|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-249 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 527.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYG-NIDVADL 81
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDpDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
....*...
gi 1327251791 242 GYVNGDFG 249
Cdd:COG1117 251 DYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-248 |
7.57e-166 |
|
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: 457.91 E-value: 7.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYGN-IDVADL 81
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKkIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 1327251791 242 GYVNGDF 248
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-231 |
6.13e-144 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 401.94 E-value: 6.13e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYG-NIDVADLR 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLkaHAFGLSGGQQQRLCIARTIAM 162
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRL--HALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVI 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-249 |
1.77e-131 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 371.42 E-value: 1.77e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYG-NIDVADLRIR 84
Cdd:PRK14239 8 VSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSpRTDTVDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEP 164
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTKGYV 244
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
....*
gi 1327251791 245 NGDFG 249
Cdd:PRK14239 248 SGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-249 |
8.43e-129 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 364.87 E-value: 8.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIY-GNIDVADL 81
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKkyIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFF---------LMGELVEHNETSVIF 232
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIF 247
|
250
....*....|....*..
gi 1327251791 233 SEPKDDRTKGYVNGDFG 249
Cdd:PRK14243 248 NSPQQQATRDYVSGRFG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-249 |
9.84e-101 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 293.67 E-value: 9.84e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYG-NIDVA 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKPNPFP-MSIYENVAYGLRAQG-IKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIA 157
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKD 237
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|..
gi 1327251791 238 DRTKGYVNGDFG 249
Cdd:PRK14267 242 ELTEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-246 |
3.38e-94 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 276.79 E-value: 3.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYgNIDVAD 80
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF-KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFP-MSIYENVAYGLRAQGI-KDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIAR 158
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDD 238
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*...
gi 1327251791 239 RTKGYVNG 246
Cdd:PRK14247 240 LTEKYVTG 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-244 |
6.72e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 271.53 E-value: 6.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYGN-IDVADLRIR 84
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERrVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEP 164
Cdd:PRK14258 90 VSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMED--LKKDFTIVIVTHSMQQARRISDRTAFF-----LMGELVEHNETSVIFSEPKD 237
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHD 249
|
....*..
gi 1327251791 238 DRTKGYV 244
Cdd:PRK14258 250 SRTREYV 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-246 |
2.53e-81 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 245.01 E-value: 2.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 8 NLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYGNIDVADLRIRVGM 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 88 VFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTKGYVNG 246
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-241 |
2.94e-80 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 241.05 E-value: 2.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliEGVTiKGKLDMDGTNIYGN-IDVADLRIR 84
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTITVDGEDLTDSkKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLR-AQGIKDkkyiDEVVEsslRSAALWDEV--KDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIkVKKMSK----AEAEE---RAMELLERVglADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDR 239
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
..
gi 1327251791 240 TK 241
Cdd:COG1126 232 TR 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-246 |
7.72e-78 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 235.71 E-value: 7.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNIYgNIDVADLR 82
Cdd:PRK14246 11 FNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF-QIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:PRK14246 90 KEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
....*
gi 1327251791 242 GYVNG 246
Cdd:PRK14246 250 KYVIG 254
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-241 |
3.50e-62 |
|
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: 202.83 E-value: 3.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY-----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGtniYGNIDVA 79
Cdd:COG1123 263 VRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsILFDGK-DLTK---LSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKP----NPFpMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRlkaHAFGLSGGQQQRLC 155
Cdd:COG1123 339 ELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR---YPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
....*...
gi 1327251791 234 EPKDDRTK 241
Cdd:COG1123 495 NPQHPYTR 502
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-217 |
1.36e-60 |
|
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: 190.05 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliEGVTiKGKLDMDGTNIYGN-IDVADLRIR 84
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTIIIDGLKLTDDkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLR-AQGIKDkkyiDEVVESSLRsaaLWDEVKDRLKAHAF--GLSGGQQQRLCIARTI 160
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIkVKGMSK----AEAEERALE---LLEKVGLADKADAYpaQLSGGQQQRVAIARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFF 217
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
1.74e-60 |
|
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: 188.55 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGtniygNIDVADLR 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGsILIDGEDLTDL-----EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLraqgikdkkyidevvesslrsaalwdevkdrlkahafglSGGQQQRLCIARTIA 161
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALGL---------------------------------------SGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGE 221
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-236 |
2.76e-59 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 187.15 E-value: 2.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFY-GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEGVtiKGKLDMDGTNIyGNIDVADLR 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG---LLKPT--SGEVLVDGKDI-TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQkpNP----FPMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDeVKDRlkaHAFGLSGGQQQRLCIAR 158
Cdd:COG1122 75 RKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEH-LADR---PPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF-TIVIVTHSMQQARRISDRTafFLM--GELVEHNETSVIFSEP 235
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRV--IVLddGRIVADGTPREVFSDY 225
|
.
gi 1327251791 236 K 236
Cdd:COG1122 226 E 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-225 |
1.88e-57 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 181.95 E-value: 1.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVADL--- 81
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGR------------DVTGVppe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALwDEVKDRlKAHafGLSGGQQQRLCIARTI 160
Cdd:cd03259 71 RRNIGMVFQDYALFPhLTVAENIAFGLKLRGVPKAE-IRARVRELLELVGL-EGLLNR-YPH--ELSGGQQQRVALARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 161 AMEPDVILMDEPTSALDPIAThkiEELMEDLKK-----DFTIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLR---EELREELKElqrelGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-232 |
2.14e-57 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 182.70 E-value: 2.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrMNDLIEGVtiKGKLDMDGTNIYGNIDVAD--LR 82
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPD--SGEVLIDGEDISGLSEAELyrLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPF-PMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIA 161
Cdd:cd03261 77 RRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL-RGAEDLYPAE---LSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIF 232
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-241 |
2.88e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 182.97 E-value: 2.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNIyGNIDVADL 81
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN----LLERPT-SGSVLVDGVDL-TALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RI---RVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEvvesslRSAALWDEV--KDRLKAHAFGLSGGQQQRLC 155
Cdd:COG1135 78 RAarrKIGMIFQHFNLLSsRTVAENVALPLEIAGV-PKAEIRK------RVAELLELVglSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAffLM--GELVEHNETSVI 231
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVA--VLenGRIVEQGPVLDV 228
|
250
....*....|
gi 1327251791 232 FSEPKDDRTK 241
Cdd:COG1135 229 FANPQSELTR 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
1.25e-55 |
|
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: 177.27 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGD--NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndlieGVTIKGKLDMDGTNIYGNiDVADLRI 83
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKL-SLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNP--FPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDevkdRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:cd03225 76 KVGLVFQNPDDqfFGPTVEEEVAFGLENLGLPEEE-IEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFF 217
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-237 |
2.48e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 181.06 E-value: 2.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVA 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrILLDGR------------DVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRI---RVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLC 155
Cdd:COG3842 71 GLPPekrNVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGL-EGLADR-YPHQ--LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPiathKI-EELMEDLKK-----DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETS 229
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDA----KLrEEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
....*...
gi 1327251791 230 VIFSEPKD 237
Cdd:COG3842 222 EIYERPAT 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-236 |
1.46e-54 |
|
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: 175.08 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNI--YGNIDVA 79
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIN----GLERPT-SGSVLVDGTDLtlLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKPNPF-PMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDevkdrlKAHAF--GLSGGQQQRLCI 156
Cdd:cd03258 79 KARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLED------KADAYpaQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 1327251791 235 PK 236
Cdd:cd03258 232 PQ 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-241 |
1.64e-54 |
|
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: 175.76 E-value: 1.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYG----DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYGNIDvA 79
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGeVTF------DGRPVTRRRR-K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKP----NPFpMSIYENVAYGLRAQGIKDkkyIDEVVESSLRSAALWDEVKDRlKAHAfgLSGGQQQRLC 155
Cdd:COG1124 76 AFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPD---REERIAELLEQVGLPPSFLDR-YPHQ--LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
....*...
gi 1327251791 234 EPKDDRTK 241
Cdd:COG1124 229 GPKHPYTR 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-213 |
4.92e-54 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 174.89 E-value: 4.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVA 79
Cdd:COG1116 9 ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGeVLVDGK------------PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIAR 158
Cdd:COG1116 77 GPGPDRGVVFQEPALLPwLTVLDNVALGLELRGV-PKAERRERARELLELVGL----AGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDR 213
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADR 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-225 |
6.30e-54 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 173.63 E-value: 6.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEgvTIKGKLDMDGTNIYGNIDVA--DLRI 83
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLR--PDSGEILVDGQDITGLSEKElyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPF-PMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAhafGLSGGQQQRLCIARTIAM 162
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPS---ELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-241 |
1.01e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 173.36 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 8 NLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDlIEGvtikGKLDMDGTNIYG-NIDVADLRIRVG 86
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE-ITS----GDLIVDGLKVNDpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 87 MVFQKPNPFP-MSIYENVAYG-LRAQGIKDKkyidevvESSLRSAALWDEVKDRLKAHAFG--LSGGQQQRLCIARTIAM 162
Cdd:PRK09493 81 MVFQQFYLFPhLTALENVMFGpLRVRGASKE-------EAEKQARELLAKVGLAERAHHYPseLSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-222 |
1.41e-52 |
|
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: 169.59 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNIYGNIDVADL 81
Cdd:cd03255 3 LKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLDRPT-SGEVRVDGTDISKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIR---VGMVFQKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIA 157
Cdd:cd03255 78 AFRrrhIGFVFQSFNLLPdLTALENVELPLLLAGVP-KKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGEL 222
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-226 |
1.74e-52 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 169.61 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIegvtiKGKLDMDGTNIYGNiDVADL 81
Cdd:cd03257 4 VKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKL-SRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIR---VGMVFQKP----NPFpMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEvkDRLKAHAFGLSGGQQQRL 154
Cdd:cd03257 78 KIRrkeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE--EVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHN 226
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-213 |
2.69e-52 |
|
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: 168.80 E-value: 2.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ----ALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVtIK---GKLDMDGTniygniDV 78
Cdd:cd03293 3 VRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLR-------IIAGL-ERptsGEVLVDGE------PV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIA 157
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAE-ARERAEELLELVGL----SGFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDR 213
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADR 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
6.69e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 6.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLdmdgtniYGNIDVADLR 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDGKP-------LSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGLRaqgIKDKKYIDEVVESSLRSAALWDEVKDRlKAHAfgLSGGQQQRLCIARTIAM 162
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDILDK-PVER--LSGGERQRLALIRALLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRT 214
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRV 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-236 |
8.07e-52 |
|
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: 175.86 E-value: 8.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY--GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndLIEGVTIKGKLDMDGTNIYGnIDVADLR 82
Cdd:COG1123 6 EVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLE-LSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKP--NPFPMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-242 |
1.78e-51 |
|
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: 168.78 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN-----QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTI--KGKLDMDGTNIY--GNI 76
Cdd:TIGR04521 3 LKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN-------GLLKptSGTVTIDGRDITakKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLRIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDEVKDRlkaHAFGLSGGQQQRL 154
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEEE-AEERVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIF 232
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
250
....*....|
gi 1327251791 233 SEPKDDRTKG 242
Cdd:TIGR04521 232 SDVDELEKIG 241
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-245 |
1.79e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 165.31 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYGNID--V 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNPFP-MSIYENVAYGlraQGIKDKKYIDEVVEsslRSAALWDEVKDRLKAHAFG--LSGGQQQRLC 155
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPhRTVLENIIEG---PVIVKGEPKEEATA---RARELLAKVGLAGKETSYPrrLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDP------IAThkIEELMEDLKkdfTIVIVTHSMQQARRISDRTAFFLMGELVEHNETS 229
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPelvgevLNT--IRQLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*.
gi 1327251791 230 VIFSEPKDDRTKGYVN 245
Cdd:PRK11264 230 ALFADPQQPRTRQFLE 245
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-238 |
2.58e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 166.42 E-value: 2.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYgNIDVADLRI 83
Cdd:COG1125 4 FENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGrILI------DGEDIR-DLDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAQGiKDKKYIDEVVESSLRSAALW-DEVKDRLKAHafgLSGGQQQRLCIARTIA 161
Cdd:COG1125 77 RIGYVIQQIGLFPhMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDpEEYRDRYPHE---LSGGQQQRVGVARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKI-EELM---EDLKKdfTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKD 237
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLqDELLrlqRELGK--TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAN 230
|
.
