSVYENVAYAPKIHGL-KDKRKldEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMD 174
Cdd:COG4175 115 ALLPhRTVLENVAFGLEIQGVpKAERR--ERAREALELVGL----AGWEDSYPDELSGGMQQRVGLARALATDPDILLMD 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 175 EPTSALDP-IST-MRiEELI---QELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDrrteDYI 248
Cdd:COG4175 189 EAFSALDPlIRReMQ-DELLelqAKLKK--TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN----DYV 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-248 |
8.78e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 168.35 E-value: 8.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlIPGvrieGSILFDGVDIYKENFDVVELR 86
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-ITS----GDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAP-KIHGLKdKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARAL 164
Cdd:PRK09493 77 QEAGMVFQQFYLFPHlTALENVMFGPlRVRGAS-KEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 165 AIEPEVLLMDEPTSALDPisTMRIEEL--IQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRD 241
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDP--ELRHEVLkvMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
....*..
gi 123770551 242 RRTEDYI 248
Cdd:PRK09493 230 QRLQEFL 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-248 |
1.07e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.52 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYK-ENFD 81
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLER--PT---SGRVLVDGQDLTAlSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFP-KSVYENVAYAPKIHGlKDKRKLDEIVEKSLRGAALWDEvKDRLhkPATgLSGGQQQRLCI 160
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSsRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDK-ADRY--PAQ-LSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSH 231
|
250
....*....|
gi 123770551 239 PRDRRTEDYI 248
Cdd:PRK11153 232 PKHPLTREFI 241
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-252 |
1.23e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 168.83 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 5 VKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPGvriEGSILFDGVDI-YKENFD-- 81
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLE--TPD---SGEIRVGGEEIrLKPDRDge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 --------VVELRKRVGMVFQSPNPFP-KSVYENVAYAPkIHGLKDKRklDEIVEkslRGAALWDEV--KDRLHK-PATg 149
Cdd:COG4598 82 lvpadrrqLQRIRTRLGMVFQSFNLWShMTVLENVIEAP-VHVLGRPK--AEAIE---RAEALLAKVglADKRDAyPAH- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 150 LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPistmrieELIQE-LK-------KKYTIVIVTHNMQQAARISDRTAFF 221
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmrdlaeEGRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260 270
....*....|....*....|....*....|.
gi 123770551 222 LNGELIEMDRTEVIFTKPRDRRTEDYITGRF 252
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-248 |
2.82e-51 |
|
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: 167.03 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYkenfDVVE 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLR-------LIAGFETptSGEILLDGKDIT----NLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIARA 163
Cdd:cd03300 70 HKRPVNTVFQNYALFPHlTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL-EGYANR--KPSQ-LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 164 LAIEPEVLLMDEPTSALDPI--STMRIEelIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKlrKDMQLE--LKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
....*....
gi 123770551 240 RDRRTEDYI 248
Cdd:cd03300 223 ANRFVADFI 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-246 |
3.10e-51 |
|
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: 166.97 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVriEGSILFDGVDIYKENFDVV-E 84
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG---LVEPT--SGSVLIDGTDINKLKGKALrQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPK-SVYENV-----AYAPKIHGLKDKRKLDEIveksLRGAALWDEV--KDRLHKPATGLSGGQQQ 156
Cdd:cd03256 76 LRRQIGMIFQQFNLIERlSVLENVlsgrlGRRSTWRSLFGLFPKEEK----QRALAALERVglLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRtafflngeLIEMDRTEV 234
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADR--------IVGLKDGRI 223
|
250
....*....|..
gi 123770551 235 IFTKPRDRRTED 246
Cdd:cd03256 224 VFDGPPAELTDE 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-225 |
4.55e-51 |
|
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: 163.95 E-value: 4.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIykENFDVVELRK 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPT---SGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQspnpfpksvyenvayapkihglkdkrkldeivekslrgaalwdevkdrlhkpatgLSGGQQQRLCIARALAIE 167
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGE 225
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-227 |
6.25e-51 |
|
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: 166.07 E-value: 6.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVRI--EGSILFDGVDIykENFDVVE 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-------NLISGFLRptSGSVLFDGEDI--TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFPK-SVYENVAYA------PKIHGLKDKRKLDEIVEKSLRgaaLWDEVK--DRLHKPATGLSGGQ 154
Cdd:cd03219 72 IARLgIGRTFQIPRLFPElTVLENVMVAaqartgSGLLLARARREEREARERAEE---LLERVGlaDLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-229 |
8.12e-51 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 176.18 E-value: 8.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIykENFDV 82
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLK-------LLLGLYEptSGRILIDGIDL--RQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPKSVYENVAYA-PKIHglkdkrklDEIVEKSLRGAALWDEVKD-------RLHKPATGLSGGQ 154
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLGdPDAT--------DEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQ 616
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGELIEM 229
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVED 690
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-178 |
3.00e-50 |
|
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: 161.66 E-value: 3.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKEnfDVVELRKRVGMVFQSPNPFP- 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL--LSP---TEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 101 KSVYENVAYAPKIHGLKDKRKLDEiVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-238 |
1.55e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 163.76 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENfDVVE 84
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLP---TSGKVTVDGLDTLDEE-NLWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSP-NPFPKS-VYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDEvkdRLHKPATgLSGGQQQRLCIAR 162
Cdd:TIGR04520 75 IRKKVGMVFQNPdNQFVGAtVEDDVAFGLENLGV-PREEMRKRVDEALKLVGMEDF---RDREPHL-LSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-248 |
4.05e-49 |
|
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: 161.35 E-value: 4.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQaLKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvrIEGSILFDGVDIYKENFDvvelR 86
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKP---DSGKILLNGKDITNLPPE----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFP-KSVYENVAYAPKIHG---LKDKRKLDEIVEKslrgaALWDEVKDRlhKPATgLSGGQQQRLCIAR 162
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKKRKvdkKEIERKVLEIAEM-----LGIDHLLNR--KPET-LSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
....*...
gi 123770551 241 DRRTEDYI 248
Cdd:cd03299 223 NEFVAEFL 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-227 |
1.64e-48 |
|
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: 160.16 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKEN-FDVVE 84
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDITKLRgKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFP-KSVYENV-----AYAPKIHGL------KDKRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSG 152
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVlhgrlGYKPTWRSLlgrfseEDKERALSALERV--------GLADKAYQRADQLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-250 |
1.80e-48 |
|
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: 163.48 E-value: 1.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 17 GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRieGSILFDGVDIYKEnfDVVEL----RKRVGMV 92
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIEPTA--GQIFIDGENIMKQ--SPVELrevrRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 93 FQSPNPFP-KSVYENVAYAPKIHGL-KDKRKldeivEKSLRGAALWDeVKDRLHKPATGLSGGQQQRLCIARALAIEPEV 170
Cdd:TIGR01186 77 FQQFALFPhMTILQNTSLGPELLGWpEQERK-----EKALELLKLVG-LEEYEHRYPDELSGGMQQRVGLARALAAEPDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYI 248
Cdd:TIGR01186 151 LLMDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
..
gi 123770551 249 TG 250
Cdd:TIGR01186 231 GK 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-227 |
4.08e-48 |
|
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: 158.08 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPgvRIEGSILFDGVDIYKEnfdvvelRK 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLK--PTSGSIRVFGKPLEKE-------RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQSPN---PFPKSVYENVA---YAPKIHGL----KDKRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQR 157
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLmglYGHKGLFRrlskADKAKVDEALERV--------GLSELADRQIGELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAfFLNGELI 227
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL-LLNRTVV 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-248 |
1.23e-47 |
|
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: 161.36 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRIE--GSILFDGVDIY---- 76
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLR-------IIAGLERQtaGTIYQGGRDITrlpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 77 -KENFdvvelrkrvGMVFQSPNPFPK-SVYENVAYapkihGLKDKR-KLDEIVEKSLRGAALWDeVKDRLHKPATGLSGG 153
Cdd:TIGR03265 74 qKRDY---------GIVFQSYALFPNlTVADNIAY-----GLKNRGmGRAEVAERVAELLDLVG-LPGSERKYPGQLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPistmRI-EELIQELKK-----KYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:TIGR03265 139 QQQRVALARALATSPGLLLLDEPLSALDA----RVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
250 260
....*....|....*....|.
gi 123770551 228 EMDRTEVIFTKPRDRRTEDYI 248
Cdd:TIGR03265 215 QVGTPQEIYRHPATPFVADFV 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-217 |
3.08e-47 |
|
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: 156.68 E-value: 3.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNdLIPGVRieGSILFDGVDIYKEN-FDVVelR 86
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SG-LLPPRS--GSIRFDGEDITGLPpHRIA--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYEN---VAYApkihgLKDKRKLDEIVEKSLrgaALWDEVKDRLHKPATGLSGGQQQRLCIAR 162
Cdd:COG0410 78 LGIGYVPEGRRIFPSlTVEENlllGAYA-----RRDRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDR 217
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-227 |
4.56e-47 |
|
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: 154.52 E-value: 4.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGvrIEGSILFDGVDIykENFDVVELRK 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG---LLKP--SSGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQSpnpfpksvyenvayapkihglkdkrkLDEIvekslrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALAIE 167
Cdd:cd03214 74 KIAYVPQA--------------------------LELL------------GLAHLADRPFNELSGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-248 |
4.91e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.07 E-value: 4.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFqaLKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVR--IEGSILFDGVDIYKENfdvVE 84
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLL-------NLIAGFLppDSGRILWNGQDLTALP---PA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKrVGMVFQSPNPFPK-SVYENVAYApkIH-GLK----DKRKLDEIVEK-SLrgaalwDEVKDRlhKPATgLSGGQQQR 157
Cdd:COG3840 70 ERP-VSMLFQENNLFPHlTVAQNIGLG--LRpGLKltaeQRAQVEQALERvGL------AGLLDR--LPGQ-LSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPIstMRIE--ELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTE 233
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
250
....*....|....*
gi 123770551 234 VIFTKPRDRRTEDYI 248
Cdd:COG3840 216 ALLDGEPPPALAAYL 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-248 |
9.43e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.06 E-value: 9.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDG-VDIYKENFDVVEL 85
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTaRSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFP-KSVYENVAYAPKIhglKDKRKLDEIVEkslRGAALWDEV-----KDRLHKPatgLSGGQQQRLC 159
Cdd:PRK11264 84 RQHVGFVFQNFNLFPhRTVLENIIEGPVI---VKGEPKEEATA---RARELLAKVglagkETSYPRR---LSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 160 IARALAIEPEVLLMDEPTSALDP------ISTMRieELIQElkkKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTE 233
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPelvgevLNTIR--QLAQE---KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*
gi 123770551 234 VIFTKPRDRRTEDYI 248
Cdd:PRK11264 230 ALFADPQQPRTRQFL 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-228 |
9.77e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.41 E-value: 9.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY-GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVVEL 85
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-----SGRILIDGVDI--RDLTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPKSVYENVAYA-PKIHglkdkrklDEIVEKSLRGAALWDEVkDRLhkP----------ATGLSGGQ 154
Cdd:COG1132 413 RRQIGVVPQDTFLFSGTIRENIRYGrPDAT--------DEEVEEAAKAAQAHEFI-EAL--PdgydtvvgerGVNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHnmqqaaRIS-----DRTAFFLNGELIE 228
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVE 554
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-227 |
1.42e-46 |
|
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: 154.59 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN--FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGVrieGSILFDGVDIykeNFDVVE 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRPTS---GTAYINGYSI---RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARA 163
Cdd:cd03263 73 ARQSLGYCPQFDALFDElTVREHLRFYARLKGLP-KSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-227 |
1.53e-46 |
|
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: 155.58 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDI-----YKenf 80
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFN-------LITGFYRptSGRILFDGRDItglppHR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvvelRKRVGMV--FQSPNPFPK-SVYENVA-----------YAPKIHGLKDKRKLDEIVEKSLrgAALwDEVK--DRLH 144
Cdd:COG0411 76 -----IARLGIArtFQNPRLFPElTVLENVLvaaharlgrglLAALLRLPRARREEREARERAE--ELL-ERVGlaDRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 145 KPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK--KYTIVIVTHNMQQAARISDRTAFFL 222
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADRIVVLD 227
|
....*
gi 123770551 223 NGELI 227
Cdd:COG0411 228 FGRVI 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-226 |
2.79e-46 |
|
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: 153.56 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKenfdvVE 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLR-------MIAGLEEptSGRIYIGGRDVTD-----LP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFP-KSVYENVAYAPKIHglkdKRKLDEIVEKSLRGAALW--DEVKDRlhKPATgLSGGQQQRLCI 160
Cdd:cd03301 69 PKDRdIAMVFQNYALYPhMTVYDNIAFGLKLR----KVPKDEIDERVREVAELLqiEHLLDR--KPKQ-LSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPI--STMRIE--ELIQELkkKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKlrVQMRAElkRLQQRL--GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-228 |
4.98e-46 |
|
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: 161.46 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYY-GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFD 81
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPKSVYENVA-YAPKIHglkdkrklDEIVEKSLRGAALWDEVKDRLHKPAT-------GLSGG 153
Cdd:COG4988 406 PASWRRQIAWVPQNPYLFAGTIRENLRlGRPDAS--------DEELEAALEAAGLDEFVAALPDGLDTplgeggrGLSGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNGELIE 228
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-240 |
6.10e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.05 E-value: 6.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYY-----------GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndlipgVRIE---- 65
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLL---------LRLEepts 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 66 GSILFDGVDIYKEN-FDVVELRKRVGMVFQSP----NPfPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVK 140
Cdd:COG4608 73 GEILFDGQDITGLSgRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 141 DRL-HKpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpIStmrIE----ELIQELKKKY--TIVIVTHNMQQAAR 213
Cdd:COG4608 152 DRYpHE----FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRH 223
|
250 260
....*....|....*....|....*..
gi 123770551 214 ISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:COG4608 224 ISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-241 |
1.27e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 151.35 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN---FQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFD 81
Cdd:PRK13637 3 IKIENLTHIYMEgtpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPT---SGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSP--NPFPKSVYENVAYAPKIHGLKDkrklDEI---VEKSLRGAAL-WDEVKDrlhKPATGLSGGQQ 155
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSE----EEIenrVKRAMNIVGLdYEDYKD---KSPFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 156 QRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRtafflngeLIEMDRTE 233
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADR--------IIVMNKGK 222
|
....*....
gi 123770551 234 VIFT-KPRD 241
Cdd:PRK13637 223 CELQgTPRE 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-227 |
3.23e-44 |
|
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: 147.79 E-value: 3.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKEnfdvvELRKRVGMVFQ 94
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAK-----ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNP--FPKSVYENVAYapkihGLKDKRKLDEIVEKSLRGAALWDEvKDRlHkPATgLSGGQQQRLCIARALAIEPEVLL 172
Cdd:cd03226 79 DVDYqlFTDSVREELLL-----GLKELDAGNEQAETVLKDLDLYAL-KER-H-PLS-LSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 173 MDEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-233 |
4.26e-44 |
|
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: 148.29 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENFDVvelR 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKP---TSGRATVAGHDVVREPREV---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWdEVKDRLHKPatgLSGGQQQRLCIARALA 165
Cdd:cd03265 73 RRIGIVFQDLSVDDElTGWENLYIHARLYGVP-GAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTE 233
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-229 |
1.53e-43 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 147.30 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY---GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVV 83
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDI--RDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVAYApkihglKDKRKLDEiVEKSLRGAALWD-----------EVKDRlhkpATGLSG 152
Cdd:cd03249 74 WLRSQIGLVSQEPVLFDGTIAENIRYG------KPDATDEE-VEEAAKKANIHDfimslpdgydtLVGER----GSQLSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGELIEM 229
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQ 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-240 |
5.07e-43 |
|
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: 145.94 E-value: 5.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDIYKenfdvVE 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR-------LIAGLErpDSGTILFGGEDATD-----VP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVEK--SLRGAALWDEVKDRLhkPATgLSGGQQQRLCI 160
Cdd:cd03296 71 VQERnVGFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKvhELLKLVQLDWLADRY--PAQ-LSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDpiSTMRiEELIQELKKKY-----TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVI 235
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALD--AKVR-KELRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
....*
gi 123770551 236 FTKPR 240
Cdd:cd03296 225 YDHPA 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-228 |
6.53e-42 |
|
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: 150.30 E-value: 6.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIykENFDVVE 84
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF--LDP---QSGSITLGGVDL--RDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPKSVYENVAYApkihglkDKRKLDEIVEKSLRGAALWDEVK---DRLHKP----ATGLSGGQQQR 157
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLA-------RPDATDEELWAALERVGLGDWLAalpDGLDTWlgegGRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFLNGELIE 228
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-250 |
6.68e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 143.57 E-value: 6.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYK---- 77
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSIVVNGQTINLvrdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 ----ENFDVVEL---RKRVGMVFQSPNPFPK-SVYENVAYAP-KIHGLKdKRKLDEIVEKSLRGAALWDEVKDrlhKPAT 148
Cdd:PRK10619 76 dgqlKVADKNQLrllRTRLTMVFQHFNLWSHmTVLENVMEAPiQVLGLS-KQEARERAVKYLAKVGIDERAQG---KYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 149 GLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250 260
....*....|....*....|...
gi 123770551 228 EMDRTEVIFTKPRDRRTEDYITG 250
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
1.21e-41 |
|
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: 149.06 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKS-TFLRTLNRMNDliPGVRIEGSILFDGVDI 75
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPD--PAAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 76 YKenFDVVELRK----RVGMVFQSP----NPFpKSVYENVAYAPKIH-GLKDKRKLDEIVEkslrgaaLWDEV-----KD 141
Cdd:COG4172 79 LG--LSERELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHrGLSGAAARARALE-------LLERVgipdpER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 142 RL----HKpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARIS 215
Cdd:COG4172 149 RLdaypHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|....*
gi 123770551 216 DRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-241 |
5.99e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 144.32 E-value: 5.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYkenfDVVE 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGFETpdSGRIMLDGQDIT----HVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPK-SVYENVAYapkihGLK-DKRKLDEI---VEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLC 159
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHmTVFENVAF-----GLRmQKTPAAEItprVMEALRMVQL-EEFAQR--KPHQ-LSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPI--STMRIEelIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGElIEMDRTevi 235
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKlrKQMQNE--LKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGR-IEQDGT--- 228
|
....*.
gi 123770551 236 ftkPRD 241
Cdd:PRK09452 229 ---PRE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-236 |
1.29e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 141.14 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENFDV 82
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLKDK---RKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQR 157
Cdd:PRK13636 78 MKLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDevrKRVDNALKRT--------GIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRtafflngeLIEMDRTEVI 235
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDN--------VFVMKEGRVI 221
|
.