gi 1327251791 238 D 238
Cdd:COG1125 231 D 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-224 |
5.75e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 163.29 E-value: 5.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNIYG--NIDVA 79
Cdd:COG1136 7 LRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG----GLDRPT-SGEVLIDGQDISSlsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIR-VGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKkyidevvESSLRSAALWDEV--KDRLKAHAFGLSGGQQQRLC 155
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPeLTALENVALPLLLAGVSRK-------ERRERARELLERVglGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGELVE 224
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-245 |
6.79e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 6.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEgVTIKGKLDM-----DGTNIYGNIDVAD 80
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLE-MPRSGTLNIagnhfDFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFP-MSIYEN-VAYGLRAQGIKDKKYIDEVVE--SSLRSAalwdEVKDRLKAHafgLSGGQQQRLCI 156
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNlIEAPCRVLGLSKDQALARAEKllERLRLK----PYADRFPLH---LSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSViFSEP 235
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQP 231
|
250
....*....|
gi 1327251791 236 KDDRTKGYVN 245
Cdd:PRK11124 232 QTEAFKNYLS 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-213 |
1.33e-49 |
|
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: 163.29 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADLRIR 84
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLL------DGRDL-ASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPN-PFPMSIYENVAYG-------LRAQGIKDkkyiDEVVESSLRSAALWDevkdrLKAHAFG-LSGGQQQRLC 155
Cdd:COG1120 77 IAYVPQEPPaPFGLTVRELVALGryphlglFGRPSAED----REAVEEALERTGLEH-----LADRPVDeLSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPiaTHKIE--ELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDL--AHQLEvlELLRRLARERgrTVVMVLHDLNLAARYADR 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-247 |
9.29e-49 |
|
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: 160.54 E-value: 9.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEgvTIKGKLDMDGTNIyGNIDVADLRIR 84
Cdd:cd03295 3 FENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINR---LIE--PTSGEIFIDGEDI-REQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVESsLRSAALWD-EVKDRLKAHafgLSGGQQQRLCIARTIAM 162
Cdd:cd03295 77 IGYVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADEL-LALVGLDPaEFADRYPHE---LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRT 240
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFV 232
|
....*..
gi 1327251791 241 KGYVNGD 247
Cdd:cd03295 233 AEFVGAD 239
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-245 |
1.04e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYGNIDVADLRIRV 85
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPNPFP-MSIYEN-VAYGLRAQGIKDKKYIDEVVE--SSLRsaalWDEVKDRLKAHafgLSGGQQQRLCIARTIA 161
Cdd:COG4161 85 GMVFQQYNLWPhLTVMENlIEAPCKVLGLSKEQAREKAMKllARLR----LTDKADRFPLH---LSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSvIFSEPKDDRT 240
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQTEAF 236
|
....*
gi 1327251791 241 KGYVN 245
Cdd:COG4161 237 AHYLS 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-236 |
2.41e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 162.62 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndlIEGVTI--KGKLDMDGTNIYGNIDVADlR 82
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRI-------IAGLETpdSGRIVLNGRDLFTNLPPRE-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 iRVGMVFQKPNPFP-MSIYENVAYGLRAQGiKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIA 161
Cdd:COG1118 76 -RVGFVFQHYALFPhMTVAENIAFGLRVRP-PSKAEIRARVEELLELVQL-EGLADRYPSQ---LSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAffLM--GELVEHNETSVIFSEPK 236
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVV--VMnqGRIEQVGTPDEVYDRPA 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-213 |
4.07e-48 |
|
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: 158.89 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN-QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdGTNIYGNIDVADLRI 83
Cdd:cd03256 3 VENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGsVLIDGT----DINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAQgikdkkyidevvESSLRSAALWDEVKDRLKA-----------HAFG----LS 147
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGR------------RSTWRSLFGLFPKEEKQRAlaalervglldKAYQradqLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 148 GGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDR 213
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-213 |
5.22e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.07 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDL-FYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIYGNI--DVADLR 82
Cdd:COG3638 5 LRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSG-----EILVDGQDVTALRgrALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQgikdkkyidevvESSLRSAA-LWDEvKDRLKAHA----FG----------- 145
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLAGRLGR------------TSTWRSLLgLFPP-EDRERALEalerVGladkayqradq 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIeelMEDLKK-----DFTIVIVTHSMQQARRISDR 213
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQV---MDLLRRiaredGITVVVNLHQVDLARRYADR 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-215 |
8.56e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 161.39 E-value: 8.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtIKGKLDMDGTNIY-GNIDVA 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRM------------IAGLEDPTSGEILiGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIR---VGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLC 155
Cdd:COG3839 69 DLPPKdrnIAMVFQSYALYPhMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGL-EDLLDR-KPKQ--LSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPiathKI-EELMEDLKK-----DFTIVIVTHSMQQARRISDRTA 215
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDA----KLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIA 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-210 |
8.63e-48 |
|
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: 155.62 E-value: 8.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN--QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYgNIDVADLR 82
Cdd:cd03228 3 FKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGeILI------DGVDLR-DLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVayglraqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIAM 162
Cdd:cd03228 76 KNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH---SMQQARRI 210
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHrlsTIRDADRI 164
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-239 |
1.45e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 158.04 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMND------LIEGVTIKGKLDMDGtniygNIDVA 79
Cdd:COG4598 11 VRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETpdsgeiRVGGEEIRLKPDRDG-----ELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 D------LRIRVGMVFQKPNPFP-MSIYENVAYG-LRAQGIkDKKYIDEVVESSLRSAALWDeVKDRLKAHafgLSGGQQ 151
Cdd:COG4598 86 DrrqlqrIRTRLGMVFQSFNLWShMTVLENVIEApVHVLGR-PKAEAIERAEALLAKVGLAD-KRDAYPAH---LSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 152 QRLCIARTIAMEPDVILMDEPTSALDPiathkieEL-------MEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDP-------ELvgevlkvMRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
250
....*....|....*.
gi 1327251791 224 EHNETSVIFSEPKDDR 239
Cdd:COG4598 234 EQGPPAEVFGNPKSER 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-243 |
3.32e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.79 E-value: 3.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVADLRI 83
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGK------------PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPN---PFPMSIYENVAYGLRAQ-------GIKDKKYIDEVvessLRSAALWDevkdrLKAHAFG-LSGGQQQ 152
Cdd:COG1121 76 RIGYVPQRAEvdwDFPITVRDVVLMGRYGRrglfrrpSRADREAVDEA----LERVGLED-----LADRPIGeLSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRTAfFLMGELVEHNETSVI 231
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEV 225
|
250
....*....|..
gi 1327251791 232 FSEPKDDRTKGY 243
Cdd:COG1121 226 LTPENLSRAYGG 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-225 |
6.14e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.61 E-value: 6.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndliEGVTI--KGKLDMDGTNIYGniDVADLRI 83
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML-------LGLLRptSGEVRVLGEDVAR--DPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDEVKDRLKahafGLSGGQQQRLCIARTIAM 162
Cdd:COG1131 74 RIGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDF-TIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGkTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-241 |
3.05e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 157.27 E-value: 3.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIkgkldMDGTNIyGNIDVADLRI---RVGMVFQKPN 93
Cdd:PRK11153 19 HALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-----VDGQDL-TALSEKELRKarrQIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 PfpMS---IYENVAYGLRAQGiKDKKYIDEVVESSLRSAALWDevkdrlKAHAF--GLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:PRK11153 93 L--LSsrtVFDNVALPLELAG-TPKAEIKARVTELLELVGLSD------KADRYpaQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 169 MDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-236 |
6.85e-46 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 155.60 E-value: 6.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrMNDLIEGVTIKGKLDMDGTNIYGnIDVAD 80
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLLK-LSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LR-IR---VGMVFQKP----NPFpMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHAFGLSGGQQQ 152
Cdd:COG0444 80 LRkIRgreIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSV 230
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*.
gi 1327251791 231 IFSEPK 236
Cdd:COG0444 238 LFENPR 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-238 |
1.97e-44 |
|
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: 149.31 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIygnIDVADLR 82
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLR-------LIAGFETptSGEILLDGKDI---TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIARTIA 161
Cdd:cd03300 72 RPVNTVFQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL-EGYANR-KPSQ--LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALD-PIATHKIEELMEdLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDD 238
Cdd:cd03300 147 NEPKVLLLDEPLGALDlKLRKDMQLELKR-LQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-246 |
2.82e-44 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 149.73 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIY------GN 75
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEG-----SIVVNGQTINlvrdkdGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 76 IDVAD------LRIRVGMVFQKPNPFP-MSIYENV------AYGLRAQGIKDK--KYIDEVvesslrsaALWDEVKDRLK 140
Cdd:PRK10619 79 LKVADknqlrlLRTRLTMVFQHFNLWShMTVLENVmeapiqVLGLSKQEARERavKYLAKV--------GIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 141 AHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLM 219
Cdd:PRK10619 151 VH---LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
250 260
....*....|....*....|....*..
gi 1327251791 220 GELVEHNETSVIFSEPKDDRTKGYVNG 246
Cdd:PRK10619 228 GKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-227 |
7.13e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 7.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYgNIDVADLRIRVGMVFQKP 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILI------DGVDIR-DLTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSIYENVAYGlraqgikDKKYIDEVVESSLRSAALWDEVkDRLKAhafG-----------LSGGQQQRLCIARTIA 161
Cdd:COG1132 424 FLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFI-EALPD---GydtvvgergvnLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE---HNE 227
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEqgtHEE 560
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-224 |
1.73e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 146.35 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliEGVTiKGKLDMDGTNIyGNI---DVADL 81
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE----ERPT-SGQVLVNGQDL-SRLkrrEIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQK----PNpfpMSIYENVAYGLRAQGiKDKKYIDEVVESSLRSAALWDevkdrlKAHAF--GLSGGQQQRLC 155
Cdd:COG2884 78 RRRIGVVFQDfrllPD---RTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSD------KAKALphELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFFLMGELVE 224
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-225 |
2.58e-43 |
|
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: 155.38 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADLR 82
Cdd:COG2274 476 LENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrILI------DGIDL-RQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGlraqgikDKKYIDEVVESSLRSAALWDEVKD-------RLKAHAFGLSGGQQQRLC 155
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTafFLM--GELVEH 225
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL-ADRI--IVLdkGRIVED 690
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-231 |
5.52e-43 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.77 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRM--NDliegvtiKGKLDMDGTNIygNIDVADLRI 83
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlkPD-------SGSILIDGEDV--RKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDEVKDRLKahafGLSGGQQQRLCIARTIAM 162
Cdd:COG4555 75 QIGVLPDERGLYDrLTVRENIRYFAELYGLFDEE-LKKRIEELIELLGLEEFLDRRVG----ELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVI 231
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-246 |
8.16e-43 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 146.25 E-value: 8.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEgvTIKGKLDMDGTNIyGNIDVADL----RIRVGMVFQKPN 93
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIE--PTSGKVLIDGQDI-AAMSRKELrelrRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 PFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEP 172
Cdd:cd03294 113 LLPhRTVLENVAFGLEVQGV-PRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 173 TSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTKGYVNG 246
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-221 |
2.00e-42 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 141.61 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIyGNIDVADLRIRV 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG-----EILIDGKDI-AKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQkpnpfpmsiyenvayglraqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIAMEPD 165
Cdd:cd00267 76 GYVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFFLMGE 221
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
2.21e-42 |
|
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: 143.73 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNiygnidvADLRI 83
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGR-DITGLP-------PHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 R--VGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKY-IDEVVEsslrsaaLWDEVKDRLKAHAFGLSGGQQQRLCIART 159
Cdd:cd03224 74 RagIGYVPEGRRIFPeLTVEENLLLGAYARRRAKRKArLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-246 |
5.92e-42 |
|
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: 146.54 E-value: 5.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEgvTIKGKLDMDGTNIyGNIDVADLRI----RVGMVF 89
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIE--PTAGQIFIDGENI-MKQSPVELREvrrkKIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVESsLRSAALwDEVKDRlkaHAFGLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:TIGR01186 78 QQFALFPhMTILQNTSLGPELLGWPEQERKEKALEL-LKLVGL-EEYEHR---YPDELSGGMQQRVGLARALAAEPDILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 169 MDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTKGYVNG 246
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-224 |
7.06e-42 |
|
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: 149.91 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADLR 82
Cdd:COG4988 338 ELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsILI------NGVDL-SDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGLRAQGikdkkyiDEVVESSLRSAALWDEVKD-------RLKAHAFGLSGGQQQRLC 155
Cdd:COG4988 411 RQIAWVPQNPYLFAGTIRENLRLGRPDAS-------DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE 224
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-174 |
7.35e-42 |
|
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: 140.09 E-value: 7.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGtniygnIDVADLRIRVGMVFQKPNPFP- 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtILLDGQ-DLTD------DERKSLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 97 MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:pfam00005 74 LTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-223 |
1.11e-41 |
|
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: 142.44 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN-QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmDGTNIYGNiDVADLRI 83
Cdd:TIGR02315 4 VENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsILLEGT---DITKLRGK-KLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRA-----QGI------KDKkyidEVVESSLRSAALWDEVKDRLKAhafgLSGGQQ 151
Cdd:TIGR02315 80 RIGMIFQHYNLIErLTVLENVLHGRLGykptwRSLlgrfseEDK----ERALSALERVGLADKAYQRADQ----LSGGQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 152 QRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
34-244 |
4.95e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 144.48 E-value: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLLRCLNRmndLIEgVTiKGKLDMDGTNIyGNIDVADLR-IR---VGMVFQKPNPFP-MSIYENVAYGLR 108
Cdd:COG4175 58 IMGLSGSGKSTLVRCLNR---LIE-PT-AGEVLIDGEDI-TKLSKKELReLRrkkMSMVFQHFALLPhRTVLENVAFGLE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 109 AQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDP-IATHKIEEL 187
Cdd:COG4175 132 IQGV-PKAERRERAREALELVGL-AGWEDS-YPDE--LSGGMQQRVGLARALATDPDILLMDEAFSALDPlIRREMQDEL 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 188 ME---DLKKdfTIVIVTHSMQQARRISDRTAffLM--GELVEHNETSVIFSEPKDDrtkgYV 244
Cdd:COG4175 207 LElqaKLKK--TIVFITHDLDEALRLGDRIA--IMkdGRIVQIGTPEEILTNPAND----YV 260
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-227 |
1.30e-40 |
|
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: 139.60 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIkgkldMDGTNIyGNIDVADLRIRVGMVFQKPNP 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIL-----LDGVDI-RDLNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYENVAYGlraqgikDKKYIDEVVESSLRSAALWDEVKD-------RLKAHAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:cd03249 89 FDGTIAENIRYG-------KPDATDEEVEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE---HNE 227
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEqgtHDE 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-239 |
1.67e-40 |
|
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: 139.39 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQaLKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndlIEG--VTIKGKLDMDGTniygniDVADL- 81
Cdd:cd03299 2 KVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLET-------IAGfiKPDSGKILLNGK------DITNLp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 --RIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIAR 158
Cdd:cd03299 68 peKRDISYVPQNYALFPhMTVYKNIAYGLKKRKV-DKKEIERKVLEIAEMLGI-DHLLNRKPET---LSGGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
...