gi 123770551 236 F 236
Cdd:PRK13636 222 L 222
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
15-218 |
2.50e-40 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 138.15 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDI--YKENfDVVELRKRVGMV 92
Cdd:TIGR02673 11 YPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA--LTPS---RGQVRIAGEDVnrLRGR-QLPLLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 93 FQSPNPFP-KSVYENVAYAPKIHGlKDKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVL 171
Cdd:TIGR02673 85 FQDFRLLPdRTVYENVALPLEVRG-KKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123770551 172 LMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRT 218
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATHDLSLVDRVAHRV 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-248 |
7.91e-40 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 139.94 E-value: 7.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 37 LIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKenfdVVELRKRVGMVFQSPNPFPK-SVYENVAYAPKIHG 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHmTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 116 LkDKRKLDEIVEKSLRGAALWDEVKDRLHKpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpistMRIEELIQ-E 194
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQlE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 195 LKKKY-----TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYI 248
Cdd:TIGR01187 143 LKTIQeqlgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-227 |
8.76e-40 |
|
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: 136.55 E-value: 8.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIyKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGVriEGSILFDGVDIYKenfDVVELR 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILA---TLTPPS--SGTIRIDGQDVLK---QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRkLDEIVEKSLRGAALWDevkdRLHKPATGLSGGQQQRLCIARALA 165
Cdd:cd03264 72 RRIGYLPQEFGVYPNfTVREFLDYIAWLKGIPSKE-VKARVDEVLELVNLGD----RAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-233 |
9.92e-40 |
|
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: 139.06 E-value: 9.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKEnfdVVELRKRVGMVFQ 94
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARVAGYDVVRE---PRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWDEVKdrlhKPATGLSGGQQQRLCIARALAIEPEVLLM 173
Cdd:TIGR01188 74 YASVDEDlTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAAD----RPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 174 DEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTE 233
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-227 |
2.14e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.56 E-value: 2.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNfQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlipgVRIEGSILFDGVDIYKENfdVVE 84
Cdd:PRK13647 5 IEVEDLHFRYkdGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-----LPQRGRVKVMGREVNAEN--EKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDevkdRLHKPATGLSGGQQQRLCIAR 162
Cdd:PRK13647 77 VRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWD----FRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-237 |
4.08e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKEN 79
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQ---SGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 FDvvELRKRVGMVFQSP-NPF-PKSVYENVAYapkihGLKDKR----KLDEIVEKslrgAALWDEVKDRLHKPATGLSGG 153
Cdd:PRK13632 78 LK--EIRKKIGIIFQNPdNQFiGATVEDDIAF-----GLENKKvppkKMKDIIDD----LAKKVGMEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAArISDRTAFFLNGELIEMDR 231
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
....*.
gi 123770551 232 TEVIFT 237
Cdd:PRK13632 226 PKEILN 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-227 |
6.13e-39 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 134.73 E-value: 6.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 24 NISLDIyKNEVTALIGPSGCGKSTFLRTLNRMNDLIPG-VRIEGSILFDGvdiyKENFDVVELRKRVGMVFQSPNPFPK- 101
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtIVLNGTVLFDS----RKKINLPPQQRKIGLVFQQYALFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENVAYAPKIHGLKDKRKLdeiVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIARALAIEPEVLLMDEPTSALD 181
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRIS---VDELLDLLGL-DHLLNR--YPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123770551 182 PISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-240 |
1.27e-38 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 140.98 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY-----------GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGvriEGSILFDGVDI 75
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPS---EGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 76 YKENF-DVVELRKRVGMVFQspNPF----PK-SVYENVAYAPKIHGLK-DKRKLDEIVEKSLRGAALWDEVKDRL-HKpa 147
Cdd:COG4172 350 DGLSRrALRPLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRYpHE-- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 148 tgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGE 225
Cdd:COG4172 426 --FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDGK 503
|
250
....*....|....*
gi 123770551 226 LIEMDRTEVIFTKPR 240
Cdd:COG4172 504 VVEQGPTEQVFDAPQ 518
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-227 |
2.16e-38 |
|
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: 133.26 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFDV 82
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPD---AGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 velRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKD---KRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRL 158
Cdd:cd03266 77 ---RRRLGFVSDSTGLYDRlTARENLEYFAGLYGLKGdelTARLEELADRL--------GMEELLDRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-211 |
2.57e-38 |
|
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: 132.16 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFDVVELRKRVGMVFQ 94
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQ---SGAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNP--FPKSVYENVAYAPKIHGLKDKRkLDEIVEKSLrgAALwdEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLL 172
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNLGLSEAE-VERRVREAL--TAV--GASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123770551 173 MDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQA 211
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-239 |
5.78e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 134.05 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFDVVEL 85
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPT---SGEVLIKGEPIKYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDEVKdrlhKPATGLSGGQQQRLCIARA 163
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGMEGFEN----KPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-234 |
9.56e-38 |
|
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: 131.88 E-value: 9.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNdLIPGVRieGSILFDGVDIYK-ENFDVVelR 86
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MG-LLPVKS--GSIRLDGEDITKlPPHERA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVEkslrgaaLWDEVKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:TIGR03410 75 AGIAYVPQGREIFPRlTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELI------EMDRTEV 234
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADRYYVMERGRVVasgagdELDEDKV 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-228 |
2.00e-37 |
|
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: 130.41 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTlnrMNDLIPGVriEGSILFDGvdiyKENFDVVELR 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIKPD--SGEITFDG----KSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRkLDEIVekslrgaalwDEV--KDRLHKPATGLSGGQQQRLCIARA 163
Cdd:cd03268 72 RRIGALIEAPGFYPNlTARENLRLLARLLGIRKKR-IDEVL----------DVVglKDSAKKKVKGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-214 |
2.02e-37 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 131.20 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVVELRKRVGMVFQSPNPFP 100
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDV--RDYTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENVAYApkihglkDKRKLDEIVEKSLRGAALWD---EVKDRLHKP----ATGLSGGQQQRLCIARALAIEPEVLLM 173
Cdd:cd03251 90 DTVAENIAYG-------RPGATREEVEEAARAANAHEfimELPEGYDTVigerGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123770551 174 DEPTSALDPISTMRIEELIQELKKKYTIVIVTHNM---QQAARI 214
Cdd:cd03251 163 DEATSALDTESERLVQAALERLMKNRTTFVIAHRLstiENADRI 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-235 |
2.18e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.07 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGVRI--EGSILFDGVDIykENF 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILS-------GVYQpdSGEILLDGEPV--RFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVE-LRKRVGMVFQSPNPFPK-SVYENVA--YAPKIHGLKDKRKLDEIVEKSLR--GAALwdevkdRLHKPATGLSGGQ 154
Cdd:COG1129 72 SPRDaQAAGIAIIHQELNLVPNlSVAENIFlgREPRRGGLIDWRAMRRRARELLArlGLDI------DPDTPVGDLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI------ 227
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVgtgpva 225
|
....*...
gi 123770551 228 EMDRTEVI 235
Cdd:COG1129 226 ELTEDELV 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-241 |
2.31e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.84 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIP---GVRIEGSILFDGvdiyKENFDVVELRKRVGMVFQSPN 97
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPtsgTVTIGERVITAG----KKNKKLKPLRKKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 P--FPKSVYENVAYAPKIHGLKD---KRKLDEIVEksLRGaaLWDEVkdrLHKPATGLSGGQQQRLCIARALAIEPEVLL 172
Cdd:PRK13634 96 HqlFEETVEKDICFGPMNFGVSEedaKQKAREMIE--LVG--LPEEL---LARSPFELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 173 MDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRD 241
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-208 |
2.94e-37 |
|
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: 130.40 E-value: 2.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIykENFD 81
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLK-------LLAGLYKptSGSVLLDGTDI--RQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPKSVYENVAYAPKIHglKDKRKL--------DEIVEKSLRGAALwdEVKDRlhkpATGLSGG 153
Cdd:cd03245 73 PADLRRNIGYVPQDVTLFYGTLRDNITLGAPLA--DDERILraaelagvTDFVNKHPNGLDL--QIGER----GRGLSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNM 208
Cdd:cd03245 145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-242 |
3.92e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 133.67 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV--RIEGSILFDGVDIYKenfdvVE 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLehQTSGHIRFHGTDVSR-----LH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFPK-SVYENVAYA---------PKIHGLKDK-RKLDEIVEKSlrgaalwdEVKDRLhkPATgLSG 152
Cdd:PRK10851 71 ARDRkVGFVFQHYALFRHmTVFDNIAFGltvlprrerPNAAAIKAKvTQLLEMVQLA--------HLADRY--PAQ-LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDpiSTMRIE------ELIQELkkKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEEL--KFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
250
....*....|....*.
gi 123770551 227 IEMDRTEVIFTKPRDR 242
Cdd:PRK10851 216 EQAGTPDQVWREPATR 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-206 |
5.09e-37 |
|
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: 136.26 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIykENFDVVELRKRVGMVFQ 94
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF--VDPT---EGSIAVNGVPL--ADADADSWRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFPKSVYENVAyapkiHGLKDKRklDEIVEKSLRGAALWDEVKDR---LHKP----ATGLSGGQQQRLCIARALAIE 167
Cdd:TIGR02857 404 HPFLFAGTIAENIR-----LARPDAS--DAEIREALERAGLDEFVAALpqgLDTPigegGAGLSGGQAQRLALARAFLRD 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTH 206
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-236 |
5.18e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 5.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfdVV 83
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPE---AGTITVGGMVLSEET--VW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSP-NPFPKS-VYENVAYAPKIHGLKDkrklDEIVEKSlrGAALwDEV--KDRLHKPATGLSGGQQQRLC 159
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFVGAtVQDDVAFGLENIGVPR----EEMVERV--DQAL-RQVgmEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTEVIF 236
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-229 |
5.53e-37 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 130.04 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYKENFDvvE 84
Cdd:cd03254 2 EIEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQ---KGQILIDGIDIRDISRK--S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPKSVYENVAYApkihglkDKRKLDEIVEKSLRGAALWDEVKDR-------LHKPATGLSGGQQQR 157
Cdd:cd03254 75 LRSMIGVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGELIEM 229
Cdd:cd03254 148 LAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIEE 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-239 |
6.13e-37 |
|
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: 133.30 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 11 DLNLYYGNFqALkNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPG--------VRIEGSILFD---GVDIYKEn 79
Cdd:COG4148 6 DFRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLR-------AIAGlerpdsgrIRLGGEVLQDsarGIFLPPH- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 fdvvelRKRVGMVFQSPNPFP-KSVYENVAYAPK-IHGLKDKRKLDEIVEksLRG-AALwdevkdrLHKPATGLSGGQQQ 156
Cdd:COG4148 76 ------RRRIGYVFQEARLFPhLSVRGNLLYGRKrAPRAERRISFDEVVE--LLGiGHL-------LDRRPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIEMDRTEV 234
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAE 220
|
....*
gi 123770551 235 IFTKP 239
Cdd:COG4148 221 VLSRP 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-248 |
1.00e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 133.04 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPgvrIEGSILFDGVDIYkenfDVVELR 86
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QP---TAGQIMLDGVDLS----HVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYapkihGLK-DKRKLDEI---VEKSLRGAALWDEVKDRLHKpatgLSGGQQQRLCIA 161
Cdd:PRK11607 91 RPINMMFQSYALFPHmTVEQNIAF-----GLKqDKLPKAEIasrVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIE-ELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
....*....
gi 123770551 240 RDRRTEDYI 248
Cdd:PRK11607 242 TTRYSAEFI 250
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-229 |
1.79e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.60 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNF----QALKNISLDIYKNEVTALIGPSGCGKSTFLrtlNRMNDLIPGVriEGSILFDGVDIYKENFDv 82
Cdd:COG4525 4 LTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGFLAPS--SGEITLDGVPVTGPGAD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 velrkRvGMVFQSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDEVKDRLHKpatgLSGGQQQRLCIA 161
Cdd:COG4525 78 -----R-GVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLALVGLADFARRRIWQ----LSGGMRQRVGIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQaarisdrtAFFLNGELIEM 229
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEE--------ALFLATRLVVM 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-226 |
1.93e-36 |
|
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: 128.29 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPgvrIEGSILFDGVDI--YKENfDVV 83
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LP---TSGTIRVNGQDVsdLRGR-AIP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPK-SVYENVAYAPKI--HGLKDKRKldeivekslRGAALWDEV--KDRLHKPATGLSGGQQQRL 158
Cdd:cd03292 75 YLRRKIGVVFQDFRLLPDrNVYENVAFALEVtgVPPREIRK---------RVPAALELVglSHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-227 |
5.01e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGvriEGSILFDGVDIykENFDVVELR 86
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPD---SGEVRLNGRPL--ADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPN-PFPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDeVKDRLHkpaTGLSGGQQQRLCIARALA 165
Cdd:PRK13548 76 RRRAVLPQHSSlSFPFTVEEVVAMGRAPHGL-SRAEDDALVAAALAQVDLAH-LAGRDY---PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 166 ------IEPEVLLMDEPTSALDP---ISTMRieeLIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLahqHHVLR---LARQLAHErgLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-227 |
6.44e-36 |
|
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: 125.23 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGVRI--EGSILFDGVDIykENFDVVE 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLYKpdSGEILVDGKEV--SFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 -LRKRVGMVFQspnpfpksvyenvayapkihglkdkrkldeivekslrgaalwdevkdrlhkpatgLSGGQQQRLCIARA 163
Cdd:cd03216 72 aRRAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-227 |
1.08e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.69 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIYKENfdvvelR 86
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGILAPD---SGEVLWDGEPLDPED------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVG-MvfqspnP-----FPK-SVYENVAYAPKIHGLK---DKRKLDEIVEKslrgaaLwdEVKDRLHKPATGLSGGQQQ 156
Cdd:COG4152 71 RRIGyL------PeerglYPKmKVGEQLVYLARLKGLSkaeAKRRADEWLER------L--GLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIV-THNMQQAARISDRTAFFLNGELI 227
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-229 |
1.17e-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: 126.96 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVVELRKRVGMVFQ 94
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI--REVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFPKSVYENVAYApkihglkDKRKLDEIVEKSLRGAALWDEVKDRLHKPAT-------GLSGGQQQRLCIARALAIE 167
Cdd:cd03253 83 DTVLFNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTivgerglKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNGELIEM 229
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-234 |
3.32e-35 |
|
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: 125.62 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKENF 80
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLG-------LLAGLDRptSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 D-VVELR-KRVGMVFQS----PNpfpKSVYENVAYAPKIHGLKDKRKldeivekslRGAALWDEV--KDRL-HKPAtGLS 151
Cdd:COG4181 82 DaRARLRaRHVGFVFQSfqllPT---LTALENVMLPLELAGRRDARA---------RARALLERVglGHRLdHYPA-QLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 152 GGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIEM 229
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
....*
gi 123770551 230 DRTEV 234
Cdd:COG4181 228 TAATA 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-235 |
4.35e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.74 E-value: 4.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfDVVELRKRVGMVFQSPNP-- 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPS---EGKVYVDGLDTSDEE-NLWDIRNKAGMVFQNPDNqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 FPKSVYENVAYAPKIHGLKDKrKLDEIVEKSLRGAALWDEvkdRLHKPATgLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:PRK13633 99 VATIVEEDVAFGPENLGIPPE-EIRERVDESLKKVGMYEY---RRHAPHL-LSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 179 ALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRtafflngeLIEMDRTEVI 235
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADR--------IIVMDSGKVV 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-239 |
4.94e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.46 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDL-NLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfdVVEL 85
Cdd:PRK13652 4 IETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPT---SGSVLIRGEPITKEN--IREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNP--FPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRL-HKpatgLSGGQQQRLCIAR 162
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVpHH----LSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-239 |
8.64e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.10 E-value: 8.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKE--NFDVVELRKRVGMVFQSPN 97
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHITPEtgNKNLKKLRKKVSLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 P--FPKSVYENVAYAPKIHGLKDKrKLDEIVEKSLRGAALWDEVKDrlhKPATGLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:PRK13641 96 AqlFENTVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDLIS---KSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 176 PTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-237 |
1.03e-34 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 124.74 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKenFDVVEL 85
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTP---QSGTVFLGDKPISM--LSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPnPFPK--SVYENVAYAPKIH-------GLKDKRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQ 156
Cdd:PRK11231 75 ARRLALLPQHH-LTPEgiTVRELVAYGRSPWlslwgrlSAEDNARVNQAMEQT--------RINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVI 235
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
..
gi 123770551 236 FT 237
Cdd:PRK11231 226 MT 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-236 |
2.85e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.47 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlipgVRIEGSILFDGVDI--YKENFDVVELRKRVGMVFQSPNP 98
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 --FPKSVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWDEVKDRlhKPATgLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFGVS-QEEAEALAREKLALVGISESLFEK--NPFE-LSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 177 TSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIF 236
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-227 |
3.22e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.81 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGN-----FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILF---------- 70
Cdd:PRK13651 2 QIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPD---TGTIEWifkdeknkkk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 71 -DGVDIYKENF-----------DVVELRKRVGMVFQ--SPNPFPKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALw 136
Cdd:PRK13651 77 tKEKEKVLEKLviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVGL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 137 DEvkDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARIS 215
Cdd:PRK13651 155 DE--SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWT 232
|
250
....*....|..
gi 123770551 216 DRTAFFLNGELI 227
Cdd:PRK13651 233 KRTIFFKDGKII 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-244 |
1.11e-33 |
|
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: 121.50 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTflrTLNRMNDLIPGVriEGSILFDGVDIYKENFDVvelR 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLVKPD--SGKILLDGQDITKLPMHK---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVF--QSPNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVEkslrgaaLWDE--VKDRLHKPATGLSGGQQQRLCIA 161
Cdd:cd03218 73 ARLGIGYlpQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEE-------LLEEfhITHLRKSKASSLSGGERRRVEIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
....
gi 123770551 241 DRRT 244
Cdd:cd03218 226 VRKV 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-212 |
1.57e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 120.66 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGVRIEGSILFDGVDIYKENfdvVELRk 87
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLTALP---AEQR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQSPNPFPK-SVYENVAYA-PKIHGLKDKRkldEIVEKSLRGAALwDEVKDRLhkPATgLSGGQQQRLCIARALA 165
Cdd:COG4136 77 RIGILFQDDLLFPHlSVGENLAFAlPPTIGRAQRR---ARVEQALEEAGL-AGFADRD--PAT-LSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELI-QELKKKYTIVI-VTHNMQQAA 212
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALlVTHDEEDAP 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-227 |
1.77e-33 |
|
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: 120.29 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNfQALkNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVRI--EGSILFDGVDIykENFDVVE 84
Cdd:cd03298 1 VRLDKIRFSYGE-QPM-HFDLTFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLINGVDV--TAAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 lrKRVGMVFQSPNPFPK-SVYENVAYapkihGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARA 163
Cdd:cd03298 70 --RPVSMLFQENNLFAHlTVEQNVGL-----GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-242 |
1.86e-33 |
|
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: 121.03 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVR--IEGSILFDGVDIYKENFDVVelrkrvgMVFQSPNPF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL-------NLISGLAqpTSGGVILEGKQITEPGPDRM-------VVFQNYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 P-KSVYENVAYAPKiHGLKDKRKLD--EIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:TIGR01184 67 PwLTVRENIALAVD-RVLPDLSKSErrAIVEEHIALVGL----TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 177 TSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRT-EVIFTKPRDR 242
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIlEVPFPRPRDR 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-239 |
2.67e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGVRIEGSILFDGVDIYKENf 80
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dVVELRKRVGMVFQSP-NPF-PKSVYENVAYapkihGLKDKR----KLDEIVEKSLRGAALWDEVKDrlhKPATgLSGGQ 154
Cdd:PRK13640 79 -VWDIREKVGIVFQNPdNQFvGATVGDDVAF-----GLENRAvprpEMIKIVRDVLADVGMLDYIDS---EPAN-LSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAArISDRTAFFLNGELIEMDRT 232
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
....*..
gi 123770551 233 EVIFTKP 239
Cdd:PRK13640 228 VEIFSKV 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-250 |
2.82e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.38 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRieGSILFDGVDIYK-ENFDVVELR-KRVGMVFQSPNP 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPTR--GQVLIDGVDIAKiSDAELREVRrKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 FPK-SVYENVAYAPKIHGLKDKRKLDEIVEkSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPT 177
Cdd:PRK10070 118 MPHmTVLDNTAFGMELAGINAEERREKALD-ALRQVGL----ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 178 SALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRTEDYITG 250
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-214 |
3.19e-33 |
|
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: 118.47 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQA--LKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDIYKenFDV 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLAR-------LILGLLrpTSGRVRLDGADISQ--WDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPKSVYENVayapkihglkdkrkldeivekslrgaalwdevkdrlhkpatgLSGGQQQRLCIAR 162
Cdd:cd03246 72 NELGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNM---QQAARI 214
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-228 |
4.41e-33 |
|
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: 121.07 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDIYKENFDVVE-LRKRVGMVFQ-S 95
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLAR-------LLLGLEkpAQGTVSFRGQDLYQLDRKQRRaFRRDVQLVFQdS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPF-PKSVYENVAYAPKIH--GLKDKRKLDEIVEKsLRGAALWDEVKDRLhkPATgLSGGQQQRLCIARALAIEPEVLL 172
Cdd:TIGR02769 98 PSAVnPRMTVRQIIGEPLRHltSLDESEQKARIAEL-LDMVGLRSEDADKL--PRQ-LSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 173 MDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-206 |
5.09e-33 |
|
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: 119.12 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIYKenfDVVELR 86
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPPS---AGEVLWNGEPIRD---AREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLK-DKRKLDEIVEK-SLRGaalwdevkdRLHKPATGLSGGQQQRLCIARA 163
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFWAALYGLRaDREAIDEALEAvGLAG---------LADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQE-LKKKYTIVIVTH 206
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-241 |
5.81e-33 |
|
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: 126.13 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQ--ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvrIEGSILFDGVDIykENFDVV 83
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL--LGLYQP---TEGSVLLDGVDI--RQIDPA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVAY-APKIHglkdkrklDEIVEKSLRGAALWDEVkdRLHkPA----------TGLSG 152
Cdd:TIGR03375 536 DLRRNIGYVPQDPRLFYGTLRDNIALgAPYAD--------DEEILRAAELAGVTEFV--RRH-PDgldmqigergRSLSG 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMR-IEELIQELKKKyTIVIVTHNMqQAARISDRtafflngeLIEMDR 231
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMDNRSEERfKDRLKRWLAGK-TLVLVTHRT-SLLDLVDR--------IIVMDN 674
|
250
....*....|
gi 123770551 232 TEVIFTKPRD 241
Cdd:TIGR03375 675 GRIVADGPKD 684
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-216 |
7.78e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.14 E-value: 7.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDIYK---ENFDVVelrkrvg 90
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDVTHrsiQQRDIC------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 91 MVFQSPNPFPK-SVYENVAYAPKIHGL-KDKRKldEIVEKSLRGAALwDEVKDRLhkpATGLSGGQQQRLCIARALAIEP 168
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGLKMLGVpKEERK--QRVKEALELVDL-AGFEDRY---VDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123770551 169 EVLLMDEPTSALDP--ISTMRieELIQELKKKYTI--VIVTHNMQQAARISD 216
Cdd:PRK11432 156 KVLLFDEPLSNLDAnlRRSMR--EKIRELQQQFNItsLYVTHDQSEAFAVSD 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-217 |
1.79e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 121.68 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGvriegsilfdgvDIY--KENFDVVE 84
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------------DLFigEKRMNDVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR-VGMVFQSPNPFPK-SVYENVAYAPKIHGlKDKRKLDEIVEKS---LRGAALWDEvkdrlhKPaTGLSGGQQQRLC 159
Cdd:PRK11000 72 PAERgVGMVFQSYALYPHlSVAENMSFGLKLAG-AKKEEINQRVNQVaevLQLAHLLDR------KP-KALSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPI--STMRIEelIQELKKKY--TIVIVTHNMQQAARISDR 217
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAAlrVQMRIE--ISRLHKRLgrTMIYVTHDQVEAMTLADK 203
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-240 |
2.72e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.68 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmnDLIPGvriEGSILFDGVDIykENFDVVELR 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQ-SPNPFPKSVYENVAYApKIHGLKDKRKLDEIVEKSLRGAALWDeVKDRLHkpaTGLSGGQQQRLCIARALA 165
Cdd:COG4559 75 RRRAVLPQhSSLAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSY---QTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 -------IEPEVLLMDEPTSALDP---ISTMRIeeLIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVI 235
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLahqHAVLRL--ARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
....*
gi 123770551 236 FTKPR 240
Cdd:COG4559 228 LTDEL 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-214 |
3.06e-32 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 117.57 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGN---FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDI--YKENF 80
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPIsqYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvveLRKRVGMVFQSPNPFPKSVYENVAYapkihGLKDKrKLDEIVEKSlRGAALWDEVKDRLHKPATG-------LSGG 153
Cdd:cd03248 86 ----LHSKVSLVGQEPVLFARSLQDNIAY-----GLQSC-SFECVKEAA-QKAHAHSFISELASGYDTEvgekgsqLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNM---QQAARI 214
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLstvERADQI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-229 |
4.22e-32 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 123.68 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGN---FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlipgVRIEGSILFDGVDIykENFDV 82
Cdd:TIGR00958 478 LIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-----QPTGGQVLLDGVPL--VQYDH 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQSPNPFPKSVYENVAYapkihGLKDKRKlDEIvekslRGAALWDEVKDRLHKPATG-----------LS 151
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENIAY-----GLTDTPD-EEI-----MAAAKAANAHDFIMEFPNGydtevgekgsqLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 152 GGQQQRLCIARALAIEPEVLLMDEPTSALDpistMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIEM 229
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAsrTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-230 |
7.09e-32 |
|
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: 116.44 E-value: 7.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNL-YYGNFQ-ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKenFDVV 83
Cdd:cd03244 2 DIEFKNVSLrYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDISK--IGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVAyapkIHGLKDkrklDEIVEKSLRGAALWDEVKDRLHKPAT-------GLSGGQQQ 156
Cdd:cd03244 75 DLRSRISIIPQDPVLFSGTIRSNLD----PFGEYS----DEELWQALERVGLKEFVESLPGGLDTvveeggeNLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHnmqqaaRI-----SDRTAFFLNGELIEMD 230
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVVEFD 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-181 |
1.19e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 122.37 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYG--NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndL---IPGvriEGSILFDGVDIykENF 80
Cdd:TIGR03797 451 AIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LgfeTPE---SGSVFYDGQDL--AGL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSPNPFPKSVYENVAYAPKIhglkdkrKLDEIVEkSLRGAALWDEVKDR---LH----KPATGLSGG 153
Cdd:TIGR03797 521 DVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPL-------TLDEAWE-AARMAGLAEDIRAMpmgMHtvisEGGGTLSGG 592
|
170 180
....*....|....*....|....*...
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALD 181
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-250 |
1.48e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.17 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPG-VRIE-GSILFDGVDIYK-ENFDVV 83
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLR-------LIGGqIAPDhGEILFDGENIPAmSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPK-SVYENVAYApkihgLKDKRKLDEIVEKS----------LRGAAlwdevkdRLhKPATgLSG 152
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDmNVFDNVAYP-----LREHTQLPAPLLHStvmmkleavgLRGAA-------KL-MPSE-LSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRtAFFLNGELIEMD 230
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIADH-AYIVADKKIVAH 225
|
250 260
....*....|....*....|
gi 123770551 231 RTEVIFTKPRDRRTEDYITG 250
Cdd:PRK11831 226 GSAQALQANPDPRVRQFLDG 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-228 |
1.60e-31 |
|
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: 114.33 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYG--NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmnDLIPGvriEGSILFDGVDI--YKENfdv 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVsdLEKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 veLRKRVGMVFQSPNPFPKSVYENVAyapkihglkdkrkldeivekslrgaalwdevkdrlhkpaTGLSGGQQQRLCIAR 162
Cdd:cd03247 73 --LSSLISVLNQRPYLFDTTLRNNLG---------------------------------------RRFSGGERQRLALAR 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFLNGELIE 228
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-243 |
1.69e-31 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 116.22 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTflrTLNRMNDLIPgvRIEGSILFDGVDIYKENFDvveLR 86
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHLPMH---ER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVF--QSPNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVEkslrgaALWDE--VKDRLHKPATGLSGGQQQRLCIA 161
Cdd:TIGR04406 74 ARLGIGYlpQEASIFRKlTVEENIMAVLEIRKDLDRAEREERLE------ALLEEfqISHLRDNKAMSLSGGERRRVEIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVT-HNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
...
gi 123770551 241 DRR 243
Cdd:TIGR04406 228 VRR 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-227 |
2.07e-31 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 116.62 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIykENFDV 82
Cdd:PRK10253 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHI--QHYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQ-SPNPFPKSVYENVAYAPKIHG--LKDKRKLDE-IVEKSLRGAAlwdeVKDRLHKPATGLSGGQQQRL 158
Cdd:PRK10253 77 KEVARRIGLLAQnATTPGDITVQELVARGRYPHQplFTRWRKEDEeAVTKAMQATG----ITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-238 |
2.36e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.14 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKEnfdVVELRKRVGMVFQSPNP- 98
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE---IKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 -FPKSVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALwdeVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPT 177
Cdd:PRK13643 97 lFEETVLKDVAFGPQNFGIP-KEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 178 SALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-228 |
4.27e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 120.51 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVVE 84
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDL--RDYTLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPKSVYENVAYAPKihglkDKRKLDEIvEKSLRGAALWDEVKDRLH-------KPATGLSGGQQQR 157
Cdd:PRK11176 415 LRNQVALVSQNVHLFNDTIANNIAYART-----EQYSREQI-EEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHnmqqaaRIS-----DRTAFFLNGELIE 228
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStiekaDEILVVEDGEIVE 558
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-239 |
4.49e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.18 E-value: 4.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPgvRIEGSILFDGVDIykENFDVVELR 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---LLP--PDSGEVLVDGLDV--ATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYA--PKIHG---LKDKRKLDEIVE----KSLRGAALwDEvkdrlhkpatgLSGGQQQ 156
Cdd:COG4604 75 KRLAILRQENHINSRlTVRELVAFGrfPYSKGrltAEDREIIDEAIAyldlEDLADRYL-DE-----------LSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDP---ISTMRI-EELIQELKKkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRT 232
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMkhsVQMMKLlRRLADELGK--TVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
....*..
gi 123770551 233 EVIFTKP 239
Cdd:COG4604 221 EEIITPE 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-227 |
1.20e-30 |
|
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: 113.14 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDG--VDIYKENfdvve 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGkpLDIAARN----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 lrkRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKD---KRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCI 160
Cdd:cd03269 71 ---RIGYLPEERGLYPKmKVIDQLVYLAQLKGLKKeeaRRRIDEWLERL--------ELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
1.29e-30 |
|
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: 118.62 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYY-GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRieGSILFDGVDIykENF 80
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG---LLDPLQ--GEVTLDGVPV--SSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVGMVFQSPNPFPKSVYENVAYApkihglkDKRKLDEIVEKSLRGAALWDEVKDR-------LHKPATGLSGG 153
Cdd:TIGR02868 403 DQDEVRRRVSVCAQDAHLFDTTVRENLRLA-------RPDATDEELWAALERVGLADWLRALpdgldtvLGEGGARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHN 207
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-206 |
2.65e-30 |
|
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: 111.49 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 5 VKIKVRDLNLY------YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmNDLIPGVRIEGSILFDGVDIYKE 78
Cdd:cd03213 2 VTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL---AGRRTGLGVSGEVLINGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 NFdvvelRKRVGMVFQSPNPFPK-SVYENVAYAPKihglkdkrkldeiveksLRgaalwdevkdrlhkpatGLSGGQQQR 157
Cdd:cd03213 79 SF-----RKIIGYVPQDDILHPTlTVRETLMFAAK-----------------LR-----------------GLSGGERKR 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTH 206
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-229 |
2.72e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.14 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVK--IKVRDLNLYYGNF-QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYKE 78
Cdd:PRK13657 328 LGRVKgaVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--PQ---SGRILIDGTDIRTV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 NfdVVELRKRVGMVFQSPNPFPKSVYENVAYapkihGLKDKRklDEIVEKSLRGAALWDEVKDRLHKPAT-------GLS 151
Cdd:PRK13657 403 T--RASLRRNIAVVFQDAGLFNRSIEDNIRV-----GRPDAT--DEEMRAAAERAQAHDFIERKPDGYDTvvgergrQLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 152 GGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGELIEM 229
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVES 550
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
3.38e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 3.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKENFDvvELRKRVGMVFQSP-N 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAK-------LMIGIEKvkSGEIFYNNQAITDDNFE--KLRKHIGIVFQNPdN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PFPKS-VYENVAYAPKIHGLKDKrKLDEIVEKSLRGAALWDEVKDRLHkpatGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK13648 95 QFVGSiVKYDVAFGLENHAVPYD-EMHRRVSEALKQVDMLERADYEPN----ALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 177 TSALDPISTMRIEELIQELK--KKYTIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-230 |
4.46e-30 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 112.28 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTL---NRMNdlipgvriEGSILFDGVDIYKE 78
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPRAT--------SGRIVFDGKDITDW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 NFDVVeLRKRVGMVFQSPNPFPK-SVYENVAYApkihGLKDKRKldEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQR 157
Cdd:PRK11614 73 QTAKI-MREAVAIVPEGRRVFSRmTVEENLAMG----GFFAERD--QFQERIKWVYELFPRLHERRIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMD 230
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
20-217 |
4.52e-30 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 111.73 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDI----YKENfdvVELRKR-VGMVFQ 94
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLD-----SGSLTLAGKEVtnlsYSQK---IILRRElIGYIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFPK-SVYENVAYAPKIHGLKDKrkldEIVEKSLRGAALWDEVKDRLHKPATgLSGGQQQRLCIARALAIEPEVLLM 173
Cdd:NF038007 91 SFNLIPHlSIFDNVALPLKYRGVAKK----ERIERVNQVLNLFGIDNRRNHKPMQ-LSGGQQQRVAIARAMVSNPALLLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 123770551 174 DEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNmQQAARISDR 217
Cdd:NF038007 166 DEPTGNLDSKNARAVLQQLKYINQKgTTIIMVTHS-DEASTYGNR 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-206 |
4.67e-30 |
|
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: 112.49 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmnDLIPGVRIEGSILfdGVDIYKEnfDVVELR 86
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTYGNDVRLF--GERRGGE--DVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVfqSP---NPFPK--SVYENV---AYApkIHGL------KDKRKLDEIVEkslrgaaLWDeVKDRLHKPATGLSG 152
Cdd:COG1119 78 KRIGLV--SPalqLRFPRdeTVLDVVlsgFFD--SIGLyreptdEQRERARELLE-------LLG-LAHLADRPFGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTH 206
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-236 |
1.08e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKENfdvVELR-KRVGMVFQSP- 96
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLN-------AIAGSLPpdSGSILIDGKDVTKLP---EYKRaKYIGRVFQDPm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 -NPFPK-SVYENVAYA---PKIHGLK---DKRKLDEIVEKsLRGAALWDEvkDRLHKPATGLSGGQQQRLCIARALAIEP 168
Cdd:COG1101 91 mGTAPSmTIEENLALAyrrGKRRGLRrglTKKRRELFREL-LATLGLGLE--NRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 169 EVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRtafflngeLIEMDRTEVIF 236
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNR--------LIMMHEGRIIL 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-228 |
1.68e-29 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 113.40 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV-RI-EGSILFDGvdiykENFDVVELRKR-VGM 91
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-------MVAGLeRItSGEIWIGG-----RVVNELEPADRdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 92 VFQSPNPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhKPATgLSGGQQQRLCIARALAIEPEV 170
Cdd:PRK11650 81 VFQNYALYPHmSVRENMAYGLKIRGM-PKAEIEERVAEAARILEL-EPLLDR--KPRE-LSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 171 LLMDEPTSALDPI--STMRIEelIQELKK--KYTIVIVTHNMQQAARISDRTAfFLNGELIE 228
Cdd:PRK11650 156 FLFDEPLSNLDAKlrVQMRLE--IQRLHRrlKTTSLYVTHDQVEAMTLADRVV-VMNGGVAE 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
2.36e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 112.25 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLN----------RMNDLIPGVRIEGSILFDGVDIYK-ENFDvvELRK 87
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNglikskygtiQVGDIYIGDKKNNHELITNPYSKKiKNFK--ELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 88 RVGMVFQSP--NPFPKSVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWDEVKDRlhkPATGLSGGQQQRLCIARALA 165
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGLDDSYLER---SPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-214 |
3.36e-29 |
|
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: 115.20 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYG--NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIykENFDVV 83
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDL--ADYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVAYApkihglkDKRKLD-EIVEKSLRGAALWDEVK---DRLHKP----ATGLSGGQQ 155
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFNDTIANNIAYG-------RTEQADrAEIERALAAAYAQDFVDklpLGLDTPigenGVLLSGGQR 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123770551 156 QRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNM---QQAARI 214
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKADRI 537
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-218 |
4.37e-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: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDI--YKENFDVVELRKRVGMVF 93
Cdd:TIGR03608 8 FGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFD-----SGQVYLNGQETppLNSKKASKFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 94 QSPNPFP-KSVYENVAYAPKIHGL--KDKRKLDEIVEKSLRgaalwdeVKDRLHKPATGLSGGQQQRLCIARALAIEPEV 170
Cdd:TIGR03608 83 QNFALIEnETVEENLDLGLKYKKLskKEKREKKKEALEKVG-------LNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMqQAARISDRT 218
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDP-EVAKQADRV 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-233 |
4.99e-29 |
|
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: 109.50 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIykENFDVVELRKRVGMVFQSPNPFP 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPE---NGRVLVDGHDL--ALADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENVAYApkihglKDKRKLDEIVE-KSLRGA-----ALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMD 174
Cdd:cd03252 90 RSIRDNIALA------DPGMSMERVIEaAKLAGAhdfisELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 175 EPTSALDPISTMRIEELIQELKKKYTIVIVTHNMqQAARISDRTAFFLNGELIEMDRTE 233
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHD 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-227 |
5.03e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.35 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKST-FlrtlnRMndlIPG-VRI-EGSILFDGVDI-----YK 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtF-----YM---IVGlVKPdSGRIFLDGEDIthlpmHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 enfdvvelRKRVGMVF--QSPNPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEkslrgaALWDE--VKDRLHKPATGLSG 152
Cdd:COG1137 75 --------RARLGIGYlpQEASIFRKlTVEDNILAVLELRKL-SKKEREERLE------ELLEEfgITHLRKSKAYSLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-238 |
6.62e-29 |
|
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: 109.03 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKENFdvvelr 86
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRP---TSGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKDKRkLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:TIGR03740 70 HKIGSLIESPPLYENlTARENLKVHTTLLGLPDSR-IDEVLNIV--------DLTNTGKKKAKQFSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRT------EVIFTK 238
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGYQGKInksenlEKLFVE 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-226 |
1.02e-28 |
|
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: 108.02 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 26 SLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVR--IEGSILFDGVDIYKenfdVVELRKRVGMVFQSPNPFPK-S 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLL-------NLIAGFIepASGSIKVNDQSHTG----LAPYQRPVSMLFQENNLFAHlT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 103 VYENVAYapkihGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDP 182
Cdd:TIGR01277 87 VRQNIGL-----GLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123770551 183 ISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:TIGR01277 162 LLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-226 |
1.17e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 111.36 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQAlkNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPG-VRIEGSILFDGvdiyKENFDVVELRKRVGMVFQ 94
Cdd:TIGR02142 9 LGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGeIVLNGRTLFDS----RKGIFLPPEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFPK-SVYENVAYapkihGLKDKRKLDEIVEkslrgaalWDEVKDRL------HKPATGLSGGQQQRLCIARALAIE 167
Cdd:TIGR02142 83 EARLFPHlSVRGNLRY-----GMKRARPSERRIS--------FERVIELLgighllGRLPGRLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 168 PEVLLMDEPTSALDPISTMRI----EELIQELkkKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-218 |
1.20e-28 |
|
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: 108.29 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmNDLiPGvriEGSILFD----GVDIYK-ENFDVVELRKR-VGMVF 93
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYL-PD---SGSILVRhdggWVDLAQaSPREILALRRRtIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 94 QspnpFPKSVyenvayaPKIHGLkdkrkldEIVEKSL------RGAALwDEVKDRLHK-----------PATgLSGGQQQ 156
Cdd:COG4778 100 Q----FLRVI-------PRVSAL-------DVVAEPLlergvdREEAR-ARARELLARlnlperlwdlpPAT-FSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYT-IVIVTHNMQQAARISDRT 218
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVADRV 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-235 |
1.26e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 108.63 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIP--G-VRIEGSI--LFDgvdiykenfdvvelrkrV 89
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LEPtsGrVEVNGRVsaLLE-----------------L 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 90 GMVFQspnpfPK-SVYENVAYAPKIHGLKDK---RKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:COG1134 96 GAGFH-----PElTGRENIYLNGRLLGLSRKeidEKFDEIVEFA--------ELGDFIDQPVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 166 IEPEVLLMDEPTSALDPI----STMRIEELIQELKkkyTIVIVTHNMQQAARISDRTAFFLNGELIEMDRT-EVI 235
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR---TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPeEVI 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-228 |
1.32e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGVrieGSILFDGVDIYKENFD--VVELRKRVGMVFQSP 96
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKPTT---GTVTVDDITITHKTKDkyIRPVRKRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NP--FPKSVYENVAYAPKIHGLKdkrkLDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMD 174
Cdd:PRK13646 95 ESqlFEDTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 175 EPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-231 |
1.43e-28 |
|
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: 107.50 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNF--QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKenFDVV 83
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDIST--IPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVayapkihglkdkRKLDEIVEKSLRGAAlwdevkdRLHKPATGLSGGQQQRLCIARA 163
Cdd:cd03369 79 DLRSSLTIIPQDPTLFSGTIRSNL------------DPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFLNGELIEMDR 231
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-237 |
1.98e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 109.33 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFD-GVDIYKEnfdVVELRKRVGMVFQSP- 96
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPaNLKKIKE---VKRLRKEIGLVFQFPe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 -NPFPKSVYENVAYAPkIHGLKDKRKLDEIVEKSLRGAALwdeVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:PRK13645 101 yQLFQETIEKDIAFGP-VNLGENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 176 PTSALDPISTMRIEELIQELKKKYT--IVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-243 |
3.32e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.84 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDgvdiykenfdvvELRKR 88
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA------------EARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 89 VGMVFQSPNPFP-KSVYENVAYapkihGLKDKRKldEIVEKSLRGAALWDEVKDRlhkPATgLSGGQQQRLCIARALAIE 167
Cdd:PRK11247 83 TRLMFQDARLLPwKKVIDNVGL-----GLKGQWR--DAALQALAAVGLADRANEW---PAA-LSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGElIEMDRTEVIftkPRDRR 243
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGK-IGLDLTVDL---PRPRR 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-227 |
3.83e-28 |
|
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: 106.97 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYYgnfQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGVRIEGSILFDGVDIYKENF 80
Cdd:cd03234 5 PWWDVGLKAKNWNKYA---RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQPRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvvelRKRVGMVFQSPNPFPK-SVYENVAYAPKI--HGLKDKRKLDEIVE-KSLRGAALwdevKDRLHKPATGLSGGQQQ 156
Cdd:cd03234 80 -----QKCVAYVRQDDILLPGlTVRETLTYTAILrlPRKSSDAIRKKRVEdVLLRDLAL----TRIGGNLVKGISGGERR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVT-HnmQQAA---RISDRTAFFLNGELI 227
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiH--QPRSdlfRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-241 |
1.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.72 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKENfdVVELRKRVGMVFQSP-NPF- 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAEN--VWNLRRKIGMVFQNPdNQFv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 PKSVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWDeVKDRlhKPATgLSGGQQQRLCIARALAIEPEVLLMDEPTSA 179
Cdd:PRK13642 96 GATVEDDVAFGMENQGIP-REEMIKRVDEALLAVNMLD-FKTR--EPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 180 LDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTEVIFTKPRD 241
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-250 |
1.83e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGVrieGSILFDGVDIykENFDVVELR 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTPTA---GTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPN-PFPKSVYENVAYAPKIH-------GLKDKRKLDEIVEkslRGAAlwDEVKDRlhkPATGLSGGQQQRL 158
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGRTPHrsrfdtwTETDRAAVERAME---RTGV--AQFADR---PVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT 228
|
250 260
....*....|....*....|.