gi 1327251791 237 DDR 239
Cdd:cd03299 223 NEF 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-213 |
4.82e-40 |
|
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: 138.24 E-value: 4.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTikgKLDmDGTNIYGNIDVADLRIR- 84
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR-------LIAGLE---RPD-SGTILFGGEDATDVPVQe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 --VGMVFQKPNPFP-MSIYENVAYGLRAQGIK---DKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIAR 158
Cdd:cd03296 74 rnVGFVFQHYALFRhMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQL-DWLADRYPAQ---LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 159 TIAMEPDVILMDEPTSALDPiathKI-EELMEDLKK-----DFTIVIVTHSMQQARRISDR 213
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDA----KVrKELRRWLRRlhdelHVTTVFVTHDQEEALEVADR 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-216 |
5.44e-40 |
|
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: 135.99 E-value: 5.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTI--KGKLDMDGTNIygNIDVADLRI 83
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-------GLLKpdSGEIKVLGKDI--KKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYglraqgikdkkyidevvesslrsaalwdevkdrlkahafglSGGQQQRLCIARTIAM 162
Cdd:cd03230 74 RIGYLPEEPSLYEnLTVRENLKL-----------------------------------------SGGMKQRLALAQALLH 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDF-TIVIVTHSMQQARRISDRTAF 216
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAI 167
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-236 |
5.92e-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: 140.32 E-value: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIygnIDVADLRIRVGMVFQKPNPFP-MSIYENVAYGLRAQGI 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSG-----SIMLDGEDV---TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 113 kDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDpiatHKIEELMEDLK 192
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLVQL----EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQLEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 193 KDF------TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:TIGR01187 144 KTIqeqlgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
33-236 |
6.87e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.25 E-value: 6.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRCLNRmndLIEgVTiKGKLDMDGTNIYG--NIDVADLRIRVGMVFQKP----NPfPMSIYENVAYG 106
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLR---LEE-PT-SGEILFDGQDITGlsGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 107 LRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLkAHAFglSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEE 186
Cdd:COG4608 122 LRIHGLASKAERRERVAELLELVGLRPEHADRY-PHEF--SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLN 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 187 LMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:COG4608 199 LLEDLQDELglTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-215 |
2.92e-39 |
|
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: 135.46 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKLDMDGTNIY-GNIDVADLRIR 84
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLR------------MIAGLEEPTSGRIYiGGRDVTDLPPK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 ---VGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIARTI 160
Cdd:cd03301 71 drdIAMVFQNYALYPhMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQI-EHLLDR-KPKQ--LSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 161 AMEPDVILMDEPTSALDPiathKI-EELMEDLKK-----DFTIVIVTHSMQQARRISDRTA 215
Cdd:cd03301 146 VREPKVFLMDEPLSNLDA----KLrVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIA 202
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-234 |
3.14e-39 |
|
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: 136.79 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY--GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNIYgnidvaDLR 82
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkVTVDGLDTLDEENLW------EIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKP-NPFPMSIYEN-VAYGLRAQGIKDKKyIDEVVESSLRSAALWDeVKDRLKAHafgLSGGQQQRLCIARTI 160
Cdd:TIGR04520 77 KKVGMVFQNPdNQFVGATVEDdVAFGLENLGVPREE-MRKRVDEALKLVGMED-FRDREPHL---LSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGELVEHNETSVIFSE 234
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-213 |
3.57e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.79 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGD-NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIYgnidva 79
Cdd:PRK13647 3 NIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGR-EVNAENEK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDeVKDRLKAHafgLSGGQQQRLCIA 157
Cdd:PRK13647 76 WVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWD-FRDKPPYH---LSYGQKKRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQ 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-223 |
4.59e-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: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRClnrmndlIEGVT--IKGKLDMDGTNIYG---NIDVADLRIRVGMVFQKPNPFP-MSIYENV 103
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRC-------IAGLEkpDGGTIVLNGTVLFDsrkKINLPPQQRKIGLVFQQYALFPhLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 104 AYGLR-AQGIKDKKYIDEVVESslrsAALwDEVKDRlkaHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATH 182
Cdd:cd03297 97 AFGLKrKRNREDRISVDELLDL----LGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 183 KIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03297 169 QLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-213 |
5.15e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.72 E-value: 5.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN-----QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmnDLIEgvTIKGKLDMDGTNIYG-NIDVA 79
Cdd:PRK13637 5 IENLTHIYMEGtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLLK--PTSGKIIIDGVDITDkKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKP--NPFPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAAL-WDEVKDRlkaHAFGLSGGQQQRLCI 156
Cdd:PRK13637 80 DIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEE-IENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADR 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-202 |
7.23e-39 |
|
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: 133.70 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 12 FYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGV--TIKGKLDMDGTNI-YGNIDVADLRIRVGMV 88
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN-------GLlrPQSGAVLIDGEPLdYSRKGLLERRQRVGLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 89 FQKPNP--FPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDV 166
Cdd:TIGR01166 74 FQDPDDqlFAADVDQDVAFGPLNLGLSEAE-VERRVREALTAVGA-SGLRERPTHC---LSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327251791 167 ILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTH 202
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-223 |
2.06e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 132.17 E-value: 2.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvTIKgkldMDGTNIyGNIDVADLRIR 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG-EIL----LDGKDL-ASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQkpnpfpmsiyenvayGLRAQGIKDK--KYIDEvvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIAM 162
Cdd:cd03214 75 IAYVPQ---------------ALELLGLAHLadRPFNE-------------------------LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 163 EPDVILMDEPTSALDPiaTHKIE--ELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03214 115 EPPILLLDEPTSHLDI--AHQIEllELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-243 |
4.10e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.96 E-value: 4.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDnqALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEG--VTIKGKLDMDGTniygniDVADLRI 83
Cdd:COG3840 4 LDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLL-------NLIAGflPPDSGRILWNGQ------DLTALPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 --R-VGMVFQKPNPFP-MSIYENVAYGLRAqGIK----DKKYIDEVvessLRSAALwDEVKDRLKAHafgLSGGQQQRLC 155
Cdd:COG3840 69 aeRpVSMLFQENNLFPhLTVAQNIGLGLRP-GLKltaeQRAQVEQA----LERVGL-AGLLDRLPGQ---LSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|
gi 1327251791 234 EPKDDRTKGY 243
Cdd:COG3840 220 GEPPPALAAY 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-215 |
4.92e-38 |
|
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: 132.27 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVADLRIR 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsIRVFGK------------PLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPN---PFPMSIYENVAYGLRAQGI-------KDKKYIDEVVESSLRSaalwdEVKDRLKAHafgLSGGQQQRL 154
Cdd:cd03235 70 IGYVPQRRSidrDFPISVRDVVLMGLYGHKGlfrrlskADKAKVDEALERVGLS-----ELADRQIGE---LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTA 215
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-213 |
1.75e-37 |
|
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: 131.41 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVTI--KGKLDMDGTNIYGniDVADLR 82
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-------NLISGFLRptSGSVLFDGEDITG--LPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMV--FQKPNPFP-MSIYENVAYGLRAQ---GIKDKKYIDEVVESSLRSAALWDEVK--DRLKAHAFGLSGGQQQRL 154
Cdd:cd03219 73 ARLGIGrtFQIPRLFPeLTVLENVMVAAQARtgsGLLLARARREEREARERAEELLERVGlaDLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDR 213
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADR 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-237 |
3.04e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.75 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNiygNIDVADLRIRVGMVFQKPNP-- 94
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtVTIGERVITAGKK---NKKLKPLRKKVGIVFQFPEHql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYENVAYGLRAQGIKD---KKYIDEVVESslrsAALWDEVKDRlkaHAFGLSGGQQQRLCIARTIAMEPDVILMDE 171
Cdd:PRK13634 99 FEETVEKDICFGPMNFGVSEedaKQKAREMIEL----VGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 172 PTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKD 237
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-241 |
3.14e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.04 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKS----TLLRCLNRmndliEGVTIKGKLDMDGTNIYGnI 76
Cdd:COG4172 8 SVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD-----PAAHPSGSILFDGQDLLG-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLR-IR---VGMVFQKP----NPFpMSIYENVAYGLRA-QGIKDKkyidevvESSLRSAALWDEV-----KDRLKAH 142
Cdd:COG4172 82 SERELRrIRgnrIAMIFQEPmtslNPL-HTIGKQIAEVLRLhRGLSGA-------AARARALELLERVgipdpERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 143 AFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAffLM- 219
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVA--VMr 231
|
250 260
....*....|....*....|...
gi 1327251791 220 -GELVEHNETSVIFSEPKDDRTK 241
Cdd:COG4172 232 qGEIVEQGPTAELFAAPQHPYTR 254
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-215 |
4.43e-36 |
|
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: 130.93 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtIKGKLDMDGTNIY-GNIDVADL--- 81
Cdd:TIGR03265 7 IDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRI------------IAGLERQTAGTIYqGGRDITRLppq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTI 160
Cdd:TIGR03265 75 KRDYGIVFQSYALFPnLTVADNIAYGLKNRGM-GRAEVAERVAELLDLVGL-PGSERKYPGQ---LSGGQQQRVALARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTA 215
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLgvTTIMVTHDQEEALSMADRIV 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-213 |
6.53e-36 |
|
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: 127.41 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNiygnidvADLRI 83
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGE-DITGLP-------PHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVF--QKPNPFP-MSIYENVAYGLRAQgiKDKKYIDEVVEsslRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:COG0410 77 RLGIGYvpEGRRIFPsLTVEENLLLGAYAR--RDRAEVRADLE---RVYELFPRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-223 |
1.35e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 126.08 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMDGTNIY--GNIDVADL---RIRVGMV 88
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT------------GELRPTSGTAYinGYSIRTDRkaaRQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 89 FQKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALwDEVKDRLkahAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:cd03263 81 PQFDALFDeLTVREHLRFYARLKGLP-KSEIKEEVELLLRVLGL-TDKANKR---ARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-214 |
2.21e-35 |
|
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: 125.44 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY-GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLdmdgTNIYGNIDVADLR 82
Cdd:TIGR02673 3 EFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGqVRIAGED----VNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:TIGR02673 79 RRIGVVFQDFRLLPdRTVYENVALPLEVRGKK-EREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRT 214
Cdd:TIGR02673 154 NSPPLLLADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVAHRV 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-209 |
2.60e-35 |
|
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: 131.64 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGD-NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGtniygnIDVADLRIR 84
Cdd:TIGR02857 324 FSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD------ADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGLRAQGikdkkyiDEVVESSLRSAALWDEVKDRLKAHAF-------GLSGGQQQRLCIA 157
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDAS-------DAEIREALERAGLDEFVAALPQGLDTpigeggaGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARR 209
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-241 |
4.01e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 130.96 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEGvtiKGKLDMDGTNIYGnIDVADLRI---RVGMVFQKP-- 92
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPS---EGEIRFDGQDLDG-LSRRALRPlrrRMQVVFQDPfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 --NPfPMSIYENVAYGLRAQGIK-DKKYIDEVVESSLRSAALWDEVKDRLkAHAFglSGGQQQRLCIARTIAMEPDVILM 169
Cdd:COG4172 374 slSP-RMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHRY-PHEF--SGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 170 DEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-223 |
7.75e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.36 E-value: 7.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFY-GDNQ---ALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVT--IKGKLDMDGTNIYG 74
Cdd:COG4525 1 MSMLTVRHVSVRYpGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLL-------NLIAGFLapSSGEITLDGVPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 75 niDVADlriRvGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDEVKDRLkahaFGLSGGQQQR 153
Cdd:COG4525 74 --PGAD---R-GVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLALVGLADFARRRI----WQLSGGMRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 154 LCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQarrisdrtAFFLMGELV 223
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEE--------ALFLATRLV 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-213 |
8.63e-35 |
|
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: 127.52 E-value: 8.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 22 INLPIPTRQVTALIGPSGCGKSTLLRC---LNRmndLIEG-VTIKGKLDMDGTNiygNIDVADLRIRVGMVFQKPNPFP- 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGrIRLGGEVLQDSAR---GIFLPPHRRRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYENVAYGL-RAQGIKDKKYIDEVVESsLRSAALwdevkdrLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:COG4148 92 LSVRGNLLYGRkRAPRAERRISFDEVVEL-LGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327251791 176 LDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDR 213
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADH 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-223 |
1.11e-34 |
|
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: 123.63 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGtniygniDVADLRIR 84
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-------EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWdEVKDRLkAHAFglSGGQQQRLCIARTIAME 163
Cdd:cd03265 75 IGIVFQDLSVDDeLTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLL-EAADRL-VKTY--SGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-236 |
1.48e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTikgKLDmDGTNIYGNIDVADL---RIRVGMVF 89
Cdd:PRK09452 24 FDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIAGFE---TPD-SGRIMLDGQDITHVpaeNRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:PRK09452 93 QSYALFPhMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQL-EEFAQR-KPHQ--LSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 169 MDEPTSALDpiatHKIEELME-DLKK-----DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:PRK09452 168 LDESLSALD----YKLRKQMQnELKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-213 |
2.50e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.97 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTIK--GKLDMDGTniygniDVADLR 82
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLEHQtsGHIRFHGT------DVSRLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IR---VGMVFQKPNPFP-MSIYENVAYGLRA---QGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLC 155
Cdd:PRK10851 71 ARdrkVGFVFQHYALFRhMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQ---LSGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDpiATHKIE------ELMEDLKkdFTIVIVTHSMQQARRISDR 213
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEELK--FTSVFVTHDQEEAMEVADR 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-224 |
4.13e-34 |
|
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: 128.73 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYgNIDVADLR 82
Cdd:COG4987 336 LEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsITL------GGVDLR-DLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGlrAQGIKDkkyiDEVVESsLRSAALWDEVKD-------RLKAHAFGLSGGQQQRLC 155
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLRLA--RPDATD----EELWAA-LERVGLGDWLAAlpdgldtWLGEGGRRLSGGERRRLA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRIsDRTAFFLMGELVE 224
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-213 |
5.00e-34 |
|
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: 122.84 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygniDVADL-- 81
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGrILFDGR------------DITGLpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 --RIRVGMV--FQKPNPFP-MSIYENVA--------YGLRAQGIKDKKYIDEVVESSLRSAALWDEVK--DRLKAHAFGL 146
Cdd:COG0411 74 hrIARLGIArtFQNPRLFPeLTVLENVLvaaharlgRGLLAALLRLPRARREEREARERAEELLERVGlaDRADEPAGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 147 SGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADR 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-214 |
8.78e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygNIDVADLR 82
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGK----------PIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNP--FPMSIYENVAYGLRAqgiKDKKYidEVVESSLRSAALWDEvKDRlkaHAFGLSGGQQQRLCIARTI 160
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKE---LDAGN--EQAETVLKDLDLYAL-KER---HPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRT 214
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-225 |
1.85e-33 |
|
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: 120.38 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTrQVTALIGPSGCGKSTLLRclnrmndLIEGVT--IKGKLDMDGTNIYGNIDvaDLR 82
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMR-------ILATLTppSSGTIRIDGQDVLKQPQ--KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIA 161
Cdd:cd03264 72 RRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-202 |
4.13e-33 |
|
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: 120.03 E-value: 4.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFYGDN-QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADLRIR 84
Cdd:cd03253 4 ENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGsILI------DGQDI-REVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGlraqgiKDKKYIDEVVEsslrsAALWDEVKDRLKAHAFG-----------LSGGQQQR 153
Cdd:cd03253 77 IGVVPQDTVLFNDTIGYNIRYG------RPDATDEEVIE-----AAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327251791 154 LCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-225 |
6.41e-33 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 119.64 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGD--NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIYGnIDVADLR 82
Cdd:cd03251 2 EFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSG-----RILIDGHDVRD-YTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGLRAQGikdkkyiDEVVESSLRSAALWDEVKD-------RLKAHAFGLSGGQQQRLC 155
Cdd:cd03251 76 RQIGLVSQDVFLFNDTVAENIAYGRPGAT-------REEVEEAARAANAHEFIMElpegydtVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH---SMQQARRIsdrtafFLM--GELVEH 225
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHrlsTIENADRI------VVLedGKIVER 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-212 |
8.13e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.14 E-value: 8.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVT--IKGKLDMDGTniygniDVADLRIR---VGM 87
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGE------DVTHRSIQqrdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 88 VFQKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDV 166
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGLKMLGVP-KEERKQRVKEALELVDL-AGFEDRYVDQ---ISGGQQQRVALARALILKPKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327251791 167 ILMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISD 212
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSD 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
9.99e-33 |
|
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: 118.87 E-value: 9.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY-GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIYGnIDVADLRI 83
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDIRD-ISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFPMSIYENVAYG-LRAQgikdkkyiDEVVESSLRSAALWDEVKDR-------LKAHAFGLSGGQQQRLC 155
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLGrPNAT--------DEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVEH 225
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEE 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-234 |
1.36e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.35 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNdliegVTIKGKLDMDGTNIyGNIDVADLRIRV 85
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-----TPQSGTVFLGDKPI-SMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQK-PNPFPMSIYENVAYGlRAQ--------GIKDKKYIDEVVESSLRsaalwDEVKDRLKAHafgLSGGQQQRLCI 156
Cdd:PRK11231 79 ALLPQHhLTPEGITVRELVAYG-RSPwlslwgrlSAEDNARVNQAMEQTRI-----NHLADRRLTD---LSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDpiATHKIE--ELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD--INHQVElmRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
.
gi 1327251791 234 E 234
Cdd:PRK11231 228 P 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
1.39e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.80 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYG---DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnRMNDLIEgvTIKGKLDMDGTNI-YGNIDVADL 81
Cdd:PRK13639 2 LETRDLKYSypdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFL---HFNGILK--PTSGEVLIKGEPIkYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwdEVKDRLKAHAfgLSGGQQQRLCIART 159
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGM--EGFENKPPHH--LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
2.06e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.57 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGD-NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDgtniYGNIDVAD 80
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID----YSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIAR 158
Cdd:PRK13636 80 LRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDE-VRKRVDNALKRTGI-EHLKDK-PTHC--LSFGQKKRVAIAG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQARRISDRTafFLMGE 221
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNV--FVMKE 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-214 |
5.08e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 116.74 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliEGVTiKGKLDMDGTNI--YGNIDVADLRIRVGMVFQK 91
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE----ELPT-SGTIRVNGQDVsdLRGRAIPYLRRKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 PNPFP-MSIYENVAYGLRAQGIKDKkyidevvESSLRSAALWDEVKDRLKAHAF--GLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:cd03292 87 FRLLPdRNVYENVAFALEVTGVPPR-------EIRKRVPAALELVGLSHKHRALpaELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327251791 169 MDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHsmqqARRISDRT 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH----AKELVDTT 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-213 |
6.62e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.13 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDgtniygniDVADLRIRVGMVFQKP 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--------DVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESS---LRSAALWDEvkdRLKAhafgLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:PRK11000 85 ALYPhLSVAENMSFGLKLAGAK-KEEINQRVNQVaevLQLAHLLDR---KPKA----LSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1327251791 169 MDEPTSALDPI--ATHKIE--ELMEDLKKdfTIVIVTHSMQQARRISDR 213
Cdd:PRK11000 157 LDEPLSNLDAAlrVQMRIEisRLHKRLGR--TMIYVTHDQVEAMTLADK 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-234 |
1.16e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.54 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNdliegVTIKGKLDMDGTNIYG---NIDVADLRIRVGMVFQKPNP 94
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLITStskNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 --FPMSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRlkaHAFGLSGGQQQRLCIARTIAMEPDVILMDEP 172
Cdd:PRK13649 97 qlFEETVLKDVAFGPQNFGVS-QEEAEALAREKLALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 173 TSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-224 |
1.35e-31 |
|
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: 116.09 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndlIEGVTIK-GKLDMDGTNIYGniDVADLRIR 84
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL------MGLLPVKsGSIRLDGEDITK--LPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGM--VFQKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVEsslrsaaLWDEVKDRLKAHAFGLSGGQQQRLCIARTIA 161
Cdd:TIGR03410 75 AGIayVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQARRISDRtaFFLM--GELVE 224
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADR--YYVMerGRVVA 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-223 |
1.83e-31 |
|
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: 115.28 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 24 LPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEG--VTIKGKLDMDGTNiYGNIDVADlriR-VGMVFQKPNPFP-MSI 99
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLL-------NLIAGfeTPQSGRVLINGVD-VTAAPPAD---RpVSMLFQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 100 YENVAYGlRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPI 179
Cdd:cd03298 88 EQNVGLG-LSPGLKLTAEDRQAIEVALARVGL-AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327251791 180 ATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03298 163 LRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-224 |
3.53e-31 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 114.24 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNIYGnidvadlriR 84
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGeITFDGKSYQKNIEALR---------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVvessLRSAALWDEVKDRLKahafGLSGGQQQRLCIARTIAME 163
Cdd:cd03268 74 IGALIEAPGFYPnLTARENLRLLARLLGIRKKR-IDEV----LDVVGLKDSAKKKVK----GFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVE 224
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-230 |
4.20e-31 |
|
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: 114.84 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQA----LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKG----KLDMDGtniygn 75
Cdd:COG4181 10 ELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGtVRLAGqdlfALDEDA------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 76 idVADLRIR-VGMVFQK----PNpfpMSIYENVAYGLRAQGIKDKKyidevvessLRSAALWDEV--KDRLKAHAFGLSG 148
Cdd:COG4181 84 --RARLRARhVGFVFQSfqllPT---LTALENVMLPLELAGRRDAR---------ARARALLERVglGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 149 GQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGELVEHN 226
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
....