gi 123770551 238 KPRDRR--------TEDYITG 250
Cdd:PRK09536 229 ADTLRAafdartavGTDPATG 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-228 |
2.60e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.92 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndlipgVRIE----GSILFDGVDIYKEN-FDVVELRKRVGMVFQ 94
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLL---------VGLEspsqGNVSWRGEPLAKLNrAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SP----NPfPKSVYENVAyAPKIHGLK-DKRKLDEIVEKSLRGAALWDEVKDRLhkPATgLSGGQQQRLCIARALAIEPE 169
Cdd:PRK10419 97 DSisavNP-RKTVREIIR-EPLRHLLSlDKAERLARASEMLRAVDLDDSVLDKR--PPQ-LSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 170 VLLMDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-226 |
2.71e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQ---ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKENfd 81
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDGLLEaeSGQIIIDGDLLTEEN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSP-NPF-PKSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDeVKDRlhKPATgLSGGQQQRLC 159
Cdd:PRK13650 76 VWDIRHKIGMVFQNPdNQFvGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKER--EPAR-LSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAArISDRTAFFLNGEL 226
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-224 |
3.25e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.66 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 26 SLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVRI--EGSILFDGVDiykeNFDVVELRKRVGMVFQSPNPFPK-S 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL-------NLIAGFLTpaSGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 103 VYENVAYApkIH-GLK----DKRKLDEIVEK-SLrgaalwDEVKDRLhkPATgLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK10771 88 VAQNIGLG--LNpGLKlnaaQREKLHAIARQmGI------EDLLARL--PGQ-LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123770551 177 TSALDPisTMRIE--ELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFLNG 224
Cdd:PRK10771 157 FSALDP--ALRQEmlTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-228 |
3.60e-27 |
|
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: 109.83 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYG-NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIykENFDVVEL 85
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLL--VGFFQAR---SGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPKSVYENVayapkIHGLKDKRKLDEIVEkSLRGAALWDEVKD-------RLHKPATGLSGGQQQRL 158
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENL-----LLGAKENVSQDEIWA-ACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKyTIVIVTHNMQQAARiSDRTAFFLNGELIE 228
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-240 |
1.19e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.43 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYY----GNF------QALKNISLDIYKNEVTALIGPSGCGKSTflrtLNRMNDLI--PgvrIEGSILF 70
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIetP---TGGELYY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 71 DGVDIYKENFDVV-ELRKRVGMVFQSP----NPfPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRL-H 144
Cdd:PRK11308 75 QGQDLLKADPEAQkLLRQKIQIVFQNPygslNP-RKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYpH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 145 KpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpistMRIE--------ELIQELKKKYtiVIVTHNMQQAARISD 216
Cdd:PRK11308 154 M----FSGGQRQRIAIARALMLDPDVVVADEPVSALD----VSVQaqvlnlmmDLQQELGLSY--VFISHDLSVVEHIAD 223
|
250 260
....*....|....*....|....
gi 123770551 217 RTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK11308 224 EVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-244 |
1.23e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 103.63 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 23 KNISLDIYKNEVTALIGPSGCGKStfLRTLNRMNDLIPGVR-IEGSILFDGVDIYKEnfdvvELRKR-VGMVFQSP---- 96
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGRVLLDGKPVAPC-----ALRGRkIATIMQNPrsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NPfpksVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALwDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK10418 93 NP----LHTMHTHARETCLALGKPADDATLTAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 177 TSALDPISTMRIEELIQELKKKYT--IVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRT 244
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-239 |
2.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.53 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfDVVELRKRVGMVFQSPNP-- 98
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQ---KGKVLVSGIDTGDFS-KLQGIRKLVGIVFQNPETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 FPKSVYENVAYAPKIHGLK--DKRKLdeiVEKSLRGAALwdeVKDRLHKPATgLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLPpiEIRKR---VDRALAEIGL---EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 177 TSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQaARISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-240 |
2.53e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.25 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYK-ENFDVVELRKRVGMVFQSP--- 96
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 -NPfPKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRL-HKpatgLSGGQQQRLCIARALAIEPEVLLMD 174
Cdd:PRK10261 414 lDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHE----FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 175 EPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-217 |
3.05e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFlrtlnrMN--------DlipgvriEGSILFDG-- 72
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDGkp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 73 VDIYKENfdvVELRKRVGMVFQSPNPFPK-SVYENVAYA--PKIHGLKDKRKLDEIVEkslrgaalwdEVKDR------L 143
Cdd:COG3845 69 VRIRSPR---DAIALGIGMVHQHFMLVPNlTVAENIVLGlePTKGGRLDRKAARARIR----------ELSERygldvdP 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 144 HKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPistMRIEELIQELKK----KYTIVIVTHNMQQAARISDR 217
Cdd:COG3845 136 DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRRlaaeGKSIIFITHKLREVMAIADR 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-228 |
5.03e-26 |
|
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: 100.68 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDliPGVRI-EGSILFDGVDIYKENfdvVEL 85
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGH--PKYEVtEGEILFKGEDITDLP---PEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVG--MVFQSPnpfpksvyenvayaPKIHGLKDK---RKLDEivekslrgaalwdevkdrlhkpatGLSGGQQQRLCI 160
Cdd:cd03217 74 RARLGifLAFQYP--------------PEIPGVKNAdflRYVNE------------------------GFSGGEKKRNEI 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 161 ARALAIEPEVLLMDEPTSALDpISTMR-IEELIQELK-KKYTIVIVTHNMQQAARI-SDRTAFFLNGELIE 228
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLD-IDALRlVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-244 |
6.10e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 17 GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRIEGSILFDGVDIYKENF-DVVELRKRVGMVFQS 95
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNRrQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPF--PK-SVYENVAyapkiHGLKDKRKLDEIVEKSLRGAALWDEV---KDRLHKPATGLSGGQQQRLCIARALAIEPE 169
Cdd:PRK15134 371 PNSSlnPRlNVLQIIE-----EGLRVHQPTLSAAQREQQVIAVMEEVgldPETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 170 VLLMDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRRT 244
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-226 |
7.98e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.72 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDIYK-ENFDVVELRKRVGM 91
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-------LICGIErpSAGKIWFSGHDITRlKNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 92 VFQSPNPF-PKSVYENVAYAPKIHG--LKDKRKLdeiVEKSLRGAALWDEVKDRlhkpATGLSGGQQQRLCIARALAIEP 168
Cdd:PRK10908 84 IFQDHHLLmDRTVYDNVAIPLIIAGasGDDIRRR---VSAALDKVGLLDKAKNF----PIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 169 EVLLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-227 |
8.00e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.01 E-value: 8.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 11 DLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFDVVELRKRVG 90
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 91 MVFQSPNP--FPKSVYENVAYAPKIHGLKDkrklDEIVEKSLRGAALWDEVKDRlHKPATGLSGGQQQRLCIARALAIEP 168
Cdd:PRK13638 81 TVFQDPEQqiFYTDIDSDIAFSLRNLGVPE----AEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 169 EVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-245 |
8.25e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKEnfDVVELRK----RVGMVFQS 95
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHA--SEQTLRGvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 P----NPF---PKSVYENVAyapkIH-GLKDKRKLDEIVE----KSLRGAAlwdevkDRLHKPATGLSGGQQQRLCIARA 163
Cdd:PRK15134 101 PmvslNPLhtlEKQLYEVLS----LHrGMRREAARGEILNcldrVGIRQAA------KRLTDYPHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRD 241
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTH 250
|
....
gi 123770551 242 RRTE 245
Cdd:PRK15134 251 PYTQ 254
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-230 |
9.95e-26 |
|
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: 100.30 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 13 NLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPG-VRIEGSI--LFDgvdiykenfdvvelrkrV 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtVTVRGRVssLLG-----------------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 90 GMVFQsPNpfpKSVYENVAYAPKIHGLKDKR---KLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALAI 166
Cdd:cd03220 92 GGGFN-PE---LTGRENIYLNGRLLGLSRKEideKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVI-VTHNMQQAARISDRTAFFLNGELIEMD 230
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-240 |
1.21e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.48 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 18 NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVriEGSILFDGVDIYK-ENFDVVELRKRVGMVFQSP 96
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKAT--DGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 ----NPfPKSVYENVA-----YAPKIHGLKDKRKLDEIVEKslrgAALWDEVKDRL-HKpatgLSGGQQQRLCIARALAI 166
Cdd:PRK15079 108 laslNP-RMTIGEIIAeplrtYHPKLSRQEVKDRVKAMMLK----VGLLPNLINRYpHE----FSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 167 EPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-228 |
1.98e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.52 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLipgvrIEGSILFDGVDI--YKENfdv 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP-----QQGEILLNGQPIadYSEA--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 vELRKRVGMVFQSPNPFPKSVYENVAYA-PKIHglkDKrKLDEIVEK--------SLRGAALWdevkdrlhkpaTG---- 149
Cdd:PRK11160 411 -ALRQAISVVSQRVHLFSATLRDNLLLAaPNAS---DE-ALIEVLQQvgleklleDDKGLNAW-----------LGeggr 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 150 -LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFLNGELIE 228
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
6-235 |
2.13e-25 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 104.64 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNFQA--LKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSILFDGVDiyKENFD 81
Cdd:TIGR03796 477 YVELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAK-------LVAGLYqpWSGEILFDGIP--REEIP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPKSVYENVAyapkihgLKDKRKLDEIVEKSLRGAALWDEVKDR-------LHKPATGLSGGQ 154
Cdd:TIGR03796 548 REVLANSVAMVDQDIFLFEGTVRDNLT-------LWDPTIPDADLVRACKDAAIHDVITSRpggydaeLAEGGANLSGGQ 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQelKKKYTIVIVTHNMqQAARISDrtafflngELIEMDRTEV 234
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRL-STIRDCD--------EIIVLERGKV 689
|
.
gi 123770551 235 I 235
Cdd:TIGR03796 690 V 690
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-223 |
2.54e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 104.34 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYY---GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRI------------------ 64
Cdd:PTZ00265 1165 KIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 65 -------------------------------EGSILFDGVDIYkeNFDVVELRKRVGMVFQSPNPFPKSVYENVAYAPKI 113
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 114 HGLKDKRK------LDEIVEkslrgaALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMR 187
Cdd:PTZ00265 1323 ATREDVKRackfaaIDEFIE------SLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*...
gi 123770551 188 IEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLN 223
Cdd:PTZ00265 1397 IEKTIVDIKDKAdkTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-210 |
2.77e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLY-YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndL--IPgvrIEGSILFDGVDIykEN 79
Cdd:PRK11174 346 DPVTIEAEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL-----LgfLP---YQGSLKINGIEL--RE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 FDVVELRKRVGMVFQSPNPFPKSVYENVAYA------PKIHGLKDKRKLDEIVEKSLRGaaLWDEVKDRlhkpATGLSGG 153
Cdd:PRK11174 416 LDPESWRKHLSWVGQNPQLPHGTLRDNVLLGnpdasdEQLQQALENAWVSEFLPLLPQG--LDTPIGDQ----AAGLSVG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQ 210
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-235 |
3.52e-25 |
|
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: 103.67 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV--RIEGSILFDGVDIYkeNFDVVELRKRVGMVFQSPNPF 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLAR-------LLVGVwpPTAGSVRLDGADLS--QWDREELGRHIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 PKSVYENVAYAPKIHglkdkrklDEIVEKSLRGAALWDEVkdrLHKP----------ATGLSGGQQQRLCIARALAIEPE 169
Cdd:COG4618 419 DGTIAENIARFGDAD--------PEKVVAAAKLAGVHEMI---LRLPdgydtrigegGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 170 VLLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTHNMqQAARISDRTAFFLNGELIEM-DRTEVI 235
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFgPRDEVL 554
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-207 |
4.06e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENFDvvELRKRVGMVFQSPNPFPK 101
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL--ISPT---SGTLLFEGEDISTLKPE--IYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENVAYAPKIHGLKDKRKldeIVEKSLRGAALWDEVkdrLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALD 181
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA---IFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180
....*....|....*....|....*...
gi 123770551 182 PISTMRIEELIQELKKKYTIVI--VTHN 207
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-218 |
4.08e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVR--IEGSIlfdgvdiykenfdVVELRKRVGMVF 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLK-------VLAGVLrpTSGTV-------------RRAGGARVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 94 QS---PNPFPKSVYENVAYA--PKIHGLKDKRKLDE-IVEKSLRGAALWDEVKDRLHKpatgLSGGQQQRLCIARALAIE 167
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGrwARRGLWRRLTRDDRaAVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRT 218
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-235 |
1.02e-24 |
|
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: 102.19 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPgvrIEGSILFD--------------- 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 72 --------GVDIYKENFDVVEL--------RKRVGMVFQSPNPF--PKSVYENVAYAPKIHGLKDKRKLDeivekslRGA 133
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDFWNLsdklrrriRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVG-------RAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 134 ALWDEVK--DRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQ 209
Cdd:TIGR03269 151 DLIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260
....*....|....*....|....*..
gi 123770551 210 QAARISDRTAFFLNGELIEM-DRTEVI 235
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEgTPDEVV 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-239 |
1.65e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.41 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGVRIEGSILFDGVDIYke 78
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREIL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 NFDVVELRK----RVGMVFQSP----NPFPKsVYENVAYAPKIHGLKDKRkldEIVEKSLR--GAALWDEVKDRLHKPAT 148
Cdd:PRK09473 85 NLPEKELNKlraeQISMIFQDPmtslNPYMR-VGEQLMEVLMLHKGMSKA---EAFEESVRmlDAVKMPEARKRMKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 149 GLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250
....*....|...
gi 123770551 227 IEMDRTEVIFTKP 239
Cdd:PRK09473 241 MEYGNARDVFYQP 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-240 |
1.72e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKST-------FLRTLNrmndlipgvrieGSILFDGVDIYKEN 79
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTvfncltgFYKPTG------------GTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 FDVVelrKRVGMV--FQSPNPFPK-SVYENVAYAPK-------IHGLKDKRKLDEIVEKSLRGAALWDEV---KDRLHKP 146
Cdd:PRK11300 74 GHQI---ARMGVVrtFQHVRLFREmTVIENLLVAQHqqlktglFSGLLKTPAFRRAESEALDRAATWLERvglLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 147 ATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNG 224
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQG 230
|
250
....*....|....*.
gi 123770551 225 ELIEMDRTEVIFTKPR 240
Cdd:PRK11300 231 TPLANGTPEEIRNNPD 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-227 |
1.96e-24 |
|
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: 97.40 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfdvVELRKRVGMVFQSPNP-- 98
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPT---SGEVRVAGLVPWKRR---KKFLRRIGVVFGQKTQlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 FPKSVYENVAYAPKIHGLKD---KRKLDEIVEkslrgaALwdEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPParfKKRLDELSE------LL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123770551 176 PTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-214 |
2.72e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 96.00 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYG-----NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLipgVRIEGSilfdgvdiykenfd 81
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEL---EKLSGS-------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 vVELRKRVGMVFQSPNPFPKSVYENVayapkIHGLK-DKRKLDEIVEKS--LRGAALWD-----EVKDRlhkpATGLSGG 153
Cdd:cd03250 62 -VSVPGSIAYVSQEPWIQNGTIRENI-----LFGKPfDEERYEKVIKACalEPDLEILPdgdltEIGEK----GINLSGG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDP-ISTMRIEELIQ-ELKKKYTIVIVTHNMQ---QAARI 214
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQllpHADQI 197
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-240 |
4.17e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmnDLIPGvriEGSILFDGVDiyKENFDVVEL-- 85
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRD--GQLRDLYALse 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 -------RKRVGMVFQSPnpfpksvyenvayapkihglKDKRKLD-----EIVEK----------SLRGAAL-W-DEVK- 140
Cdd:PRK11701 81 aerrrllRTEWGFVHQHP--------------------RDGLRMQvsaggNIGERlmavgarhygDIRATAGdWlERVEi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 141 --DRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISD 216
Cdd:PRK11701 141 daARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAH 220
|
250 260
....*....|....*....|....
gi 123770551 217 RTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDDPQ 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
4.47e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYKEnfd 81
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PD---AGKITVLGVPVPAR--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALWDEVKDRLhkpaTGLSGGQQQRLCI 160
Cdd:PRK13536 109 ARLARARIGVVPQFDNLDLEfTVRENLLVFGRYFGMS-TREIEAVIPSLLEFARLESKADARV----SDLSGGMKRRLTL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRI-EELIQELKKKYTIVIVTHNMQQAARISDR 217
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-227 |
7.29e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 96.31 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVRI--EGSILFDGVDIYKENFDVvelrkrvGMVF 93
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLL-------NLIAGFVPyqHGSITLDGKPVEGPGAER-------GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 94 QSPNPFP-KSVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALWDEVKDRLHKpatgLSGGQQQRLCIARALAIEPEVLL 172
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 173 MDEPTSALDPISTMRIEELI----QELKKKytIVIVTHNMQQAArisdrtafFLNGELI 227
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLlklwQETGKQ--VLLITHDIEEAV--------FMATELV 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-227 |
1.18e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGV-RIEGSilfdgvdiykenfDVVEL---------RKRVGM 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyRVAGQ-------------DVATLdadalaqlrREHFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 92 VFQSPNPFPK-SVYENVAyAPKIH-GLKDKRKLDEIVEKSLRGAalwdeVKDRLHKPATGLSGGQQQRLCIARALAIEPE 169
Cdd:PRK10535 91 IFQRYHLLSHlTAAQNVE-VPAVYaGLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 170 VLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARiSDRTAFFLNGELI 227
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-228 |
1.89e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKENFDV-VELR-KRVGMVFQSPNPF 99
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 PK-SVYENVAYAPKIHGLKDKRKLDeivekslRGAALWDEV--KDRL-HKPATgLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:PRK10584 101 PTlNALENVELPALLRGESSRQSRN-------GAKALLEQLglGKRLdHLPAQ-LSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 176 PTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFLNGELIE 228
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-226 |
3.27e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRM--NDLIPGVRIEgsilFDGVDIYKENF---D 81
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIE----LLGRTVQREGRlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPK-SVYENVA----------------YAPkihgLKDKRKLDEIVEKSLRGAAlwdevkdrlH 144
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRlSVLENVLigalgstpfwrtcfswFTR----EQKQRALQALTRVGMVHFA---------H 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 145 KPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFL 222
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALR 227
|
....
gi 123770551 223 NGEL 226
Cdd:PRK09984 228 QGHV 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-215 |
3.62e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPgvrIEGSILFDGVDIYK-ENFDVVELRKR-VGMVFQSPNPF 99
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT--P---TSGDVIFNGQPMSKlSSAAKAELRNQkLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 PK-SVYENVAyAPKIHGlkdKRKLDEIVEKSLRGAALWDEVKDRLHKPATgLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:PRK11629 100 PDfTALENVA-MPLLIG---KKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 123770551 179 ALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARIS 215
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-235 |
3.64e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvrIEGSILFDGvdiykenfdvvelRKR 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEP---DSGEVSIPK-------------GLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 89 VGMVFQSPNPFP-KSVYENV--AYAPKIHGLKDKR----KLDEIVEKSLRGAALWDEVKDR------------------- 142
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVldGDAELRALEAELEeleaKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 143 ---LHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKkyTIVIVTHnmqqaarisDRta 219
Cdd:COG0488 143 eedLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH---------DR-- 209
|
250
....*....|....*....
gi 123770551 220 FFLN---GELIEMDRTEVI 235
Cdd:COG0488 210 YFLDrvaTRILELDRGKLT 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-239 |
3.99e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYY----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKENFDVVE 84
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-----QAGGLVQCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKR------------VGMVFQSP----NP-FPksVYENVAYAPKIH-GLKDKRKLDEivEKSLRGAALWDEVKDRLHKP 146
Cdd:PRK10261 90 LSEQsaaqmrhvrgadMAMIFQEPmtslNPvFT--VGEQIAESIRLHqGASREEAMVE--AKRMLDQVRIPEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 147 ATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYT--IVIVTHNMQQAARISDRTAFFLNG 224
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
250
....*....|....*
gi 123770551 225 ELIEMDRTEVIFTKP 239
Cdd:PRK10261 246 EAVETGSVEQIFHAP 260
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-227 |
9.48e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.77 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPGvriEGSILFDGVDIYKENfdvVELRKRVGMVF-Qspnp 98
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPT---SGEVRVLGYVPFKRR---KEFARRIGVVFgQ---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 fpKS-------VYENVAYAPKIHGLKD---KRKLDEIVEkslrgaALwdEVKDRLHKPATGLSGGQQQRLCIARALAIEP 168
Cdd:COG4586 104 --RSqlwwdlpAIDSFRLLKAIYRIPDaeyKKRLDELVE------LL--DLGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 169 EVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-206 |
1.21e-22 |
|
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: 96.26 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRIE--GSILFDGVDIYKENFDvvELRKRVGMVFQSPNPF 99
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLAR-------LIVGIWPPtsGSVRLDGADLKQWDRE--TFGKHIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 PKSVYENVAYapkihgLKDKRKLDEIVEKS-LRGAalwDEVKDRLHK-------PA-TGLSGGQQQRLCIARALAIEPEV 170
Cdd:TIGR01842 405 PGTVAENIAR------FGENADPEKIIEAAkLAGV---HELILRLPDgydtvigPGgATLSGGQRQRIALARALYGDPKL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTH 206
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-240 |
1.82e-22 |
|
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: 92.59 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGvriEGSILFDGVD-IYKENFDVVEL 85
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPD---HGTATYIMRSgAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRV------GMVFQSPNPFPK---SVYENVAYAPKIHGLKDKRKLDEIVEKSLRgaalwdEVK---DRLHKPATGLSGG 153
Cdd:TIGR02323 79 ERRRlmrtewGFVHQNPRDGLRmrvSAGANIGERLMAIGARHYGNIRATAQDWLE------EVEidpTRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIEMDR 231
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
....*....
gi 123770551 232 TEVIFTKPR 240
Cdd:TIGR02323 233 TDQVLDDPQ 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-237 |
1.88e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFlrtLNRMNDLIPGvriEGSILFDGVDIykENFDVVEL-RKRVGMVFQSPNPFP 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPL--SDWSAAELaRHRAYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENVA--YAPKIHGLKDKRKLDEIVEkslrgaALwdEVKDRLHKPATGLSGGQQQRLCIARAL-----AIEPE--VL 171
Cdd:COG4138 84 MPVFQYLAlhQPAGASSEAVEQLLAQLAE------AL--GLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 172 LMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-240 |
1.99e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGN----FQALKNISLDIYKNEVTALIGPSGCGKStfLRTLNRMNdLI--PGVRIEGSILFDGVDIYKenF 80
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMG-LIdyPGRVMAEKLEFNGQDLQR--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRKRVG----MVFQSP----NPFPKSVYEnVAYAPKIH--GLKDKRKLDEIVEKSLRGAAlwdEVKDRLHKPATGL 150
Cdd:PRK11022 79 SEKERRNLVGaevaMIFQDPmtslNPCYTVGFQ-IMEAIKVHqgGNKKTRRQRAIDLLNQVGIP---DPASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 151 SGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|..
gi 123770551 229 MDRTEVIFTKPR 240
Cdd:PRK11022 235 TGKAHDIFRAPR 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-235 |
2.40e-22 |
|
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: 95.25 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY-----GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILF----DGVDIYK 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--AGVLEPT---SGEVNVrvgdEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 ENFDVVELRKR-VGMVFQSPNPFP-KSVYENVAYAPKIHGLKDKRKLDEIVekSLRGAALWDE-VKDRLHKPATGLSGGQ 154
Cdd:TIGR03269 355 PGPDGRGRAKRyIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEEkAEEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFLNGELIEMDRT 232
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
...
gi 123770551 233 EVI 235
Cdd:TIGR03269 513 EEI 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-206 |
4.01e-22 |
|
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: 88.66 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvrIEGSILFDGVdiykenfdvvelr 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEP---DEGIVTWGST------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 krvgmvfqspnpfpksvyENVAYAPKihglkdkrkldeivekslrgaalwdevkdrlhkpatgLSGGQQQRLCIARALAI 166
Cdd:cd03221 63 ------------------VKIGYFEQ-------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 123770551 167 EPEVLLMDEPTSALDPIStmrIEELIQELKKKY-TIVIVTH 206
Cdd:cd03221 88 NPNLLLLDEPTNHLDLES---IEALEEALKEYPgTVILVSH 125
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-226 |
5.39e-22 |
|
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: 95.08 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTflrTLNRMNDLIPGVriEGSILFDGVDIyKENFDVVelRKRVGMVFQSPNPFP 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPPT--SGTVLVGGKDI-ETNLDAV--RQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 K-SVYENVAYAPKIHGlkdkRKLDEiveKSLRGAALWDE--VKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPT 177
Cdd:TIGR01257 1017 HlTVAEHILFYAQLKG----RSWEE---AQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123770551 178 SALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-227 |
5.81e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPGVrieGSILFDGVDIYKEnfdVVELR 86
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT--HPDA---GSISLCGEPVPSR---ARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALA 165
Cdd:PRK13537 80 QRVGVVPQFDNLDPDfTVRENLLVFGRYFGLS-AAAARALVPPLLEFAKL----ENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRI-EELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-206 |
7.29e-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: 94.12 E-value: 7.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLipgvrIEGSILFDGVDIYkenfDV--VELRKRVGMVFQSPN 97
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV-----TSGRILIDGQDIR----DVtqASLRAAIGIVPQDTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PFPKSVYENVAYApkihglkdkrKLD---EIVEKSLRGAALWD-----------EVKDRLHKpatgLSGGQQQRLCIARA 163
Cdd:COG5265 443 LFNDTIAYNIAYG----------RPDaseEEVEAAARAAQIHDfieslpdgydtRVGERGLK----LSGGEKQRVAIART 508
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTH 206
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-233 |
1.72e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.47 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 24 NISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPG--------VRIEGSILFDgvdIYKENFDVVELRkRVGMVFQS 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI-------NAISGltrpqkgrIVLNGRVLFD---AEKGICLPPEKR-RIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPFPK-SVYENVAYapkihGLKDKRK--LDEIVEksLRGAalwDEVKDRLhkPATgLSGGQQQRLCIARALAIEPEVLL 172
Cdd:PRK11144 85 ARLFPHyKVRGNLRY-----GMAKSMVaqFDKIVA--LLGI---EPLLDRY--PGS-LSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 173 MDEPTSALD-PistmRIEELI---QELKKKYTIVI--VTHNMQQAARISDRTAFFLNGELIEMDRTE 233
Cdd:PRK11144 152 MDEPLASLDlP----RKRELLpylERLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-207 |
1.84e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.74 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNdlIPGVRI-EGSILFDGVDIykenfdvVEL- 85
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MG--HPKYEVtSGSILLDGEDI-------LELs 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 -----RKRVGMVFQSPNPFP--------KSVYENVAYAPkihgLKDKRKLDEIVEKSlrgaalwDEVK---DRLHKPA-T 148
Cdd:COG0396 71 pderaRAGIFLAFQYPVEIPgvsvsnflRTALNARRGEE----LSAREFLKLLKEKM-------KELGldeDFLDRYVnE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 149 GLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTMRI-EELIQELKKK-YTIVIVTHN 207
Cdd:COG0396 140 GFSGGEKKRNEILQMLLLEPKLAILDETDSGLD-IDALRIvAEGVNKLRSPdRGILIITHY 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-228 |
5.08e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIP--GVRIEGSilfdGVDI-Y----KEN 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPdsGTVKLGE----TVKIgYfdqhQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 FDvvelrkrvgmvfqsPNpfpKSVYENVAYApkihglkdkrkLDEIVEKSLR---GAALWDEvkDRLHKPATGLSGGQQQ 156
Cdd:COG0488 390 LD--------------PD---KTVLDELRDG-----------APGGTEQEVRgylGRFLFSG--DDAFKPVGVLSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDpISTMRI-EELIQElkkkY--TIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLD-IETLEAlEEALDD----FpgTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-206 |
4.09e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQAL-KNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIP-GvriEGSIlfdgvdiykenfdvvE 84
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWPyG---SGRI---------------A 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVF--QSPnpfpksvY-------ENVAYaPKIHGLKDkrklDEIVEKSLRGAALwDEVKDRLHKPA---TGLSG 152
Cdd:COG4178 422 RPAGARVLFlpQRP-------YlplgtlrEALLY-PATAEAFS----DAELREALEAVGL-GHLAERLDEEAdwdQVLSL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTH 206
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-234 |
5.78e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLYygnfQALKNISLDIYKNEVTALIGPSGCGKSTFLRTlnrmndlIPGVR--IEGSILFDG--VDI---- 75
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARA-------LFGADpaDSGEIRLDGkpVRIrspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 76 --------YkenfdVVELRKRVGMVFqspnpfPKSVYENVAYA--PKI--HGLKDKRKLDEIVEKSLRgaALwdEVK-DR 142
Cdd:COG1129 323 dairagiaY-----VPEDRKGEGLVL------DLSIRENITLAslDRLsrGGLLDRRRERALAEEYIK--RL--RIKtPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 143 LHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTMR-IEELIQELKKK-YTIVIVTHNMQQAARISDRTAF 220
Cdd:COG1129 388 PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGAKAeIYRLIRELAAEgKAVIVISSELPELLGLSDRILV 466
|
250
....*....|....*
gi 123770551 221 FLNGELI-EMDRTEV 234
Cdd:COG1129 467 MREGRIVgELDREEA 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-243 |
5.78e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTflrTLNRMNDLIPgvRIEGSILFDGVDIykenfDVVEL----RKRVGM 91
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDI-----SLLPLharaRRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 92 VFQSPNPFPK-SVYENVAYAPKI-HGLKDKRKLDeivekslRGAALWDE-----VKDRLhkpATGLSGGQQQRLCIARAL 164
Cdd:PRK10895 83 LPQEASIFRRlSVYDNLMAVLQIrDDLSAEQRED-------RANELMEEfhiehLRDSM---GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVT-HNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPRDRR 243
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-253 |
1.00e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 85.65 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIP-----GVRIEGSILFDGVDIYKenFDVVELRKRVGMVFQSP 96
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGggaprGARVTGDVTLNGEPLAA--IDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NP-FPKSVYENVAYAPKIHGLK---DKRKLDEIVEKSLR--GAALWDEvkdrlhKPATGLSGGQQQRLCIARALA----- 165
Cdd:PRK13547 93 QPaFAFSAREIVLLGRYPHARRagaLTHRDGEIAWQALAlaGATALVG------RDVTTLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 ----IEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVT--HNMQQAARISDRTAFFLNGELiemdrteVIFTKP 239
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLADGAI-------VAHGAP 239
|
250
....*....|....
gi 123770551 240 RDRRTEDYITGRFG 253
Cdd:PRK13547 240 ADVLTPAHIARCYG 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-207 |
1.37e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVriEGSILFDGVDIykENFDVVE---- 84
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG---LLPPA--AGTIKLDGGDI--DDPDVAEachy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMvfqspNPFpKSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAAlwdevkdrlHKPATGLSGGQQQRLCIARAL 164
Cdd:PRK13539 78 LGHRNAM-----KPA-LTVAENLEFWAAFLGGEELDIAAALEAVGLAPLA---------HLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQE-LKKKYTIVIVTHN 207
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-237 |
1.85e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGVRIEGSILFDGVDIYKEnfdvvELRKRVGMVFQSPNPFPK 101
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPIDAK-----EMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 -SVYENVAYAPKI----HGLKDKRKldEIVEKSLRGAALWDEVKDRLHKPAT--GLSGGQQQRLCIARALAIEPEVLLMD 174
Cdd:TIGR00955 114 lTVREHLMFQAHLrmprRVTKKEKR--ERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 175 EPTSALDPISTMRIEELIQELKKKYTIVIVT-HnmQQAARIsdrtaFFLNGELIEMDRTEVIFT 237
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiH--QPSSEL-----FELFDKIILMAEGRVAYL 248
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-206 |
1.22e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKENFDvvELRKRVGMVFQSPNPFP 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENVAYapkihGLKDKRKldEIVEKSLRGAALWD-----------EVKDRlhkpATGLSGGQQQRLCIARALAIEPE 169
Cdd:PRK10789 403 DTVANNIAL-----GRPDATQ--QEIEHVARLASVHDdilrlpqgydtEVGER----GVMLSGGQKQRISIARALLLNAE 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 123770551 170 VLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTH 206
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-209 |
5.65e-18 |
|
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: 79.68 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 18 NFQALKNISLDIYKNEVTALIGPSGCGKSTFL-RTLNRMNdlipgvRIEGSILFDGVDIYKENFDVVELRKRVGMVFQSP 96
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NPF--PKSVYENVAYAPKIHGLKDKRKLDEI-VEKSLRGAALWDEVKdrLHKPATGLSGGQQQRLCIARALAIEPEVLLM 173
Cdd:cd03290 87 KPWllNATVEENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 123770551 174 DEPTSALD-PISTMRIEELIQELKK--KYTIVIVTHNMQ 209
Cdd:cd03290 165 DDPFSALDiHLSDHLMQEGILKFLQddKRTLVLVTHKLQ 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-213 |
7.41e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.48 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVRI--EGSILFDGVDIYKENFdvve 84
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEVLGGDMADARH---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 lRKRVG-----MvfqsP-----NPFPK-SVYENVAYAPKIHGLkDKRKLDEIVEKSLRGAALwDEVKDRlhkPATGLSGG 153
Cdd:NF033858 71 -RRAVCpriayM----PqglgkNLYPTlSVFENLDFFGRLFGQ-DAAERRRRIDELLRATGL-APFADR---PAGKLSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 154 QQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK---YTIVIVTHNMQQAAR 213
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-233 |
9.23e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.48 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRIE-GSILFDGVDIYKenFDVVELRKRVGMVFQSPNPFP 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI------VELErGRILIDGCDISK--FGLMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENvayapkihglkdkrkLDEIVEKSlrGAALWD-----EVKDRLHKPATGL-----------SGGQQQRLCIARAL 164
Cdd:PLN03130 1327 GTVRFN---------------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 165 AIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTE 233
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPE 1457
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-227 |
9.87e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIykENFDV 82
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP--PS---EGEILLDAQPL--ESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRVGMVFQS-PNPFPKSVYENVAY-------APKIHGLKDKRKLDEIVekSLRGaalwdeVKDRLHKPATGLSGGQ 154
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAIgrypwhgALGRFGAADREKVEEAI--SLVG------LKPLAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 155 QQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-228 |
1.26e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGvriEGSILFDGVD----------------IYKENFDVV 83
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILS--GNYQPD---AGSILIDGQEmrfasttaalaagvaiIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELrkrvgmvfqspnpfpkSVYENV--AYAPKIHGLKDKRKLDEIVEKSLrgAALWDEVKDrlHKPATGLSGGQQQRLCIA 161
Cdd:PRK11288 93 EM----------------TVAENLylGQLPHKGGIVNRRLLNYEAREQL--EHLGVDIDP--DTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 162 RALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVI-VTHNMQQAARISDRTAFFLNGELIE 228
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-226 |
2.00e-17 |
|
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: 77.47 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLYYgnfqALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGVR--IEGSILFDGVDIykeNFD 81
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-------GLRppASGEITLDGKPV---TRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMvfqspnpfpksvyenvAYAP---KIHGLKdkrkLDEIVEKSLRGAALwdevkdrlhkpatgLSGGQQQRL 158
Cdd:cd03215 68 SPRDAIRAGI----------------AYVPedrKREGLV----LDLSVAENIALSSL--------------LSGGNQQKV 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGEL 226
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-206 |
2.15e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQ-ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGVDIYKENF 80
Cdd:PRK10790 336 LQSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLT---EGEIRLDGRPLSSLSH 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVveLRKRVGMVFQSPNPFPKSVYENVAYAPKIHGLKDKRKLdEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCI 160
Cdd:PRK10790 411 SV--LRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTH 206
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-227 |
6.43e-17 |
|
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: 79.48 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGVRIEGSILFDGVDIYKENFDVVElRKRVGMVFQS 95
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS---GVYPHGTWDGEIYWSGSPLKASNIRDTE-RAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPFPK-SVYENVAYAPKIHGLKDKRKLDEIVeksLRGAALWDEVK---DRLHKPATGLSGGQQQRLCIARALAIEPEVL 171
Cdd:TIGR02633 87 LTLVPElSVAENIFLGNEITLPGGRMAYNAMY---LRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 172 LMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-203 |
7.87e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVK-IKVRDLNLYYG---NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGvdiyK 77
Cdd:PTZ00265 377 LKDIKkIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIIND----S 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 ENFDVVEL---RKRVGMVFQSPNPFPKSVYENVAYApkIHGLKDKRKLDEIVEK-------------SLRG--------- 132
Cdd:PTZ00265 448 HNLKDINLkwwRSKIGVVSQDPLLFSNSIKNNIKYS--LYSLKDLEALSNYYNEdgndsqenknkrnSCRAkcagdlndm 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 133 -------------------------------------AALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:PTZ00265 526 snttdsneliemrknyqtikdsevvdvskkvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
250 260 270
....*....|....*....|....*....|.