gi 1327251791 227 ETSV 230
Cdd:COG4181 229 AATA 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-234 |
4.94e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRclnRMNDLIegVTIKGKLDMDGTNIYGNIDVADLRIRVGMVFQKP-NPFP 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAK---HMNALL--IPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYE-NVAYGLRAQGIKDKKyIDEVVESSLRSAALWDevkdrLKAHA-FGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:PRK13633 100 ATIVEeDVAFGPENLGIPPEE-IRERVDESLKKVGMYE-----YRRHApHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 175 ALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGELVEHNETSVIFSE 234
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-233 |
5.83e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 5.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTniygnidV 78
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGMVLSEET-------V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKP-NPFPMSIYEN-VAYGLRAQGIKDKKYIdEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCI 156
Cdd:PRK13635 77 WDVRRQVGMVFQNPdNQFVGATVQDdVAFGLENIGVPREEMV-ERVDQALRQVGM-EDFLNREPHR---LSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK--KDFTIVIVTHSMQQARRiSDRTAFFLMGELVEHNETSVIFS 233
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-235 |
5.94e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndLIEGVTIKGKLDMDGTNIyGNIDVA 79
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITL-TAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKP-NPF-PMSIYENVAYGLRAQGIKDKKYIdEVVESSLRSAALWDEVKdrlkAHAFGLSGGQQQRLCIA 157
Cdd:PRK13640 81 DIREKVGIVFQNPdNQFvGATVGDDVAFGLENRAVPRPEMI-KIVRDVLADVGMLDYID----SEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQArRISDRTAFFLMGELVEHNETSVIFSEP 235
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-223 |
8.22e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 113.25 E-value: 8.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGtniygniDVADLRIRVGMVFQKP 92
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-------EPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRLKahafGLSGGQQQRLCIARTIAMEPDVILMDE 171
Cdd:TIGR01188 76 SVDEdLTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 172 PTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-207 |
1.06e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.26 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmNDLIEGVTIKGKLDMDGTNIYgniDVADLRIRV 85
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLT---ALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyiDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEP 164
Cdd:COG4136 79 GILFQDDLLFPhLSVGENLAFALPPTIGRAQR--RARVEQALEEAGL-AGFADRDPAT---LSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQA 207
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDA 197
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-236 |
1.39e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFYG-----DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnRMNDLIEgvTIKGKLDMDGTNI---YGNIDV 78
Cdd:PRK13641 6 ENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQ---HFNALLK--PSSGTITIAGYHItpeTGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIKDKKYIDEVVESsLRSAALWDEVKDRlkaHAFGLSGGQQQRLCI 156
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSEDEAKEKALKW-LKKVGLSEDLISK---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEP 235
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
.
gi 1327251791 236 K 236
Cdd:PRK13641 237 E 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
1.81e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY---GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIYgnidvaDL 81
Cdd:PRK13652 4 IETRDLCYsysGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsVLIRGE-PITKENIR------EV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNP--FPMSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIART 159
Cdd:PRK13652 77 RKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEP 235
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-204 |
3.82e-29 |
|
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: 109.22 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIyGNIDV 78
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLK-------LLAGLYKptSGSVLLDGTDI-RQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNPFPMSIYENVAYGLRAQGikdkkyiDEVVESSLRSAALWDEVKD-------RLKAHAFGLSGGQQ 151
Cdd:cd03245 74 ADLRRNIGYVPQDVTLFYGTLRDNITLGAPLAD-------DERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 152 QRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSM 204
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-213 |
5.56e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.77 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGvtikgkLDM--DGTNIYGNIDVADLRI 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-------LLAG------LETpsAGELLAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAqgikdkKYIDEVVEsSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAM 162
Cdd:PRK11247 82 DTRLMFQDARLLPwKKVIDNVGLGLKG------QWRDAALQ-ALAAVGLADRANEWPAA----LSGGQKQRVALARALIH 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDR 213
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADR 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
8.13e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 8.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGD--NQALKSINLPIPTRQVTALIGPSGCGKSTLlrclnrmNDLIEGV--TIKGKLDMDGTNI-YGNIDv 78
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTI-------SKILTGLlkPQSGEIKIDGITIsKENLK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 aDLRIRVGMVFQKP-NPF-PMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAalwdeVKDRLKAHAFGLSGGQQQRLCI 156
Cdd:PRK13632 80 -EIRKKIGIIFQNPdNQFiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVG-----MEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQArRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-237 |
8.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 8.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNK-FDIENLDLFY---GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVtikgkLDMDGTNIYGNi 76
Cdd:PRK13642 1 MNKiLEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK-----VKIDGELLTAE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLRIRVGMVFQKP-NPF-PMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALwdEVKDRLKAHafgLSGGQQQRL 154
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKTREPAR---LSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRiSDRTAFFLMGELVEHNETSVIF 232
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
....*
gi 1327251791 233 SEPKD 237
Cdd:PRK13642 229 ATSED 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-213 |
1.05e-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: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 22 INLPIPTRQVTALIGPSGCGKSTLLRClnrmndlIEGVT--IKGKLDMDGTNIYGN---IDVADLRIRVGMVFQKPNPFP 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRL-------IAGLTrpDEGEIVLNGRTLFDSrkgIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 -MSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLkahafglSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:TIGR02142 89 hLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRL-------SGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327251791 176 LDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDR 213
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADR 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-202 |
1.05e-28 |
|
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: 109.02 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIK--GKldmdgtnIYGNIDVADL 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGE-------RRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMV---FQKPNPFPMSIYENVAYGLRAQ-GIkDKKYIDEVVESSLRSAALW--DEVKDRLkahaFG-LSGGQQQRL 154
Cdd:COG1119 77 RKRIGLVspaLQLRFPRDETVLDVVLSGFFDSiGL-YREPTDEQRERARELLELLglAHLADRP----FGtLSQGEQRRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTH 202
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTH 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
1.40e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 105.97 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTI--KGKLDMDGTNIYGNIDVADL 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS-------GLYKpdSGEILVDGKEVSFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQkpnpfpmsiyenvayglraqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIA 161
Cdd:cd03216 74 RAGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-234 |
1.43e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.44 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 16 NQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGklDMDGTNIYGNIDVADLRIRVGMVFQKPNP- 94
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKQKEIKPVRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 -FPMSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRlkaHAFGLSGGQQQRLCIARTIAMEPDVILMDEPT 173
Cdd:PRK13643 97 lFEETVLKDVAFGPQNFGIP-KEKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 174 SALDPIATHKIEELMEDLKKDF-TIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
1.81e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.41 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRM-------------NDLIEGVTIKGKLDMDGTNIYGNI-----DV 78
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIQKTRfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQ--KPNPFPMSIYENVAYGLRAQGIKD-------KKYIDEVvesslrsaALwDEvkDRLKAHAFGLSGG 149
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKeeakkraAKYIELV--------GL-DE--SYLQRSPFELSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNET 228
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDT 249
|
....*...
gi 1327251791 229 SVIFSEPK 236
Cdd:PRK13651 250 YDILSDNK 257
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-210 |
2.34e-28 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 106.93 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNI--YGNIDVADL-R 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIG----LLEKFD-SGQVYLNGQETppLNSKKASKFrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKpnpFPM----SIYENVAYGLRAQgIKDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIAR 158
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGLKYK-KLSKKEKREKKKEALEKVGL----NLKLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSM---QQARRI 210
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-246 |
3.83e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.51 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndLIEgvTIKGKLDMDGTNIyGNIDVADLR----IRVGMVF 89
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIE--PTRGQVLIDGVDI-AKISDAELRevrrKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVESsLRSAALWDevkdrlKAHAF--GLSGGQQQRLCIARTIAMEPDV 166
Cdd:PRK10070 113 QSFALMPhMTVLDNTAFGMELAGINAEERREKALDA-LRQVGLEN------YAHSYpdELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 167 ILMDEPTSALDP-IATHKIEELME-DLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTKGYV 244
Cdd:PRK10070 186 LLMDEAFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
..
gi 1327251791 245 NG 246
Cdd:PRK10070 266 RG 267
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-233 |
5.40e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.17 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGtNIYGNIDVADLRIRVGMVFQKP--NP 94
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPA-NLKKIKEVKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYENVAYGLRAQGiKDKKYIDEVVESSLRSAALwdeVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:PRK13645 104 FQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 175 ALDPIATHKIEELMEDLKKDFT--IVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-223 |
5.60e-28 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 107.38 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNdliegVTIKGKLDMDGTNI--YGNIDVADlriR 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHIqhYASKEVAR---R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKP-NPFPMSIYENVAYGLRAQG---IKDKKYIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTI 160
Cdd:PRK10253 83 IGLLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 161 AMEPDVILMDEPTSALDpiATHKIE--ELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK10253 159 AQETAIMLLDEPTTWLD--ISHQIDllELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-227 |
5.85e-28 |
|
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: 106.80 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNdliegVTIKGKLDMDGTNIyGNIDVADLRIR 84
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-----VPENGRVLVDGHDL-ALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGLRAQGIKdkkyidEVVESslrsAALWDevkdrlkAHAF-----------------GLS 147
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNIALADPGMSME------RVIEA----AKLAG-------AHDFiselpegydtivgeqgaGLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 148 GGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE--- 224
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEqgs 219
|
...
gi 1327251791 225 HNE 227
Cdd:cd03252 220 HDE 222
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-235 |
9.25e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.15 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliEGVTiKGKLDMDGTNIYgniDVADLRIR 84
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF----EQPT-AGQIMLDGVDLS---HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRaQGIKDKKYIDEVVESSLRSAALWDEVKDrlKAHAfgLSGGQQQRLCIARTIAME 163
Cdd:PRK11607 93 INMMFQSYALFPhMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR--KPHQ--LSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 164 PDVILMDEPTSALDPIATHKIE-ELMEDLKK-DFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEP 235
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-236 |
9.47e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.13 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRCLNrmndLIEGVTiKGKLDMDGTNIYGN--IDVADLRIRVGMVFQKP----NPF---------PM 97
Cdd:PRK11308 45 AVVGESGCGKSTLARLLT----MIETPT-GGELYYQGQDLLKAdpEAQKLLRQKIQIVFQNPygslNPRkkvgqileePL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 98 SIYENVAYGLRAqgikdkkyidEVVESSLRSAALWDEVKDRLkAHAFglSGGQQQRLCIARTIAMEPDVILMDEPTSALD 177
Cdd:PRK11308 120 LINTSLSAAERR----------EKALAMMAKVGLRPEHYDRY-PHMF--SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 178 PIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-225 |
1.05e-27 |
|
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: 110.58 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYG--DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIyGNIDVAD 80
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-----PDSGQILLDGHDL-ADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFPMSIYENVAYGLRAQgikdkkYIDEVVESSLRSAALWDEVkDRLK--------AHAFGLSGGQQQ 152
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQ------ADRAEIERALAAAYAQDFV-DKLPlgldtpigENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVEH 225
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVER 548
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-244 |
1.10e-27 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 106.32 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLfYGDNQALKSINLPIPTRQVTALIGPSGCGKStlLRCLNRMNDLIEGVT-IKGKLDMDGTNIYGnidvADL 81
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGRVLLDGKPVAP----CAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIR-VGMVFQKP----NPFpMSIYENVAYGLRAQGIKDKkyiDEVVESSLRSAALwDEVKDRLKAHAFGLSGGQQQRLCI 156
Cdd:PRK10418 77 RGRkIATIMQNPrsafNPL-HTMHTHARETCLALGKPAD---DATLTAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
250
....*....|
gi 1327251791 235 PKDDRTKGYV 244
Cdd:PRK10418 232 PKHAVTRSLV 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
1.33e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-----ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLN-----RMNDL-IEGVTIKGKLDMDGTNIYG 74
Cdd:PRK13631 24 VKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIqVGDIYIGDKKNNHELITNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 75 NI----DVADLRIRVGMVFQKP--NPFPMSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRlkaHAFGLSG 148
Cdd:PRK13631 104 YSkkikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGLDDSYLER---SPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 149 GQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVEHNE 227
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*...