gi 123770551 176 PTSALDPISTMRIEELIQELK---KKYTIVI 203
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKgneNRITIII 636
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-217 |
8.11e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDliPGvriEGSILFDGVDIYK-ENFDVVEL 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PT---KGTITINNINYNKlDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 rkRVGMVFQSPNPFPK-SVYEN--VAYAP--KIHGLK--DKRKLDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRL 158
Cdd:PRK09700 81 --GIGIIYQELSVIDElTVLENlyIGRHLtkKVCGVNiiDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYT-IVIVTHNMQQAARISDR 217
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDR 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-217 |
1.66e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTflrTLNRMNDLIPGVriEGSI-LF----DGVDIyk 77
Cdd:NF033858 263 DEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKST---TMKMLTGLLPAS--EGEAwLFgqpvDAGDI-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 enfdvvELRKRVGMVFQSpnpFPK----SVYENVAYAPKIHGLKDKR---KLDEIVEK-SLRgaalwdEVKDRLhkpATG 149
Cdd:NF033858 336 ------ATRRRVGYMSQA---FSLygelTVRQNLELHARLFHLPAAEiaaRVAEMLERfDLA------DVADAL---PDS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 150 LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAARiSDR 217
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAER-CDR 466
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-238 |
2.68e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.09 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRIE-GSILFDGVDIYKenFDVV 83
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI------VELEkGRIMIDDCDVAK--FGLT 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENvayapkihglkdkrkLDEIVEKSlrGAALWD-----EVKDRLHKPATGL-------- 150
Cdd:PLN03232 1307 DLRRVLSIIPQSPVLFSGTVRFN---------------IDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevsegg 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 151 ---SGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNGELI 227
Cdd:PLN03232 1370 enfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
250
....*....|.
gi 123770551 228 EMDRTEVIFTK 238
Cdd:PLN03232 1449 EYDSPQELLSR 1459
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-204 |
3.11e-16 |
|
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: 74.61 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 18 NFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGVRIEGSILFDGVDiYKENFDVveLRKRVGMVFQSPN 97
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIP-YKEFAEK--YPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PFPK-SVYENVAYAPKIHGlkdkrklDEIVEkslrgaalwdevkdrlhkpatGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:cd03233 94 HFPTlTVRETLDFALRCKG-------NEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|....*...
gi 123770551 177 TSALDPISTMRIEELIQELKKKYTIVIV 204
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-253 |
6.75e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgvrIE---GSILFDGvdiYKENFDVVELR-KRVGMVFQS 95
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--------IEptsGELLIDD---HPLHFGDYSYRsQRIRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 P----NP---------FPKSVyeNVAYAPKihgLKDKRkldeiVEKSLRGAALwdeVKDRLHKPATGLSGGQQQRLCIAR 162
Cdd:PRK15112 96 PstslNPrqrisqildFPLRL--NTDLEPE---QREKQ-----IIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTI--VIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
250
....*....|...
gi 123770551 241 DRRTEDYITGRFG 253
Cdd:PRK15112 243 HELTKRLIAGHFG 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-235 |
9.50e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRIE--GSILFDGVDIYKENfdvVE 84
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMK-------IIAGIVPPdsGTLEIGGNPCARLT---PA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVG--MVFQSPNPFPK-SVYENVAYA-PKihGLKDKRKLDEIVekslrgAALWDEVKdrLHKPATGLSGGQQQRLCI 160
Cdd:PRK15439 82 KAHQLGiyLVPQEPLLFPNlSVKENILFGlPK--RQASMQKMKQLL------AALGCQLD--LDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 161 ARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRT------AFFLNGELIEMDRTE 233
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQgVGIVFISHKLPEIRQLADRIsvmrdgTIALSGKTADLSTDD 231
|
..
gi 123770551 234 VI 235
Cdd:PRK15439 232 II 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-195 |
1.89e-15 |
|
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: 72.28 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 13 NLYY------GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTL-NRMNDlipGVrIEGSILFDGVDIyKENFdvvel 85
Cdd:cd03232 8 NLNYtvpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTA---GV-ITGEILINGRPL-DKNF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 RKRVGMVFQSPNPFPKSVyenvayapkihglkdkrkldeiVEKSLRGAALwdevkdrlhkpATGLSGGQQQRLCIARALA 165
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLT----------------------VREALRFSAL-----------LRGLSVEQRKRLTIGVELA 124
|
170 180 190
....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQEL 195
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-240 |
2.37e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 25 ISLDIYKNEVTALIGPSGCGKSTFlrtLNRMNDLIPGvriEGSILFDGVDIykENFDVVEL-RKRVGMVFQSPNPFPKSV 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPL--EAWSAAELaRHRAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 104 YENVAY--APKIHGLKDKRKLDEIVEkSLRgaalwdeVKDRLHKPATGLSGGQQQRLCIARAL-----AIEPE--VLLMD 174
Cdd:PRK03695 87 FQYLTLhqPDKTRTEAVASALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 175 EPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTKPR 240
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-206 |
2.42e-15 |
|
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: 72.01 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndLIPgvrIEGSILFDGVDIYKenfdVVELRKR 88
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRP---DSGEVRWNGTPLAE----QRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 89 vGMVFQSPNPFPK---SVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAAlwdevkdrlHKPATGLSGGQQQRLCIARALA 165
Cdd:TIGR01189 74 -NILYLGHLPGLKpelSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE---------DLPAAQLSAGQQRRLALARLWL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123770551 166 IEPEVLLMDEPTSALDPISTMRIEELIQE-LKKKYTIVIVTH 206
Cdd:TIGR01189 144 SRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-206 |
2.50e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndLIPGVRIEGSILFDGVDIYKEnfdvvelrkrvgmvfqspnp 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGRE-------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 fpKSVYENVayaPKIHGLKDKRKLDEIVekSLRGAALWdevkdrLHKPATgLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:COG2401 100 --ASLIDAI---GRKGDFKDAVELLNAV--GLSDAVLW------LRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 123770551 179 ALDPISTMRIEELIQEL--KKKYTIVIVTH 206
Cdd:COG2401 166 HLDRQTAKRVARNLQKLarRAGITLVVATH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-206 |
2.79e-15 |
|
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: 71.03 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQAL-KNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPgvriegsiLFDGvdiykenfdvvel 85
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLWP--------WGSG------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 rkRVGMvfqspnPFPksvyENVAYAPKihglkdKRKLdeiVEKSLRGAAL--WDEVkdrlhkpatgLSGGQQQRLCIARA 163
Cdd:cd03223 57 --RIGM------PEG----EDLLFLPQ------RPYL---PLGTLREQLIypWDDV----------LSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELkkKYTIVIVTH 206
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-227 |
3.50e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGV--RIEGSILFDGVDIykeNFDVVELRKR--VGMVFQS 95
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLT-------GIytRDAGSILYLGKEV---TFNGPKSSQEagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPFPK-SVYENVAYAPKI---HGLKDKRKLDEIVEKSLrgAALwdEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVL 171
Cdd:PRK10762 88 LNLIPQlTIAENIFLGREFvnrFGRIDWKKMYAEADKLL--ARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 172 LMDEPTSALDPISTMRIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-234 |
3.81e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLY-YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVR--IEGSILFDGVDIykENF 80
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELA-------EALAGLRppASGSIRLDGEDI--TGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 DVVELRK-----------RVGMVfqsPNpfpKSVYENVA----YAPKI--HGLKDKRKL----DEIVEK-SLRGAALWDe 138
Cdd:COG3845 326 SPRERRRlgvayipedrlGRGLV---PD---MSVAENLIlgryRRPPFsrGGFLDRKAIrafaEELIEEfDVRTPGPDT- 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 139 vkdrlhkPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDR 217
Cdd:COG3845 399 -------PARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLISEDLDEILALSDR 471
|
250
....*....|....*...
gi 123770551 218 TAFFLNGELI-EMDRTEV 234
Cdd:COG3845 472 IAVMYEGRIVgEVPAAEA 489
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-238 |
7.17e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.86 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNF--QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIYKenFDVV 83
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDISK--LPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFPKSVYENVAyapkihglKDKRKLDEIVEKSLRGAALWDEVKDR-------LHKPATGLSGGQQQ 156
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNGELIEMDRTEVIF 236
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
..
gi 123770551 237 TK 238
Cdd:cd03288 243 AQ 244
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-237 |
9.93e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYYGN-FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndlIPGVRI-EGSILFDGVDIYKE 78
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKAL------MGFVRLaSGKISILGQPTRQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 79 nfdvveLRKR-VGMVFQSPN---PFPKSVYENVAYAPKIH-GL--KDKRKLDEIVEKSLrgaALWDEVKDRlHKPATGLS 151
Cdd:PRK15056 75 ------LQKNlVAYVPQSEEvdwSFPVLVEDVVMMGRYGHmGWlrRAKKRDRQIVTAAL---ARVDMVEFR-HRQIGELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 152 GGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAfFLNGELIEMD 230
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASG 223
|
....*..
gi 123770551 231 RTEVIFT 237
Cdd:PRK15056 224 PTETTFT 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-235 |
1.51e-14 |
|
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: 72.66 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRIEgsilFDGVDIYKENFdvvelrkRVGMVFQ 94
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAGVDKD----FNGEARPQPGI-------KVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNPFP-KSVYENVayapkIHGLKDKR----KLDEI--------------------VEKSLRGAALWD-----EVK-DRL 143
Cdd:TIGR03719 76 EPQLDPtKTVRENV-----EEGVAEIKdaldRFNEIsakyaepdadfdklaaeqaeLQEIIDAADAWDldsqlEIAmDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 144 HKPA-----TGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKkyTIVIVTHnmqqaarisDRt 218
Cdd:TIGR03719 151 RCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH---------DR- 218
|
250 260
....*....|....*....|
gi 123770551 219 aFFLN---GELIEMDRTEVI 235
Cdd:TIGR03719 219 -YFLDnvaGWILELDRGRGI 237
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-239 |
6.74e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.93 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 17 GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLR------------TLNRMNdlipgvriegsilFDGVDIYKenFDVVE 84
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaicgitkdnwhvTADRFR-------------WNGIDLLK--LSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVG----MVFQSP----NPfpksvyenvayAPKIhglkdKRKLDE-IVEKSLRGAaLWDEVKDR-------LHKpaT 148
Cdd:COG4170 83 RRKIIGreiaMIFQEPssclDP-----------SAKI-----GDQLIEaIPSWTFKGK-WWQRFKWRkkraielLHR--V 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 149 G--------------LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK--KYTIVIVTHNMQQAA 212
Cdd:COG4170 144 GikdhkdimnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESIS 223
|
250 260
....*....|....*....|....*..
gi 123770551 213 RISDRTAFFLNGELIEMDRTEVIFTKP 239
Cdd:COG4170 224 QWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-214 |
1.00e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 33 EVTALIGPSGCGKSTFLrtlNRMNDLIPGVRIEGSILFDGVDIYKEnfdvveLRKRVGMVFQSPNPFPK-SVYENVAYA- 110
Cdd:PLN03211 95 EILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQ------ILKRTGFVTQDDILYPHlTVRETLVFCs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 111 ----PKIHGLKDKRKLDEIVEKSLRGAALWDEVKDrlHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTM 186
Cdd:PLN03211 166 llrlPKSLTKQEKILVAESVISELGLTKCENTIIG--NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|....*....
gi 123770551 187 RIEELIQELKKK-YTIVIVTHnmQQAARI 214
Cdd:PLN03211 244 RLVLTLGSLAQKgKTIVTSMH--QPSSRV 270
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-233 |
1.06e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRdlNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKENFD-- 81
Cdd:PRK10982 248 EVILEVR--NLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-----KSAGTITLHGKKINNHNANea 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 -------VVELRKRVGMVFQSPNPFpKSVYENV-AYAPKIHGLKDKR-KLD-EIVEKSLRgaalwdeVKDRLHKPATG-L 150
Cdd:PRK10982 321 inhgfalVTEERRSTGIYAYLDIGF-NSLISNIrNYKNKVGLLDNSRmKSDtQWVIDSMR-------VKTPGHRTQIGsL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 151 SGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFLNGELIEM 229
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
....
gi 123770551 230 DRTE 233
Cdd:PRK10982 473 VDTK 476
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-206 |
1.09e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndliPGVRI-EGSILFDGVDIYKEN 79
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH----PAYKIlEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 fdvVELRKRVG--MVFQSPNPFPKSVYEN---VAYAP--KIHGLKDKRKLD--EIVEKSLRGAALwDEVkdRLHKPAT-G 149
Cdd:CHL00131 78 ---PEERAHLGifLAFQYPIEIPGVSNADflrLAYNSkrKFQGLPELDPLEflEIINEKLKLVGM-DPS--FLSRNVNeG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 150 LSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTMR-IEELIQELK-KKYTIVIVTH 206
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKiIAEGINKLMtSENSIILITH 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-216 |
1.16e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 14 LYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRmndlipgvrieGSILFDGVDIYKENFDVVELRkrvgmvf 93
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-----------EVLLDDGRIIYEQDLIVARLQ------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 94 QSPnpfPK----SVYENVA--------YAPKIHGLKDK----------RKLDEIVEKsLRGAALW---DEVKDRL----- 143
Cdd:PRK11147 73 QDP---PRnvegTVYDFVAegieeqaeYLKRYHDISHLvetdpseknlNELAKLQEQ-LDHHNLWqleNRINEVLaqlgl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 144 --HKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTmrIEELIQELKK-KYTIVIVTH------NMqqAARI 214
Cdd:PRK11147 149 dpDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirNM--ATRI 223
|
..
gi 123770551 215 SD 216
Cdd:PRK11147 224 VD 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-248 |
1.19e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 16 YGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGVRIEGSILFDGVDIYKENFDVVElRKRVGMVFQS 95
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFEGEELQASNIRDTE-RAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPFPK-SVYENVAYAPKI--HGLKDKRKLdeivekSLRGAALWDEVKDRL--HKPATGLSGGQQQRLCIARALAIEPEV 170
Cdd:PRK13549 91 LALVKElSVLENIFLGNEItpGGIMDYDAM------YLRAQKLLAQLKLDInpATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEmdrtevifTKPRDRRTEDYI 248
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISDTICVIRDGRHIG--------TRPAAGMTEDDI 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-248 |
2.85e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.29 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 17 GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTL---NRMNDLIPGVRIEgsilFDGVDIYKenFDVVELRKRVG--- 90
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvTKDNWRVTADRMR----FDDIDLLR--LSPRERRKLVGhnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 91 -MVFQSP----NPfPKSVYENVAYApkIHGLKDK-RKLDEIVEKSLRGAALWDEVKDRLHKPATG-----LSGGQQQRLC 159
Cdd:PRK15093 92 sMIFQEPqsclDP-SERVGRQLMQN--IPGWTYKgRWWQRFGWRKRRAIELLHRVGIKDHKDAMRsfpyeLTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFT 237
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
250
....*....|.
gi 123770551 238 KPRDRRTEDYI 248
Cdd:PRK15093 249 TPHHPYTQALI 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-226 |
4.80e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 23 KNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGVR--IEGSILFDGVDIykeNFDVVELRKRVGMVF-----QS 95
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLY-------GLRpaRGGRIMLNGKEI---NALSTAQRLARGLVYlpedrQS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPF-PKSVYENV-AYAPKIHGLKDKRKLDE-IVEKSLRgaALWDEVKDrLHKPATGLSGGQQQRLCIARALAIEPEVLL 172
Cdd:PRK15439 350 SGLYlDAPLAWNVcALTHNRRGFWIKPARENaVLERYRR--ALNIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 173 MDEPTSALDPISTMRIEELIQELKKKYTIVI-VTHNMQQAARISDRTAFFLNGEL 226
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-234 |
5.03e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYKenFDVVELRKRVGMVFQSPNPFPK 101
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNIAK--IGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENV----AYApkihglkdkrklDEIVEKSLRGAALWDEVK---DRL-HKPATG---LSGGQQQRLCIARALAIEPEV 170
Cdd:TIGR00957 1375 SLRMNLdpfsQYS------------DEEVWWALELAHLKTFVSalpDKLdHECAEGgenLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 171 LLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQaarISDRTafflngELIEMDRTEV 234
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYT------RVIVLDKGEV 1497
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-209 |
5.42e-13 |
|
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: 66.80 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRIEGSILFDGVdiykeNFDVV 83
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGV-----SWNSV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 EL---RKRVGMVFQSPNPFPKSVYENV-AYA----PKIHGLKDKRKLDEIVEKslrgaaLWDEVKDRLHKPATGLSGGQQ 155
Cdd:cd03289 71 PLqkwRKAFGVIPQKVFIFSGTFRKNLdPYGkwsdEEIWKVAEEVGLKSVIEQ------FPGQLDFVLVDGGCVLSHGHK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123770551 156 QRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQ 209
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-227 |
1.05e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIykeNFDVVE--LRKRVGMVFQSPN 97
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEI---DFKSSKeaLENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PF-PKSVYENV--AYAPKIHGLKDKRKLDEIVEkslrgaALWDEVK---DRLHKPATgLSGGQQQRLCIARALAIEPEVL 171
Cdd:PRK10982 84 LVlQRSVMDNMwlGRYPTKGMFVDQDKMYRDTK------AIFDELDidiDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 172 LMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELI 227
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-208 |
1.06e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 31 KNEVTALIGPSGCGKSTFLRTLNrmNDLIPGV-RIEGSILFDGVdiykenfdvveLRKRVGMVFQspNPFpKSVYEN--- 106
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILS--GELIPNLgDYEEEPSWDEV-----------LKRFRGTELQ--NYF-KKLYNGeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 107 -------VAYAPKIhgLKDK-----RKLDEivekslRGAalWDEVKDRL------HKPATGLSGGQQQRLCIARALAIEP 168
Cdd:PRK13409 162 vvhkpqyVDLIPKV--FKGKvrellKKVDE------RGK--LDEVVERLglenilDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123770551 169 EVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNM 208
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-248 |
2.97e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 13 NLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGV--RIEGSILFDGVDIyKENFDVVELRKRVG 90
Cdd:PRK09700 270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELM-------NCLFGVdkRAGGEIRLNGKDI-SPRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 91 MVFQSPNP---FPK-SVYENVAYAPKIH--------GLKDKRKLDEIVEKSLRGAALwdeVKDRLHKPATGLSGGQQQRL 158
Cdd:PRK09700 342 YITESRRDngfFPNfSIAQNMAISRSLKdggykgamGLFHEVDEQRTAENQRELLAL---KCHSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIEmdrtevIFT 237
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQ------ILT 492
|
250
....*....|.