gi 1327251791 228 TSVIFSEP 235
Cdd:PRK13631 260 PYEIFTDQ 267
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-222 |
2.14e-27 |
|
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: 104.56 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 23 NLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVT--IKGKLDMDGTNIYGnidVADLRIRVGMVFQKPNPFP-MSI 99
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLL-------NLIAGFIepASGSIKVNDQSHTG---LAPYQRPVSMLFQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 100 YENVAYGLRAqGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPI 179
Cdd:TIGR01277 88 RQNIGLGLHP-GLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQ---LSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327251791 180 ATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGEL 222
Cdd:TIGR01277 163 LREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-205 |
2.87e-27 |
|
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: 109.57 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDNQ--ALKSINLPI-PTRQVtALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDV 78
Cdd:TIGR03375 463 EIEFRNVSFAYPGQEtpALDNVSLTIrPGEKV-AIIGRIGSGKSTLLKLLLGLYQPTEGsVLL------DGVDI-RQIDP 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNPFPMSIYENVAYGlrAQGIKDkkyiDEVVESsLRSAALWDEVkdRLKAHAF---------GLSGG 149
Cdd:TIGR03375 535 ADLRRNIGYVPQDPRLFYGTLRDNIALG--APYADD----EEILRA-AELAGVTEFV--RRHPDGLdmqigergrSLSGG 605
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQ 205
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-213 |
5.65e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 5.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTIK--GKLDMDGTNI-YGNIDVAdLRIRVGMVF 89
Cdd:COG1129 14 FGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILS-------GVYQPdsGEILLDGEPVrFRSPRDA-QAAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFP-MSIYENVAYG--LRAQGIKDKKYIDEvvesslRSAALWDEVKDRLKAHA--FGLSGGQQQRLCIARTIAMEP 164
Cdd:COG1129 86 QELNLVPnLSVAENIFLGrePRRGGLIDWRAMRR------RARELLARLGLDIDPDTpvGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADR 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-210 |
8.13e-27 |
|
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: 101.91 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQA--LKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGV--TIKGKLDMDGTNIyGNIDVADL 81
Cdd:cd03246 3 VENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLAR-------LILGLlrPTSGRVRLDGADI-SQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVayglraqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIA 161
Cdd:cd03246 75 GDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALY 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSM---QQARRI 210
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPetlASADRI 165
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-213 |
1.13e-26 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 102.87 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmDGTNIYGNIDVADLRIRVGMVFQKPNPF 95
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGsLTLAGK---EVTNLSYSQKIILRRELIGYIFQSFNLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 96 P-MSIYENVAYGLRAQGIKDKKYIDEVvessLRSAALWDeVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:NF038007 96 PhLSIFDNVALPLKYRGVAKKERIERV----NQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTG 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327251791 175 ALDPIATHKIEELMEDL-KKDFTIVIVTHSmQQARRISDR 213
Cdd:NF038007 171 NLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNR 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-203 |
1.23e-26 |
|
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: 107.45 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIYgNIDVADLRIRVGMVFQKPN 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 PFPMSIYENVAYGlRAQGIkdkkyiDEVVESSLRSAALWDEVKDR-------LKAHAFGLSGGQQQRLCIARTIAMEPDV 166
Cdd:TIGR02868 420 LFDTTVRENLRLA-RPDAT------DEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327251791 167 ILMDEPTSALDPIAThkiEELMEDLKK---DFTIVIVTHS 203
Cdd:TIGR02868 493 LLLDEPTEHLDAETA---DELLEDLLAalsGRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-210 |
1.61e-26 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 102.55 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNIYgnidvadLRIRVGMVFQKPN 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGqVLLDGKPISQYEHKY-------LHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 PFPMSIYENVAYGLraQGIKDkkyiDEVVESSLRSAA----------LWDEVKDRlkahAFGLSGGQQQRLCIARTIAME 163
Cdd:cd03248 99 LFARSLQDNIAYGL--QSCSF----ECVKEAAQKAHAhsfiselasgYDTEVGEK----GSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH---SMQQARRI 210
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHrlsTVERADQI 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-177 |
2.00e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.93 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFY-GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnRMNDLIEGVTiKGKLDMDGTNIyGNIDVA 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL----RMVAGLERIT-SGEIWIGGRVV-NELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIrvGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALwDEVKDRlKAHAfgLSGGQQQRLCIAR 158
Cdd:PRK11650 75 DRDI--AMVFQNYALYPhMSVRENMAYGLKIRGM-PKAEIEERVAEAARILEL-EPLLDR-KPRE--LSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 1327251791 159 TIAMEPDVILMDEPTSALD 177
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-246 |
3.77e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 3.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNI--YGNI 76
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLR-------LIGGQIApdHGEILFDGENIpaMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLRIRVGMVFQKPNPFP-MSIYENVAYGLRAQgikdkkyiDEVVESSLRSAALwdevkdrLKAHAFG---------- 145
Cdd:PRK11831 78 RLYTVRKRMSMLFQSGALFTdMNVFDNVAYPLREH--------TQLPAPLLHSTVM-------MKLEAVGlrgaaklmps 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 146 -LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRtAFFLMGEL 222
Cdd:PRK11831 143 eLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIADH-AYIVADKK 221
|
250 260
....*....|....*....|....
gi 1327251791 223 VEHNETSVIFSEPKDDRTKGYVNG 246
Cdd:PRK11831 222 IVAHGSAQALQANPDPRVRQFLDG 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-214 |
6.02e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.00 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtIKGKLDMDGtniyGNIDVADLRiRVGMVFQK- 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKV------------LAGVLRPTS----GTVRRAGGA-RVAYVPQRs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 --PNPFPMSIYENVAYG-------LRAQGIKDKKyideVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAM 162
Cdd:NF040873 65 evPDSLPLTVRDLVAMGrwarrglWRRLTRDDRA----AVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRT 214
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-205 |
6.52e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.24 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-----ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndLIEGVTIKGKLDMDGtniygnidvad 80
Cdd:cd03250 3 VEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----LGELEKLSGSVSVPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 lriRVGMVFQKPNPFPMSIYENVAYGlraqgikdKKYIDEVVESSLRSAALwdeVKDrLKAHAFG-----------LSGG 149
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENILFG--------KPFDEERYEKVIKACAL---EPD-LEILPDGdlteigekginLSGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDP-IATHKIEE-LMEDLKKDFTIVIVTHSMQ 205
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENcILGLLLNNKTRILVTHQLQ 189
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-224 |
7.09e-26 |
|
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: 100.65 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADL 81
Cdd:cd03244 4 EFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGsILI------DGVDI-SKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVayglraqgikD--KKYIDEVVESSLRSAALWDEVKDRLKAHAF-------GLSGGQQQ 152
Cdd:cd03244 77 RSRISIIPQDPVLFSGTIRSNL----------DpfGEYSDEELWQALERVGLKEFVESLPGGLDTvveeggeNLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHsmqqarRI-----SDRTAFFLMGELVE 224
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVVE 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
8.03e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 8.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIyGNIDVADLRI 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGeVLV------DGLDV-ATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKpNPFPM--SIYENVAYG--------LRAQgikDKKYIDEVVE----SSLRSAALwDEvkdrlkahafgLSGG 149
Cdd:COG4604 76 RLAILRQE-NHINSrlTVRELVAFGrfpyskgrLTAE---DREIIDEAIAyldlEDLADRYL-DE-----------LSGG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADH 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-236 |
8.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 8.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRclnRMNDLIEGVTikGKLDMDGTNIYGNID---VADLRIRVGMVFQKPN 93
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQ---NINALLKPTT--GTVTVDDITITHKTKdkyIRPVRKRIGMVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 P--FPMSIYENVAYGLRAQGIKdkkyIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDE 171
Cdd:PRK13646 96 SqlFEDTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 172 PTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-223 |
1.27e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 100.13 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGtniygnIDV- 78
Cdd:cd03266 4 ADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLR-------MLAGLLEpdAGFATVDG------FDVv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ---ADLRIRVGMVFQKPNPFP-MSIYENVAY-----GLRAQGIKDKkyIDEVVESSlrsaalwdEVKDRLKAHAFGLSGG 149
Cdd:cd03266 71 kepAEARRRLGFVSDSTGLYDrLTARENLEYfaglyGLKGDELTAR--LEELADRL--------GMEELLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-177 |
1.49e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 104.65 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDN--QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndLIEGVTIKGKLDMDGTNIYGnIDVADLR 82
Cdd:TIGR03797 453 EVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDLAG-LDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGLRAQgikdkkyIDEVVESsLRSAALWDEVKDR-------LKAHAFGLSGGQQQRLC 155
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENIAGGAPLT-------LDEAWEA-ARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQRLL 598
|
170 180
....*....|....*....|..
gi 1327251791 156 IARTIAMEPDVILMDEPTSALD 177
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALD 620
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-224 |
1.58e-25 |
|
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: 98.54 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDN--QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmnDLiegVTIKGKLDMDGTNIygNIDVADL 81
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DL---KPQQGEITLDGVPV--SDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVayGLRaqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIA 161
Cdd:cd03247 74 SSLISVLNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRIsDRTAFFLMGELVE 224
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-203 |
2.08e-25 |
|
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: 98.78 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmnDLIEGVTIKGKLDMDGTNIYGNidvaDLRIRVGMVFQKPNPFP-M 97
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---GRRTGLGVSGEVLINGRPLDKR----SFRKIIGYVPQDDILHPtL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 98 SIYENVAYglraqgikdkkyidevvesslrSAALwdevkdRlkahafGLSGGQQQRLCIARTIAMEPDVILMDEPTSALD 177
Cdd:cd03213 98 TVRETLMF----------------------AAKL------R------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*..
gi 1327251791 178 PIATHKIEELMEDLKKD-FTIVIVTHS 203
Cdd:cd03213 144 SSSALQVMSLLRRLADTgRTIICSIHQ 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-224 |
2.28e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.27 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 12 FYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvTIKgkldMDGTNIYGnIDVADLRIRVGMVFQK 91
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG-RIL----IDGTDIRT-VTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 PNPFPMSIYENVAYGlraqgiKDKKYIDEVVESSLRSAAL--WDEVKDRLKAHAfG-----LSGGQQQRLCIARTIAMEP 164
Cdd:PRK13657 418 AGLFNRSIEDNIRVG------RPDATDEEMRAAAERAQAHdfIERKPDGYDTVV-GergrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE 224
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-233 |
2.54e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 100.26 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKG----KLDMDGTNIYgnidvadlRIRVGMVFQK 91
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGtVSFRGqdlyQLDRKQRRAF--------RRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 P----NPfPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVI 167
Cdd:TIGR02769 97 SpsavNP-RMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-225 |
4.64e-25 |
|
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: 98.25 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDN--QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIyGNIDVAD 80
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG-----KIEIDGIDI-STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFPMSIYENV-AYGlraqgikdkKYIDEVVESSLRsaalwdevkdrLKAHAFGLSGGQQQRLCIART 159
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLdPFD---------EYSDEEIYGALR-----------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMqqaRRISDRTAFFLM--GELVEH 225
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRL---RTIIDYDKILVMdaGEVKEY 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-213 |
7.35e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.88 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIYGNIDVAdlR 82
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLR-------MLLGLTHpdAGSISLCGEPVPSRARHA--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVA-----YGLRAQGIKdkkyidEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCI 156
Cdd:PRK13537 80 QRVGVVPQFDNLDPdFTVRENLLvfgryFGLSAAAAR------ALVPPLLEFAKL----ENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKI-EELMEDLKKDFTIVIVTHSMQQARRISDR 213
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-227 |
1.10e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 102.13 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNqALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIyGNIDVADLRIRVGMVFQKP 92
Cdd:TIGR01193 485 YGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSL-KDIDRHTLRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSIYENVAYGLRAQGIKDKkyIDEVVESslrsAALWDEVKD-------RLKAHAFGLSGGQQQRLCIARTIAMEPD 165
Cdd:TIGR01193 558 YIFSGSILENLLLGAKENVSQDE--IWAACEI----AEIKDDIENmplgyqtELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDLkKDFTIVIVTHSMQQARRiSDRTAFFLMGELVEHNE 227
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-202 |
1.28e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 101.82 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFY-GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIkgkldmDGTNIYgniDV--ADLR 82
Cdd:COG5265 361 ENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGrILI------DGQDIR---DVtqASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAYGlRAQGIkdkkyiDEVVESSLRSAALWD-----------EVKDR-LKahafgLSGGQ 150
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNIAYG-RPDAS------EEEVEAAARAAQIHDfieslpdgydtRVGERgLK-----LSGGE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 151 QQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-202 |
1.86e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIE--NLDLFY--GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNI--Ygni 76
Cdd:PRK11176 339 KGDIEfrNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG-----EILLDGHDLrdY--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLRIRVGMVFQKPNPFPMSIYENVAYGlraqgiKDKKYIDEVVESSLRSAALWDEVKdRLKaHAFG---------LS 147
Cdd:PRK11176 411 TLASLRNQVALVSQNVHLFNDTIANNIAYA------RTEQYSREQIEEAARMAYAMDFIN-KMD-NGLDtvigengvlLS 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 148 GGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-207 |
2.47e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 2.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIygnidvADLRIRVGMVFQKP-NPFP 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF------EKLRKHIGIVFQNPdNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYE-NVAYGLRAQGIKDKKyIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:PRK13648 98 GSIVKyDVAFGLENHAVPYDE-MHRRVSEALKQVDMLERADYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190
....*....|....*....|....*....|....
gi 1327251791 176 LDPIATHKIEELMEDLK--KDFTIVIVTHSMQQA 207
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKseHNITIISITHDLSEA 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-202 |
2.52e-24 |
|
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: 96.01 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRC---LNRMNDliegvtikGKLDMDGTNIygNIDVADLR 82
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIlagLLPPSA--------GEVLWNGEPI--RDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFP-MSIYENVAYGLRAQGIK-DKKYIDEVVESsLRSAALWDevkdrLKAHAfgLSGGQQQRLCIARTI 160
Cdd:COG4133 75 RRLAYLGHADGLKPeLTVRENLRFWAALYGLRaDREAIDEALEA-VGLAGLAD-----LPVRQ--LSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMED-LKKDFTIVIVTH 202
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-224 |
4.28e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.57 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNdliegVTIKGKLDMDGTNIYgNIDVADLRIRVGMVFQKPNP 94
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-----QPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYENVAYGLRaqgikdkKYIDEVVESSLRSAALWDEVKDRLKA-------HAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:TIGR00958 567 FSGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEFPNGydtevgeKGSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEdlKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVE 224
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-214 |
6.94e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 6.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLrclnrmnDLIEG--VTIKGKLDMDGTNiygNIDVADLRIRVGMVFQKPNPFP-MSIYENVAYGLrA 109
Cdd:PRK10771 29 AILGPSGAGKSTLL-------NLIAGflTPASGSLTLNGQD---HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 110 QGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELME 189
Cdd:PRK10771 98 PGLKLNAAQREKLHAIARQMGI-EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180
....*....|....*....|....*..
gi 1327251791 190 DL--KKDFTIVIVTHSMQQARRISDRT 214
Cdd:PRK10771 174 QVcqERQLTLLMVSHSLEDAARIAPRS 200
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-223 |
8.56e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 8.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGvtikgkLDMDGTNIYGNI-------DVADLRIRVGMVF 89
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLL-------DAISG------RVEGGGTTSGQIlfngqprKPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFP-MSIYENVAYG--LRAQGIKDKKYIDEVVE-SSLRSAALWDEVKDRLKahafGLSGGQQQRLCIARTIAMEPD 165
Cdd:cd03234 88 QDDILLPgLTVRETLTYTaiLRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVK----GISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVThsMQQAR----RISDRTAFFLMGELV 223
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILT--IHQPRsdlfRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-213 |
1.01e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQ---ALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIYGN 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVR-------LIDGLLEaeSGQIIIDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 76 iDVADLRIRVGMVFQKP-NPFPMSIYEN-VAYGLRAQGIkDKKYIDEVVESSLRSAALWDeVKDRLKAHafgLSGGQQQR 153
Cdd:PRK13650 75 -NVWDIRHKIGMVFQNPdNQFVGATVEDdVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKEREPAR---LSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 154 LCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQArRISDR 213
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDR 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-213 |
1.02e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrMNDLI---EG-VTIKGKldmdgtniygNIDVAD 80
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRI---ILGILapdSGeVLWDGE----------PLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRiRVG-M-----VFQKpnpfpMSIYENVAY-----GLRAQGIKDKkyIDEVVEsslrsaALwdEVKDRLKAHAFGLSGG 149
Cdd:COG4152 70 RR-RIGyLpeergLYPK-----MKVGEQLVYlarlkGLSKAEAKRR--ADEWLE------RL--GLGDRANKKVEELSKG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIV-THSMQQARRISDR 213
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDR 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-241 |
1.12e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNIYgniDVADLRIRVGMVFQKPNPfPMSIYENVAYG----LR 108
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG---KLQALRRDIQFIFQDPYA-SLDPRQTVGDSimepLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 109 AQGIKDKKYIDEVVESSLRSAALWDEVKDRLkAHAFglSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELM 188
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLPEHAWRY-PHEF--SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 189 EDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK10261 507 LDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-213 |
1.36e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIYGNIDVAdlRIRVGMVFQ 90
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIAR-------MILGMTSpdAGKITVLGVPVPARARLA--RARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 91 KPNPFP-MSIYEN-VAYGlRAQGIKDKKyIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:PRK13536 122 FDNLDLeFTVRENlLVFG-RYFGMSTRE-IEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327251791 169 MDEPTSALDPIATHKI-EELMEDLKKDFTIVIVTHSMQQARRISDR 213
Cdd:PRK13536 196 LDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-213 |
1.60e-23 |
|
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: 94.27 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygNIDVADlRIR 84
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGeVLFDGK----------PLDIAA-RNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAME 163
Cdd:cd03269 72 IGYLPEERGLYPkMKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDR 213
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDR 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-214 |
2.38e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 16 NQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtIKGKLDMDGTNIY-GNIDVADL----RIR-VGMVF 89
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA------------IAGSLPPDSGSILiDGKDVTKLpeykRAKyIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QkpNPF----P-MSIYENVA--------YGLRaQGIKdKKYIDEVVEsSLRSAALWDEvkDRLKAHAFGLSGGQQQRLci 156
Cdd:COG1101 87 Q--DPMmgtaPsMTIEENLAlayrrgkrRGLR-RGLT-KKRRELFRE-LLATLGLGLE--NRLDTKVGLLSGGQRQAL-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 157 arTIAM----EPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRT 214
Cdd:COG1101 158 --SLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-241 |
2.66e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.31 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLD-LFYGDNQALKS---INLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGK--LDMDgtniygNI 76
Cdd:PRK15079 18 FDIKDGKqWFWQPPKTLKAvdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGeVAWLGKdlLGMK------DD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 77 DVADLRIRVGMVFQKP----NPfPMSIYENVAYGLRAQGIKDKKyidevvesslrsaalwDEVKDRLKA----------- 141
Cdd:PRK15079 92 EWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTYHPKLSR----------------QEVKDRVKAmmlkvgllpnl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 142 -----HAFglSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDRT 214
Cdd:PRK15079 155 inrypHEF--SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRV 232
|
250 260
....*....|....*....|....*..
gi 1327251791 215 AFFLMGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK15079 233 LVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-223 |
2.93e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEG-VTIKGkldmdGTNIYGNIDVADLRIR 84
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL-------NLIAGfVPYQH-----GSITLDGKPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFP-MSIYENVAYGLRAQGIkDKKYIDEVVESSLRSAALWDEVKDRLkahaFGLSGGQQQRLCIARTIAME 163
Cdd:PRK11248 72 RGVVFQNEGLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYI----WQLSGGQRQRVGIARALAAN 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQarrisdrtAFFLMGELV 223
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEE--------AVFMATELV 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-244 |
4.59e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.79 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYgdnqaLKSINLPI--------PTRQVTALIGPSGCGKSTLLRCLNRMNDLI------------------ 56
Cdd:PTZ00265 1165 KIEIMDVNFRY-----ISRPNVPIykdltfscDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 57 --------EGVTIK-----------------------GKLDMDGTNIYgNIDVADLRIRVGMVFQKPNPFPMSIYENVAY 105
Cdd:PTZ00265 1240 qdyqgdeeQNVGMKnvnefsltkeggsgedstvfknsGKILLDGVDIC-DYNLKDLRNLFSIVSQEPMLFNMSIYENIKF 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 106 GLRAQGIKDKKY------IDEVVESslrsaaLWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPI 179
Cdd:PTZ00265 1319 GKEDATREDVKRackfaaIDEFIES------LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 180 ATHKIEELMEDLKK--DFTIVIVTHSMQQARRiSDRTafflmgelvehnetsVIFSEPkdDRTKGYV 244
Cdd:PTZ00265 1393 SEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKI---------------VVFNNP--DRTGSFV 1441
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-236 |
1.00e-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: 93.36 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMD-GTNIYGNIDVAD--- 80
Cdd:TIGR02323 5 QVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA------------GRLAPDhGTATYIMRSGAElel 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 -----------LRIRVGMVFQKP-NPFPMSIYENVAYGLRAQGIKDKKYidevveSSLRSAAL-W-DEVK---DRLKAHA 143
Cdd:TIGR02323 73 yqlseaerrrlMRTEWGFVHQNPrDGLRMRVSAGANIGERLMAIGARHY------GNIRATAQdWlEEVEidpTRIDDLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 144 FGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGE 221
Cdd:TIGR02323 147 RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGR 226
|
250
....*....|....*
gi 1327251791 222 LVEHNETSVIFSEPK 236
Cdd:TIGR02323 227 VVESGLTDQVLDDPQ 241
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-236 |
1.71e-22 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 92.34 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTllrCLNRMNDLIEgvTIKGKLDMDGTNIygNIDVADLRIRV 85
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDI--THLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVF--QKPNPF-PMSIYENVAYGLRAQGIKDKKYIDEVVEsslrsaALWDE--VKDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:TIGR04406 77 GIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLE------ALLEEfqISHLRDNKAMSLSGGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPK 236
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKeRGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-213 |
3.39e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmNDLiegVTIKGKLDMDGTNIyGNIDVADLRIR 84
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GEL---SPDSGEVRLNGRPL-ADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPN-PFPMSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDeVKDRLKAHafgLSGGQQQRLCIARTIA-- 161
Cdd:PRK13548 78 RAVLPQHSSlSFPFTVEEVVAMGRAPHGLSRAE-DDALVAAALAQVDLAH-LAGRDYPQ---LSGGEQQRVQLARVLAql 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 162 ----MEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDR 213
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYADR 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-213 |
5.73e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 22 INLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVTI--KGKLDMDGT---NIYGNIDVADLRIRVGMVFQKPNPFP 96
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLI-------NAISGLTRpqKGRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 -MSIYENVAYGLRAqgiKDKKYIDEVVEsslrsaaLWDeVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:PRK11144 90 hYKVRGNLRYGMAK---SMVAQFDKIVA-------LLG-IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327251791 176 LD-PiathKIEELM---EDLKKDFTIVI--VTHSMQQARRISDR 213
Cdd:PRK11144 159 LDlP----RKRELLpylERLAREINIPIlyVSHSLDEILRLADR 198
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-224 |
8.21e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKG----KLDMDGtniygnidVADLRIRVGMVFQK 91
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGnVSWRGeplaKLNRAQ--------RKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 P----NPfPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVI 167
Cdd:PRK10419 98 SisavNP-RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELVE 224
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-235 |
1.20e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 90.37 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMD-GTNIYGN-----IDVA 79
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALS------------ARLAPDaGEVHYRMrdgqlRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DL---------RIRVGMVFQKP-NPFPMSIYE--NVAYGLRAQGikDKKYIDevvessLRSAAL-W-DEVK---DRLKAH 142
Cdd:PRK11701 77 ALseaerrrllRTEWGFVHQHPrDGLRMQVSAggNIGERLMAVG--ARHYGD------IRATAGdWlERVEidaARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 143 AFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMG 220
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250
....*....|....*
gi 1327251791 221 ELVEHNETSVIFSEP 235
Cdd:PRK11701 229 RVVESGLTDQVLDDP 243
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-213 |
1.23e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.84 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKG----KLDMDGTniygnidvADLRIR-V 85
Cdd:PRK10584 19 GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGeVSLVGqplhQMDEEAR--------AKLRAKhV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPNPFP-MSIYENVAYGLRAQGIKDKkyidevvESSLRSAALWDEV--KDRLKAHAFGLSGGQQQRLCIARTIAM 162
Cdd:PRK10584 91 GFVFQSFMLIPtLNALENVELPALLRGESSR-------QSRNGAKALLEQLglGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRR 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-249 |
3.41e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndlIEGVTikGKLDMDGTNI-YGNIDVADLRIRvgMVFQKP--- 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM---IEPTS--GELLIDDHPLhFGDYSYRSQRIR--MIFQDPsts 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 -NP---------FPMSIYENVAYGLRAQGIKDkkyidevvesSLRSAALwdeVKDRLKAHAFGLSGGQQQRLCIARTIAM 162
Cdd:PRK15112 100 lNPrqrisqildFPLRLNTDLEPEQREKQIIE----------TLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRT 240
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELT 246
|
....*....