gi 123770551 238 KpRDRRTEDYI 248
Cdd:PRK09700 493 N-RDDMSEEEI 502
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-206 |
3.62e-12 |
|
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: 63.67 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPG-VRIEGSILFDGVDIYKENfdvvelrkrvgMVFQSPNPFP 100
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDFQRDSIARG-----------LLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 K---SVYENVAYAPKIHGlkDKRKLDEIVEKSLRGAAlwdevkdrlHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPT 177
Cdd:cd03231 85 KttlSVLENLRFWHADHS--DEQVEEALARVGLNGFE---------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 123770551 178 SALDPISTMRIEELI-QELKKKYTIVIVTH 206
Cdd:cd03231 154 TALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-217 |
4.22e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQaLKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPgvrIEGSILFDgVDI-YKENFD 81
Cdd:PRK13409 337 RETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLA--GVLKP---DEGEVDPE-LKIsYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNPFPKSVYENVAYapkIHGLKdkrkLDEIVEKSLrgaalwdevkdrlhkpaTGLSGGQQQRLCIA 161
Cdd:PRK13409 410 KPDYDGTVEDLLRSITDDLGSSYYKSEI---IKPLQ----LERLLDKNV-----------------KDLSGGELQRVAIA 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 162 RALAIEPEVLLMDEPTSALD---PISTMRIEELIQELKKKyTIVIVTHNMQQAARISDR 217
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRIAEEREA-TALVVDHDIYMIDYISDR 523
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-208 |
5.12e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.35 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTL-NRMNDLIPGVRIEGSILFDGVDIYKENfdvVELRKRVGMVFQSPNPFP 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVHMKGSVAYVPQQAWIQN---DSLRENILFGKALNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 101 KSVYENVAYAPKIHGLKDKRKlDEIVEKSLRgaalwdevkdrlhkpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSAL 180
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDR-TEIGEKGVN------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190
....*....|....*....|....*....|.
gi 123770551 181 DPISTMRIEELI---QELKKKYTIVIVTHNM 208
Cdd:TIGR00957 792 DAHVGKHIFEHVigpEGVLKNKTRILVTHGI 822
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-229 |
8.44e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIpgvriEGSILFDGVDIykENFDVVELRKRVGMVFQSPNPFPK 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVC-----GGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENVAYAPKIHGLKDKRKLdEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPE-VLLMDEPTSAL 180
Cdd:PTZ00243 1399 TVRQNVDPFLEASSAEVWAAL-ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANI 1477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123770551 181 DPISTMRIEELIQELKKKYTIVIVTHNMQQAARIsDRTAFFLNGELIEM 229
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEM 1525
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-204 |
9.48e-12 |
|
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: 64.42 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 31 KNEVTALIGPSGCGKSTFLRTLNrmNDLIPGV--------------RIEGSILFDgvdiYKEnfDVVELRKRVGMvfqsp 96
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILS--GELKPNLgdydeepswdevlkRFRGTELQD----YFK--KLANGEIKVAH----- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 npfpKSVYenVAYAPKIHGLK--------DKR-KLDEIVEKsLRGAALWDevkdrlhKPATGLSGGQQQRLCIARALAIE 167
Cdd:COG1245 165 ----KPQY--VDLIPKVFKGTvrellekvDERgKLDELAEK-LGLENILD-------RDISELSGGELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 123770551 168 PEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIV 204
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLV 267
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-217 |
1.26e-11 |
|
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: 64.04 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQaLKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPGvriEGSILFDgVDI-YKENFD 81
Cdd:COG1245 338 EETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILA--GVLKPD---EGEVDED-LKIsYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELRKRVGMVFQSPNP--FPKSVYENvayapkihglkdkrkldEIVEKsLRgaalwdeVKDRLHKPATGLSGGQQQRLC 159
Cdd:COG1245 411 SPDYDGTVEEFLRSANTddFGSSYYKT-----------------EIIKP-LG-------LEKLLDKNVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 160 IARALAIEPEVLLMDEPTSALDPISTMRIEELIQ---ELKKKYTIViVTHNMQQAARISDR 217
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaENRGKTAMV-VDHDIYLIDYISDR 525
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-208 |
1.76e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGvdiykenfdvvelR 86
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAPD---EGVIKRNG-------------K 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVGMVFQSPN---PFPKSVYENVAYAPkihGLKDKRKLDEIveKSLRGAALwdevkdrLHKPATGLSGGQQQRLCIARA 163
Cdd:PRK09544 67 LRIGYVPQKLYldtTLPLTVNRFLRLRP---GTKKEDILPAL--KRVQAGHL-------IDAPMQKLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK--YTIVIVTHNM 208
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-221 |
1.77e-11 |
|
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: 62.43 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 28 DIYKNEVTALIGPSGCGKSTFLRTLnrmndlipgvriEGSILFDGVDIYKENFDVvelrkrvgmvfqSPNP------FPK 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEGDIEIELDTV------------SYKPqyikadYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENVAYAPKIHGLKDKRKLDeiVEKSLRGAALWD-EVKDrlhkpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSAL 180
Cdd:cd03237 77 TVRDLLSSITKDFYTHPYFKTE--IAKPLQIEQILDrEVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123770551 181 DPISTMRIEELIQE--LKKKYTIVIVTHNMQQAARISDRTAFF 221
Cdd:cd03237 147 DVEQRLMASKVIRRfaENNEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-209 |
2.78e-11 |
|
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: 63.39 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYY--GNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMndlipgVRIEGSILFDGVdiykeNFDVVEL- 85
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDGV-----SWNSVTLq 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 --RKRVGMVFQSPNPFPKSVYENV-AYA----PKIHGLKDKRKLDEIVEKslrgaaLWDEVKDRLHKPATGLSGGQQQRL 158
Cdd:TIGR01271 1289 twRKAFGVIPQKVFIFSGTFRKNLdPYEqwsdEEIWKVAEEVGLKSVIEQ------FPDKLDFVLVDGGYVLSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123770551 159 CIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQ 209
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-224 |
3.48e-11 |
|
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: 63.01 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 11 DLNLYYGNFQ-----ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGvdiykenfdvvel 85
Cdd:TIGR01271 426 DDGLFFSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSG------------- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 rkRVGMVFQSPNPFPKSVYENVayapkIHGLKdkrkLDEIVEKSLRGAALWDE------VKDR--LHKPATGLSGGQQQR 157
Cdd:TIGR01271 488 --RISFSPQTSWIMPGTIKDNI-----IFGLS----YDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGITLSGGQRAR 556
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRI-EELIQELKKKYTIVIVTHNMQQAARiSDRTAFFLNG 224
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-226 |
1.17e-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: 60.99 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLYYGNFQALK---NISLDIYKNEVTALIGPSGCGKSTFLRTLNrmnDLIPGvRIEGSILFDGVDIYKENF 80
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALF---GAYPG-KFEGNVFINGKPVDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 D---------VVELRKRVGMVFQspnpfpKSVYENVAYApKIHGLKDKRKLDEIVEKSLRGAALwdevkDRLHK------ 145
Cdd:TIGR02633 331 AqairagiamVPEDRKRHGIVPI------LGVGKNITLS-VLKSFCFKMRIDAAAELQIIGSAI-----QRLKVktaspf 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 146 -PATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLN 223
Cdd:TIGR02633 399 lPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGE 478
|
...
gi 123770551 224 GEL 226
Cdd:TIGR02633 479 GKL 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-206 |
1.33e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvrIEGSILfdgvdiYKENfdvvelrkr 88
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEP---DSGTVK------WSEN--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 89 vgmvfqspnpfpksvyENVAYAPKIHG--------LKD------KRKLDEIVEKSLRGAALW--DEVKdrlhKPATGLSG 152
Cdd:PRK15064 382 ----------------ANIGYYAQDHAydfendltLFDwmsqwrQEGDDEQAVRGTLGRLLFsqDDIK----KSVKVLSG 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 153 GQQQRLCIARALAIEPEVLLMDEPTSALDPIStmrIEELIQELKK-KYTIVIVTH 206
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSH 493
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-209 |
1.74e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 9 VRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIP-------GVRIEGSILfdgvDIYKENFD 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQAdsgrihcGTKLEVAYF----DQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 vvelrkrvgmvfqsPNpfpKSVYENVAyapkiHGLKDkrkldeiVEKSLRGAALWDEVKD------RLHKPATGLSGGQQ 155
Cdd:PRK11147 396 --------------PE---KTVMDNLA-----EGKQE-------VMVNGRPRHVLGYLQDflfhpkRAMTPVKALSGGER 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 156 QRLCIARaLAIEPEVLL-MDEPTSALDpISTMrieELIQELKKKY--TIVIVTHNMQ 209
Cdd:PRK11147 447 NRLLLAR-LFLKPSNLLiLDEPTNDLD-VETL---ELLEELLDSYqgTVLLVSHDRQ 498
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-217 |
3.03e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNlyyGnfQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV--RIEGSILFDGVDIY----K 77
Cdd:PRK10762 255 EVRLKVDNLS---G--PGVNDVSFTLRKGEILGVSGLMGAGRTELMK-------VLYGAlpRTSGYVTLDGHEVVtrspQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 ENFD-----VVELRKRVGMVFQspnpfpKSVYENVA-----YAPKIHGLKDKRKLDEIVEKSLRgaaLWDEVKDRLHKPA 147
Cdd:PRK10762 323 DGLAngivyISEDRKRDGLVLG------MSVKENMSltalrYFSRAGGSLKHADEQQAVSDFIR---LFNIKTPSMEQAI 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 148 TGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDR 217
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDR 464
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-195 |
4.16e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLyygnfqaLKNISLDIYKNEVTALIGPSGCGKSTFLRTL-NRMNDlipGVRIEGSILFDGVDIyKENFdv 82
Cdd:TIGR00956 768 EVKIKKEKRVI-------LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTT---GVITGGDRLVNGRPL-DSSF-- 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 velRKRVGMVFQSPNPFPKS-VYENVAYA-----PKIHGLKDKrklDEIVEKSLRGAALWDEVKDRLHKPATGLSGGQQQ 156
Cdd:TIGR00956 835 ---QRSIGYVQQQDLHLPTStVRESLRFSaylrqPKSVSKSEK---MEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRK 908
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123770551 157 RLCIARALAIEPEVLL-MDEPTSALDPISTMRIEELIQEL 195
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-248 |
4.31e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNrmndlipGV----RIEGSILFDGvdiykenfDVVELRK-----RVGM 91
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-------GVyphgSYEGEILFDG--------EVCRFKDirdseALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 92 VF--QSPNPFPK-SVYENVAYAPkihglkdkrkldeivEKSLRGAALWDEVKDR----LHK------PATGLSG---GQQ 155
Cdd:NF040905 81 VIihQELALIPYlSIAENIFLGN---------------ERAKRGVIDWNETNRRarelLAKvgldesPDTLVTDigvGKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 156 QRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFLNGELIE---MDR 231
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSITVLRDGRTIEtldCRA 225
|
250
....*....|....*..
gi 123770551 232 TEViftkprdrrTEDYI 248
Cdd:NF040905 226 DEV---------TEDRI 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-225 |
4.44e-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: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 11 DLNLYYGNFQ-----ALKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriEGSILFDGvdiykenfdvvel 85
Cdd:cd03291 37 DNNLFFSNLClvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSG------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 86 rkRVGMVFQSPNPFPKSVYENVayapkIHGLKdkrkLDEIVEKSLRGAALWDE------VKDR--LHKPATGLSGGQQQR 157
Cdd:cd03291 99 --RISFSSQFSWIMPGTIKENI-----IFGVS----YDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123770551 158 LCIARALAIEPEVLLMDEPTSALDPISTMRI-EELIQELKKKYTIVIVTHNMQQaARISDRTAFFLNGE 225
Cdd:cd03291 168 ISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-208 |
4.96e-10 |
|
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: 58.15 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 33 EVTALIGPSGCGKSTFLRTLNrmNDLIPGVRIEGS------IL--FDGVDIYKENFDVVELRKRVGMVFQSPNPFPKSVY 104
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILA--GKLKPNLGKFDDppdwdeILdeFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 105 ENVAyapKIHGLKDKR-KLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPI 183
Cdd:cd03236 105 GKVG---ELLKKKDERgKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*.
gi 123770551 184 STMRIEELIQEL-KKKYTIVIVTHNM 208
Cdd:cd03236 174 QRLNAARLIRELaEDDNYVLVVEHDL 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-235 |
5.48e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRIEgsilFDGVDIYKENFdvvelrkRVGMVFQSP--N 97
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAGVDKE----FEGEARPAPGI-------KVGYLPQEPqlD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PfPKSVYENVAYApkIHGLKDK-RKLDEI--------------------VEKSLRGAALWD-----EVK-DRLHKPA--- 147
Cdd:PRK11819 83 P-EKTVRENVEEG--VAEVKAAlDRFNEIyaayaepdadfdalaaeqgeLQEIIDAADAWDldsqlEIAmDALRCPPwda 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 148 --TGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPIStmrIEELIQELKK-KYTIVIVTHnmqqaarisDRtaFFLN- 223
Cdd:PRK11819 160 kvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDyPGTVVAVTH---------DR--YFLDn 225
|
250
....*....|....
gi 123770551 224 --GELIEMDRTEVI 235
Cdd:PRK11819 226 vaGWILELDRGRGI 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-230 |
1.20e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYG--NFqALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNdlIPgvrIEGSILFDGVDIYKENFDvv 83
Cdd:PRK10522 322 TLELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY--QP---QSGEILLDGKPVTAEQPE-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 84 ELRKRVGMVFQSPNPFpksvyenvayaPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHKPA-TGLSGGQQQRLCIAR 162
Cdd:PRK10522 394 DYRKLFSAVFTDFHLF-----------DQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISnLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 163 ALAIEPEVLLMDEPTSALDPisTMRIE---ELIQELKKK-YTIVIVTHN---MQQAarisDRTAFFLNGELIEMD 230
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDP--HFRREfyqVLLPLLQEMgKTIFAISHDdhyFIHA----DRLLEMRNGQLSELT 531
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-206 |
1.89e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSdvkikVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLipgVRIEGSILFDGVDIYKenf 80
Cdd:PRK09580 1 MLS-----IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY---EVTGGTVEFKGKDLLE--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvVELRKRVG----MVFQSPNPFPkSVYENVAYAPKIHGLKDKRKL---------DEIVEKslrgAALWDEVKDRLHKPA 147
Cdd:PRK09580 70 --LSPEDRAGegifMAFQYPVEIP-GVSNQFFLQTALNAVRSYRGQepldrfdfqDLMEEK----IALLKMPEDLLTRSV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 148 T-GLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK-KYTIVIVTH 206
Cdd:PRK09580 143 NvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTH 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-228 |
6.87e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTflrtLNRMndlipgvrIEGSILFDGVDIyKENFDVVELRKRVGMVFQSpnp 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKST----LSNI--------IGGSLSPTVGKV-DRNGEVSVIAISAGLSGQL--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 fpkSVYENVAYAPKIHGLKDK--RKL-DEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDE 175
Cdd:PRK13546 101 ---TGIENIEFKMLCMGFKRKeiKAMtPKIIEFS--------ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123770551 176 PTSALDPISTMRIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFLNGELIE 228
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
8-210 |
8.03e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 8.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 8 KVRDLNLYYGNFQ---ALKNISLDIYKNEVTALIGPSGCGKSTflrtlnrMNDLIPGVRIEgsilfdgvdiykeNFDVVE 84
Cdd:PRK13545 23 KLKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKST-------LSNLIAGVTMP-------------NKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSPNPFPK-SVYENVAYAPKIHGLKdKRKLDEIVEKSLRGAalwdEVKDRLHKPATGLSGGQQQRLCIARA 163
Cdd:PRK13545 83 IKGSAALIAISSGLNGQlTGIENIELKGLMMGLT-KEKIKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAIS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123770551 164 LAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQ 210
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQ 205
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-217 |
1.72e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.27 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 24 NISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipgvRIEGSILFDGVDIYK--ENF--DVVELRKRVGMvfqspnpf 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR-----PDAGEVLWQGEPIRRqrDEYhqDLLYLGHQPGI-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 100 pKSV---YENVAYAPKIHGLKDkrklDEIVEKSLRGAALwdevKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:PRK13538 86 -KTEltaLENLRFYQRLHGPGD----DEALWEALAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123770551 177 TSALDPISTMRIEELIQELKKKYTIVIVT-HnmQQAARISDR 217
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTtH--QDLPVASDK 196
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-216 |
1.72e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.71 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLyygnfQALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmndlipgvriegsilFDGvdIYKEnfdvveLR 86
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--------------------NEG--LYAS------GK 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 87 KRVgmvfqspNPFPKSVYENVAYAPKihglkdkrKLDEIVEKSLRGAalwdevkdRLHKPATGLSGGQQQRLCIARALAI 166
Cdd:cd03238 48 ARL-------ISFLPKFSRNKLIFID--------QLQFLIDVGLGYL--------TLGQKLSTLSGGELQRVKLASELFS 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 167 EPE--VLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHN---MQQAARISD 216
Cdd:cd03238 105 EPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-206 |
2.35e-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: 54.17 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDgvdiyken 79
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR-------MITGQEQpdSGTIEIG-------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 fDVVELrkrvGMVFQS-----PNpfpKSVYENVAYApkihglkdkrkLDEIVEKSLrgaalwdEVKDRLH---------- 144
Cdd:TIGR03719 383 -ETVKL----AYVDQSrdaldPN---KTVWEEISGG-----------LDIIKLGKR-------EIPSRAYvgrfnfkgsd 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123770551 145 --KPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTMR-IEELIQELKKkyTIVIVTH 206
Cdd:TIGR03719 437 qqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-VETLRaLEEALLNFAG--CAVVISH 498
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-181 |
2.55e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 20 QALKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmnDLIPGVR----IEGSILFDGVDIYKENFDVVElrkrvGMVFQS 95
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKtggyIEGDIRISGFPKKQETFARIS-----GYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 96 PNPFPK-SVYENVAYA-----PKIHGLKDK-RKLDEIVEkslrgAALWDEVKDRL--HKPATGLSGGQQQRLCIARALAI 166
Cdd:PLN03140 962 DIHSPQvTVRESLIYSaflrlPKEVSKEEKmMFVDEVME-----LVELDNLKDAIvgLPGVTGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*
gi 123770551 167 EPEVLLMDEPTSALD 181
Cdd:PLN03140 1037 NPSIIFMDEPTSGLD 1051
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-222 |
5.57e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV-RIE-GSILFDGVDIYKenfDVVE 84
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLK-------LIAGLlNPEkGEILFERQSIKK---DLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 85 LRKRVGMVFQSP--NPFpKSVYENVAYapKIHGLKDKRKLDEIVEKSlrgaalwdEVKDRLHKPATGLSGGQQQRLCIAR 162
Cdd:PRK13540 72 YQKQLCFVGHRSgiNPY-LTLRENCLY--DIHFSPGAVGITELCRLF--------SLEHLIDYPCGLLSSGQKRQVALLR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFL 222
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-217 |
5.98e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNlyygnFQALKN-ISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGV--RIEGSILFDGVDI-YK 77
Cdd:PRK11288 253 LGEVRLRLDGLK-----GPGLREpISFSVRAGEIVGLFGLVGAGRSELMK-------LLYGAtrRTAGQVYLDGKPIdIR 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 78 ENFDVV--------ELRKRVGMVFQSpnpfpkSVYENVAYAPKIHGLK-----DKRKLDEIVE---KSLRgaalwdeVKD 141
Cdd:PRK11288 321 SPRDAIragimlcpEDRKAEGIIPVH------SVADNINISARRHHLRagcliNNRWEAENADrfiRSLN-------IKT 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 142 R-LHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNMQQAARISDR 217
Cdd:PRK11288 388 PsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADR 465
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-208 |
8.10e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.85 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLrtlnrmND-LIPGVriegSILFDGVDIYKENFDVVE-LRK--RVGMVFQSP- 96
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI------NDtLYPAL----ARRLHLKKEQPGNHDRIEgLEHidKVIVIDQSPi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 ------NPfpkSVYENV------AYAPKIHGlkdKRKLDEIVEKSLRGAALWD-----------------EVKDRLH--- 144
Cdd:cd03271 81 grtprsNP---ATYTGVfdeireLFCEVCKG---KRYNRETLEVRYKGKSIADvldmtveealeffenipKIARKLQtlc 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 145 ----------KPATGLSGGQQQRLCIARAL---AIEPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTHNM 208
Cdd:cd03271 155 dvglgyiklgQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNL 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-206 |
8.86e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 8.86e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 144 HKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIqeLKKKYTIVIVTH 206
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-225 |
1.00e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 7 IKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLN------RMNDLIPGVRIEGSilfdGVDIYkenf 80
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgYSNDLTLFGRRRGS----GETIW---- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 81 dvvELRKRVGMVFQSpnpfpksvyenvayapkIHglkdkrkLDEIVEKSLRGAAL---------WDEVKDRLHK------ 145
Cdd:PRK10938 333 ---DIKKHIGYVSSS-----------------LH-------LDYRVSTSVRNVILsgffdsigiYQAVSDRQQKlaqqwl 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 146 ------------PATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPIStmR------IEELIQELKKKytIVIVTHN 207
Cdd:PRK10938 386 dilgidkrtadaPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLN--RqlvrrfVDVLISEGETQ--LLFVSHH 461
|
250
....*....|....*....
gi 123770551 208 MQQAAR-ISDRTAFFLNGE 225
Cdd:PRK10938 462 AEDAPAcITHRLEFVPDGD 480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-238 |
2.48e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 117 KDKR-KLDEIVEK-SLRGAAlwdevkdrlHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRI-EELIQ 193
Cdd:NF000106 119 KDARaRADELLERfSLTEAA---------GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRS 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 123770551 194 ELKKKYTIVIVTHNMQQAARISDRTAFFLNGELIEMDRTEVIFTK 238
Cdd:NF000106 190 MVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-238 |
3.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrMNDLIPGvriegsilfdgvdiykENFDVVeLRKRVGMVFQSPNPFPK 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHA----------------ETSSVV-IRGSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 102 SVYENVAYAPKIHGLKDKRKLD-EIVEKSLRGAALWD--EVKDRlhkpATGLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:PLN03232 694 TVRENILFGSDFESERYWRAIDvTALQHDLDLLPGRDltEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 179 ALDP-ISTMRIEELIQELKKKYTIVIVT---HNMQQAARISDRTAFFLN--GELIEMDRTEVIFTK 238
Cdd:PLN03232 770 ALDAhVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDRIILVSEGMIKeeGTFAELSKSGSLFKK 835
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-213 |
3.94e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKSTFLRTLnrmndlipgvriegsilfdgvdiyKENFDVVELR----KRVGMVFQSPN 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSL------------------------LSQFEISEGRvwaeRSIAYVPQQAW 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 PFPKSVYENVAYAPKihglKDKRKLDEIV-----EKSLR--GAALWDEVKDRlhkpATGLSGGQQQRLCIARALAIEPEV 170
Cdd:PTZ00243 732 IMNATVRGNILFFDE----EDAARLADAVrvsqlEADLAqlGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123770551 171 LLMDEPTSALDPISTMRI-EELIQELKKKYTIVIVTHNMQQAAR 213
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVvEECFLGALAGKTRVLATHQVHVVPR 847
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-214 |
3.96e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGK----STFLRTLNRMNDliPGVRIEGSILFDGVDIYKENFDVvelrkRVGMVFQSPn 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKtsliSAMLGELPPRSD--ASVVIRGTVAYVPQVSWIFNATV-----RDNILFGSP- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 98 pfpksvYENVAYAPKIHGLKDKRKLDeivekSLRGAALwDEVKDRlhkpATGLSGGQQQRLCIARALAIEPEVLLMDEPT 177
Cdd:PLN03130 705 ------FDPERYERAIDVTALQHDLD-----LLPGGDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123770551 178 SALDPISTMRIEE--LIQELKKKyTIVIVT---HNMQQAARI 214
Cdd:PLN03130 769 SALDAHVGRQVFDkcIKDELRGK-TRVLVTnqlHFLSQVDRI 809
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-206 |
4.34e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 50.18 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 21 ALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGVRI--EGSILFDGVDIYKENFDvvELRKRVGMVFQSPNP 98
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAK-------LLTGLYRpeSGEILLDGQPVTADNRE--AYRQLFSAVFSDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 99 FPKsVY--ENVAYAPKIHGLKDKRKLDEIVekSLRGAALWDevkdrlhkpaTGLSGGQQQRLCIARALAIEPEVLLMDEP 176
Cdd:COG4615 418 FDR-LLglDGEADPARARELLERLELDHKV--SVEDGRFST----------TDLSQGQRKRLALLVALLEDRPILVFDEW 484
|
170 180 190
....*....|....*....|....*....|...
gi 123770551 177 TSALDPISTmRI--EELIQELKKK-YTIVIVTH 206
Cdd:COG4615 485 AADQDPEFR-RVfyTELLPELKARgKTVIAISH 516
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-203 |
6.66e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 4 DVKIKVRDLNLY---YGNFQALKNISLDIYKNEVTALIGPSGCGK-----STFLRTLnrmndlipGVRIEGSILFDGVDI 75
Cdd:NF040905 255 EVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRtelamSVFGRSY--------GRNISGTVFKDGKEV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 76 YKENFD---------VVELRKRVGMVFqspnpfPKSVYENVAyAPKIHGLKDKRKLDEIVEkslRGAAlwDEVKDRLHKP 146
Cdd:NF040905 327 DVSTVSdaidaglayVTEDRKGYGLNL------IDDIKRNIT-LANLGKVSRRGVIDENEE---IKVA--EEYRKKMNIK 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 147 ATG-------LSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKK--KYTIVI 203
Cdd:NF040905 395 TPSvfqkvgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAegKGVIVI 460
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-206 |
7.03e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 49.23 E-value: 7.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKvrdlnlyygNFQALKNISLDIYKNeVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFD 81
Cdd:COG3593 3 LEKIKIK---------NFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 V-VELRKRVGMVFQS------PNPFPKSVYE-NVAYAPKIHGLKDKrkLDEIVEKSLRGAAL-----WDEVKDRLHK--- 145
Cdd:COG3593 73 IeLTFGSLLSRLLRLllkeedKEELEEALEElNEELKEALKALNEL--LSEYLKELLDGLDLelelsLDELEDLLKSlsl 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123770551 146 --------PATGLSGGQQQRLCIARALAI-------EPEVLLMDEPTSALDPISTMRIEELIQEL-KKKYTIVIVTH 206
Cdd:COG3593 151 riedgkelPLDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTH 227
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-231 |
7.37e-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: 49.75 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 37 LIGPSGCGKSTFLRTLNRMNDLIPGVRI---EGSILFDGVDIYkenFDVVELRKRVgmvfqspnPFPKSVYENvayapKI 113
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTkpaKGKLFYVPQRPY---MTLGTLRDQI--------IYPDSSEDM-----KR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 114 HGLKDKR--------KLDEIVEkslRGAAlWDEVKDRLHKpatgLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPist 185
Cdd:TIGR00954 547 RGLSDKDleqildnvQLTHILE---REGG-WSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV--- 615
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123770551 186 mRIEELIQELKKKYTIVIVThnmqqaarISDRTAFFLNGE-LIEMDR 231
Cdd:TIGR00954 616 -DVEGYMYRLCREFGITLFS--------VSHRKSLWKYHEyLLYMDG 653
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
146-217 |
8.76e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 8.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 146 PATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQAARISDR 217
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGLSDR 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-220 |
1.38e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 19 FQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDlipGVRI--EGSILFDGVDiyKENFdvvELRKRVGMVFQSP 96
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTD---GFHIgvEGVITYDGIT--PEEI---KKHYRGDVVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 97 NP--FPK-SVYENVAYAPKIHGLKDKRKLdeiVEKSLRGAALWDEVKDRL---HKPAT--------GLSGGQQQRLCIAR 162
Cdd:TIGR00956 146 TDvhFPHlTVGETLDFAARCKTPQNRPDG---VSREEYAKHIADVYMATYglsHTRNTkvgndfvrGVSGGERKRVSIAE 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 163 ALAIEPEVLLMDEPTSALDPISTMrieELIQELKkkytivivthnmqQAARISDRTAF 220
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATAL---EFIRALK-------------TSANILDTTPL 264
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-225 |
1.64e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 31 KNEVTALIGPSGCGKSTFLRTLnrMNDLIPgvRIEGSILFDGVDIykenfdvvelrkrvgmvfqspnpfpksvyenvaya 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--ARELGP--PGGGVIYIDGEDI----------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 111 pkihglkdkrkldeivekslRGAALWDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEE 190
Cdd:smart00382 42 --------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123770551 191 ------LIQELKKKYTIVIVTHNMQQ------AARISDRTAFFLNGE 225
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
103-224 |
2.05e-06 |
|
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: 48.47 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 103 VYENVAYAPKIHGLKD----------KRKLDEIVEKSLRGAALW-------DEVKDRLhkpATGLSGGQQQRLCIARALA 165
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDlltgrehlylYARLRGVPAEEIEKVANWsiqslglSLYADRL---AGTYSGGNKRKLSTAIALI 2086
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 166 IEPEVLLMDEPTSALDPIS-TMRIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFLNG 224
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQArRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
149-213 |
3.07e-06 |
|
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: 45.81 E-value: 3.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 149 GLSGGQQQRLCIARALAIE---PEVL-LMDEPTSALDPISTMRIEELIQELKKKYTIVIV-THNMQQAAR 213
Cdd:cd03227 77 QLSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIViTHLPELAEL 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-216 |
4.08e-06 |
|
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: 46.48 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKST--------------------FLRT-LNRMNDliPGV-RIEGsiLFDGVDIyKEN 79
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsaYARQfLGQMDK--PDVdSIEG--LSPAIAI-DQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 80 FDVVELRKRVGMVFQSpNPFPKSVYENVayapkihGLKdkRKLDEIVEKSLrgAALwdevkdRLHKPATGLSGGQQQRLC 159
Cdd:cd03270 86 TTSRNPRSTVGTVTEI-YDYLRLLFARV-------GIR--ERLGFLVDVGL--GYL------TLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 160 IARALAIEPEVLL--MDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHN---MQQAARISD 216
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDedtIRAADHVID 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-208 |
6.79e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 6.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123770551 142 RLHKPATGLSGGQQQRLCIARAL---AIEPEVLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNM 208
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL 892
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-216 |
1.37e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 143 LHKPATGLSGGQQQRLCIARAL---AIEPEVLLMDEPTSALdpiSTMRIEELIQELK----KKYTIVIVTHNMqQAARIS 215
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVA 878
|
.
gi 123770551 216 D 216
Cdd:PRK00635 879 D 879
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-221 |
1.55e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 136 WDEVKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMRIEELIQEL--KKKYTIVIVTHNMQQAAR 213
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDY 137
|
....*...
gi 123770551 214 ISDRTAFF 221
Cdd:cd03222 138 LSDRIHVF 145
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
3-207 |
2.33e-05 |
|
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: 44.69 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 3 SDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDV 82
Cdd:pfam13304 102 EDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 83 VELRKRvgmvfqspnpfpkSVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAALWDEVKDRLHK-PATGLSGGQQQRLCIA 161
Cdd:pfam13304 182 KELLQR-------------LVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElPAFELSDGTKRLLALL 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123770551 162 RALAI---EPEVLLMDEPTSALDPISTMRIEELIQELKKKYT-IVIVTHN 207
Cdd:pfam13304 249 AALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHS 298
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
157-223 |
3.41e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123770551 157 RLCIARALAIEPEVLLMDEPTSALDpISTMR-IEELIQElkKKYTIVIVTHnmqqaarisDRtaFFLN 223
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INTIRwLEDVLNE--RNSTMIIISH---------DR--HFLN 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
113-207 |
5.79e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 113 IHGlkdkrKLDEIVEKSL--RGAALWDEV---KDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDPISTMR 187
Cdd:PRK10636 113 IHG-----KLDAIDAWTIrsRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIW 187
|
90 100
....*....|....*....|..
gi 123770551 188 IEELIqelkKKY--TIVIVTHN 207
Cdd:PRK10636 188 LEKWL----KSYqgTLILISHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-194 |
7.89e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 2 LSDVKIKVRDLNLYYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRTlnrmndlipgvrIEGsilfdgvdiyKENFD 81
Cdd:PRK11819 320 LGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM------------ITG----------QEQPD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 82 VVELR----KRVGMVFQS-----PNpfpKSVYENVAyapkiHGLkdkrklDEI-VEKSlrgaalwdEVKDRLH------- 144
Cdd:PRK11819 378 SGTIKigetVKLAYVDQSrdaldPN---KTVWEEIS-----GGL------DIIkVGNR--------EIPSRAYvgrfnfk 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 145 -----KPATGLSGGQQQRLCIARALAIEPEVLLMDEPTSALDpISTMR-IEELIQE 194
Cdd:PRK11819 436 ggdqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-VETLRaLEEALLE 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-204 |
9.01e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 26 SLDIYKNEVTALIGPSGCGKSTFLRTLNrmNDLIPgvrIEGSILFDGVDIYKENFDvvELRKRVGMVFQSPNPFPKSVYE 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA--GELPL---LSGERQSQFSHITRLSFE--QLQKLVSDEWQRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 106 NvayapkihglkDK-RKLDEIVEKSLRGAALWDE------VKDRLHKPATGLSGGQQQRLCIARALAIEPEVLLMDEPTS 178
Cdd:PRK10938 96 D-----------DTgRTTAEIIQDEVKDPARCEQlaqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*..
gi 123770551 179 ALDPISTMRIEELIQEL-KKKYTIVIV 204
Cdd:PRK10938 165 GLDVASRQQLAELLASLhQSGITLVLV 191
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-80 |
1.13e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 1 MLSDVKIKvrdlnlyygNFQALKNISLDIykNEVTALIGPSGCGKSTF---LRTLNRM--NDLIPGVRIEG---SILFDG 72
Cdd:COG4637 1 MITRIRIK---------NFKSLRDLELPL--GPLTVLIGANGSGKSNLldaLRFLSDAarGGLQDALARRGgleELLWRG 69
|
....*...
gi 123770551 73 VDIYKENF 80
Cdd:COG4637 70 PRTITEPI 77
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-216 |
1.54e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123770551 150 LSGGQQQRLCIARALAIEPE--VLLMDEPTSALDPISTMRIEELIQELKKK-YTIVIVTHNMQQ---AARISD 216
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIID 549
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-195 |
1.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 15 YYGNFQALKNISLDIYKNEVTALIGPSGCGKSTFLRtlnrmndLIPGvriegsilfdgvdiykenfdvvELRKRVGMVFQ 94
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILK-------LISG----------------------ELQPSSGTVFR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 95 SPNpfpksVYENVAYAPKIHGLKDKRKLDEIVEKSLRGAAlwdEVKDRLH------------KPATGLSGGQQQRLCIAR 162
Cdd:PLN03073 569 SAK-----VRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVP---EQKLRAHlgsfgvtgnlalQPMYTLSGGQKSRVAFAK 640
|
170 180 190
....*....|....*....|....*....|...
gi 123770551 163 ALAIEPEVLLMDEPTSALDPIStmrIEELIQEL 195
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDA---VEALIQGL 670
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
6-207 |
2.00e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 6 KIKVRDLNLYYGNfqalKNISLDiykNEVTALIGPSGCGKSTFL------------RTLNRMNDLIPGVRIEGSILFDgv 73
Cdd:COG0419 4 RLRLENFRSYRDT----ETIDFD---DGLNLIVGPNGAGKSTILeairyalygkarSRSKLRSDLINVGSEEASVELE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 74 diYKENFDVVELRKRVGMVFQSPNPFPKSVYENVAYAPKIHGL----KDKRKLDEIVEKSLRGAALWDEVKDRLHKPATG 149
Cdd:COG0419 75 --FEHGGKRYRIERRQGEFAEFLEAKPSERKEALKRLLGLEIYeelkERLKELEEALESALEELAELQKLKQEILAQLSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123770551 150 ------LSGGQQQRLCIARALAiepevLLMDepTSALDPIstmRIEELIQELKKkytIVIVTHN 207
Cdd:COG0419 153 ldpietLSGGERLRLALADLLS-----LILD--FGSLDEE---RLERLLDALEE---LAIITHV 203
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
18-55 |
3.27e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.43 E-value: 3.27e-04
10 20 30
....*....|....*....|....*....|....*...
gi 123770551 18 NFQALKNISLDIyKNEVTALIGPSGCGKSTFLRTLNRM 55
Cdd:pfam13175 10 NFRCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIF 46
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-47 |
2.13e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 2.13e-03
10 20
....*....|....*....|....*.
gi 123770551 22 LKNISLDIYKNEVTALIGPSGCGKST 47
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
150-206 |
2.87e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 2.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123770551 150 LSGGQQQ------RLCIARALAIEPEVLLMDEPTSALDPIS-TMRIEELIQELKKKYT--IVIVTH 206
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
33-54 |
3.06e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.12 E-value: 3.06e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
34-93 |
3.31e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123770551 34 VTALIGPSGCGKSTFLRTLNRMNDLIPGVRIEGSILFDGVDIYKENFDVVELRKRVGMVF 93
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEF 60
|
|
| |