gi 1327251791 241 KGYVNGDFG 249
Cdd:PRK15112 247 KRLIAGHFG 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-213 |
3.97e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnRMNDLIEGVTIKG-KLDMDGTNIY--GNI--DVAD 80
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSAGsHIELLGRTVQreGRLarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFP-MSIYENVAYGlraqgikdkkyidevvesSLRSAALWDEV----KDRLKAHAF----------- 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVNrLSVLENVLIG------------------ALGSTPFWRTCfswfTREQKQRALqaltrvgmvhf 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 145 ------GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDR 213
Cdd:PRK09984 146 ahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCER 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-233 |
4.87e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTI-KGK-LDmdgtniYGNIDVADLRIRVGMVFQ 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwQGKpLD------YSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 91 KPNP--FPMSIYENVAYGLRAQGIKDKKYIDEVvesslrsaalwDEVKDRLKAHAFG------LSGGQQQRLCIARTIAM 162
Cdd:PRK13638 85 DPEQqiFYTDIDSDIAFSLRNLGVPEAEITRRV-----------DEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 163 EPDVILMDEPTSALDPIA-THKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFS 233
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGrTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-206 |
1.11e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.67 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLF-YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmNDLIEGVTIKGKLDMDGTNIyGNIDVADLRIR 84
Cdd:PRK11174 352 AEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIEL-RELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGlraqgikDKKYIDEVVESSLRSAALWD-----------EVKDRlkahAFGLSGGQQQR 153
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLG-------NPDASDEQLQQALENAWVSEflpllpqgldtPIGDQ----AAGLSVGQAQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 154 LCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQ 206
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-223 |
1.40e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 12 FYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVT--IKGKLDMDGTNI--YGNIDVADLRIRVGM 87
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-------LICGIErpSAGKIWFSGHDItrLKNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 88 VFQKPNPF-PMSIYENVAYGLRAQGIKDKKYIDEVvesslrSAALwDEVK--DRLKAHAFGLSGGQQQRLCIARTIAMEP 164
Cdd:PRK10908 84 IFQDHHLLmDRTVYDNVAIPLIIAGASGDDIRRRV------SAAL-DKVGllDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKK-DFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-213 |
1.46e-20 |
|
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: 86.83 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTniygniDVADL-- 81
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFY-------MIVGLVKpdSGKILLDGQ------DITKLpm 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 --RIRVGMVF--QKPNPF-PMSIYENVAYGLRAQGiKDKKYIDEVVESSLRSAALwDEVKDRLkahAFGLSGGQQQRLCI 156
Cdd:cd03218 70 hkRARLGIGYlpQEASIFrKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVEI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDR 213
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITDR 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-241 |
1.48e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKST----LLRCLNRmndliegvtiKGKLDMDGTNI--YGNIDVADLRIRVGM 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS----------QGEIWFDGQPLhnLNRRQLLPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 88 VFQKP----NPfPMSIYENVAYGLRA-QGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHafgLSGGQQQRLCIARTIAM 162
Cdd:PRK15134 367 VFQDPnsslNP-RLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE---FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKDFTI--VIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSEPKDDRT 240
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
.
gi 1327251791 241 K 241
Cdd:PRK15134 523 R 523
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-213 |
1.53e-20 |
|
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: 86.75 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVT--IKGKLDMDGTNIygnidvadlrIRVG----MVFQKP 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL-------NLISGLAqpTSGGVILEGKQI----------TEPGpdrmVVFQNY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFP-MSIYENVAYGL-RAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMD 170
Cdd:TIGR01184 64 SLLPwLTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQ---LSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327251791 171 EPTSALDPIATHKI-EELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:TIGR01184 140 EPFGALDALTRGNLqEELMQIWEEHrVTVLMVTHDVDEALLLSDR 184
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-223 |
2.36e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndliEGVTIKGKLDMDGTNIyGNIDVADLRIR 84
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG-----ELTPSSGEVRLNGRPL-AAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPN-PFPMSIYENVAYGlRAQGIKDKKYIDEVVESSLRSAALWDevkdrLKAHAF-GLSGGQQQRLCIARTIA- 161
Cdd:COG4559 77 RAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-----LAGRSYqTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 162 ------MEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRtaFFLM--GELV 223
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADR--ILLLhqGRLV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-202 |
2.78e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMDGtniyGNIDVADlRIRV 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA------------GELEPDS----GEVSIPK-GLRI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPNPFP-MSIYENVAYGLR--AQGIKDKKYIDEVVESSLRSAALWDEVKDRLKA--------------HAFG--- 145
Cdd:COG0488 64 GYLPQEPPLDDdLTVLDTVLDGDAelRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilSGLGfpe 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 146 ---------LSGGQQQRLCIARTIAMEPDVILMDEPTSALDpIAThkIEELmEDLKKDF--TIVIVTH 202
Cdd:COG0488 144 edldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES--IEWL-EEFLKNYpgTVLVVSH 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-202 |
4.47e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQAL-KSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGkLDMDGTniyGNIDVADLRir 84
Cdd:COG4178 365 LEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIA------------G-LWPYGS---GRIARPAGA-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 vGMVF--QKPNpFPM-SIYENVAYGLRAQGIKDkkyidEVVESSLRSAALwDEVKDRLKAHA---FGLSGGQQQRLCIAR 158
Cdd:COG4178 427 -RVLFlpQRPY-LPLgTLREALLYPATAEAFSD-----AELREALEAVGL-GHLAERLDEEAdwdQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-202 |
5.32e-20 |
|
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: 88.65 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndliEGV--TIKGKLDMDGTNIYgNIDVADLRIRVGMVFQK 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL-------VGVwpPTAGSVRLDGADLS-QWDREELGRHIGYLPQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 PNPFPMSIYENVAyglRAQGIKDkkyiDEVVEsslrsAALWDEVKD-----------RLKAHAFGLSGGQQQRLCIARTI 160
Cdd:COG4618 415 VELFDGTIAENIA---RFGDADP----EKVVA-----AAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTH 202
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITH 525
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-210 |
5.32e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLlrclnrMNdliegvtIKGKLDMDGTNIY--GNIDVADL-------- 81
Cdd:PRK10535 17 GEEQveVLKGISLDIYAGEMVAIVGASGSGKSTL------MN-------ILGCLDKPTSGTYrvAGQDVATLdadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 -RIRVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAalwdeVKDRLKAHAFGLSGGQQQRLCIART 159
Cdd:PRK10535 84 rREHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 160 IAMEPDVILMDEPTSALDpiaTHKIEELMEDLK----KDFTIVIVTHSMQ---QARRI 210
Cdd:PRK10535 159 LMNGGQVILADEPTGALD---SHSGEEVMAILHqlrdRGHTVIIVTHDPQvaaQAERV 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-228 |
8.37e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTniygnidVADLrIRVGMVFQ 90
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLK-------LIAGILEptSGRVEVNGR-------VSAL-LELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 91 kPNpfpMSIYENV-----AYGLRAQGIKDKkyIDEVVESSlrsaalwdEVKDRL----KAhafgLSGGQQQRLCIARTIA 161
Cdd:COG1134 101 -PE---LTGRENIylngrLLGLSRKEIDEK--FDEIVEFA--------ELGDFIdqpvKT----YSSGMRARLAFAVATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKKDF-TIVIVTHSMQQARRISDRtAFFLM-GELVEHNET 228
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDR-AIWLEkGRLVMDGDP 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-214 |
8.87e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.79 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmNDLIEGVTIkgkLDMDGtniYGNIDVAD------LRIR---VGM 87
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPDSGSI---LVRHD---GGWVDLAQaspreiLALRrrtIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 88 VFQKPNPFP-MSIYENVAYGLRAQGIKDKkyidevvESSLRSAALWD--EVKDRLkahaFGL-----SGGQQQRLCIART 159
Cdd:COG4778 98 VSQFLRVIPrVSALDVVAEPLLERGVDRE-------EARARARELLArlNLPERL----WDLppatfSGGEQQRVNIARG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFT-IVIVTHSMQQARRISDRT 214
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVADRV 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-205 |
1.03e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 84.30 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndLIEGVTIKGKLDMDGTNIYGNIDVADL---RIRVGMVFQKPNPF 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 96 PMSIYENVAYGLRAQGIKDKKYIDEV-VESSLRSAALWDEVKdrLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....
gi 1327251791 175 ALD-PIATHKIEE-LMEDLKKD-FTIVIVTHSMQ 205
Cdd:cd03290 170 ALDiHLSDHLMQEgILKFLQDDkRTLVLVTHKLQ 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-223 |
1.23e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndliEGVTIKGKLDMDGTNIYGNIDVADLRIRV 85
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-----DPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPNPFP-MSIYENVAYGlraQGIKDKKYIDEVVEsslRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEP 164
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMG---GFFAERDQFQERIK---WVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 165 DVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-225 |
1.31e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQ--ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEgvtikGKLDMDGTNIyGNIDVADLR 82
Cdd:PRK11160 340 TLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ-----GEILLNGQPI-ADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQKPNPFPMSIYENVAygLRAQGIKDKKYIDEVVESSLRSAAlwdEVKDRLKAHaFG-----LSGGQQQRLCIA 157
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLL--LAAPNASDEALIEVLQQVGLEKLL---EDDKGLNAW-LGeggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH---SMQQARRIsdrtafFLM--GELVEH 225
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltGLEQFDRI------CVMdnGQIIEQ 554
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-235 |
2.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKLDMDGTNIYGnidvadLRI 83
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGkVLVSGIDTGDFSKLQG------IRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNP--FPMSIYENVAYG---LRAQGIKDKKYIDEvvesslrsaALWDEVKDRLKAHA-FGLSGGQQQRLCIA 157
Cdd:PRK13644 78 LVGIVFQNPETqfVGRTVEEDLAFGpenLCLPPIEIRKRVDR---------ALAEIGLEKYRHRSpKTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQArRISDRTAFFLMGELVEHNETSVIFSEP 235
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-247 |
2.85e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKS-TLLRCLnRMNDLIEGVTIKGKLDMDGTNIYgNIDVA 79
Cdd:PRK15134 7 AIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPPVVYPSGDIRFHGESLL-HASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLR-IR---VGMVFQKP----NPF---PMSIYENVAY--GLRAQGIKDK--KYIDEVvesSLRSAAlwdevkDRLKAHAF 144
Cdd:PRK15134 85 TLRgVRgnkIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRREAARGEilNCLDRV---GIRQAA------KRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 145 GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKK--DFTIVIVTHSMQQARRISDRTAFFLMGEL 222
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250 260
....*....|....*....|....*
gi 1327251791 223 VEHNETSVIFSEPKDDRTKGYVNGD 247
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLNSE 260
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-225 |
3.13e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.11 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrMNDLIE-----GVTIKGKLDMDGTNIyGNIDVADL 81
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGggaprGARVTGDVTLNGEPL-AAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNP-FPMSIYENVAYG----LRAQG---IKDKKYIDEVVESSLRSAALWDEVKDrlkahafgLSGGQQQR 153
Cdd:PRK13547 82 ARLRAVLPQAAQPaFAFSAREIVLLGryphARRAGaltHRDGEIAWQALALAGATALVGRDVTT--------LSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 154 LCIARTIAM---------EPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVT--HSMQQARRISDRTAFFLMGEL 222
Cdd:PRK13547 154 VQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLADGAI 233
|
...
gi 1327251791 223 VEH 225
Cdd:PRK13547 234 VAH 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-213 |
3.26e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGK-LDMDGTNiygniDVADLRIrvGMVFQ 90
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGeILIDGKpVRIRSPR-----DAIALGI--GMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 91 KPNPFP-MSIYENVAYGL--RAQGIKDKKYIDEVVEsslrsaalwdEVKDR------LKAHAFGLSGGQQQRLCIARTIA 161
Cdd:COG3845 88 HFMLVPnLTVAENIVLGLepTKGGRLDRKAARARIR----------ELSERygldvdPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 162 MEPDVILMDEPTSALDPiatHKIEELMEDLKK----DFTIVIVTHSMQQARRISDR 213
Cdd:COG3845 158 RGARILILDEPTAVLTP---QEADELFEILRRlaaeGKSIIFITHKLREVMAIADR 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-224 |
3.84e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.97 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTniygnidVADLrIRVGMVFQ 90
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLR-------LLAGIYPpdSGTVTVRGR-------VSSL-LGLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 91 kPNpfpMSIYENVAYGLRAQGIKDK---KYIDEVVESSlrsaalwdEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:cd03220 97 -PE---LTGRENIYLNGRLLGLSRKeidEKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 168 LMDEPTSALDPIATHKIEELMEDLKKDFTIVI-VTHSMQQARRISDRTAFFLMGELVE 224
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-213 |
8.00e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtIKGKLDMDGTNIY-GNIDVA 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYM------------IVGLVKPDSGRIFlDGEDIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DL----RIRVGM--------VFQKpnpfpMSIYENVAYGLRAQGiKDKKYIDEVVESslrsaaLWDE-----VKDRLkah 142
Cdd:COG1137 69 HLpmhkRARLGIgylpqeasIFRK-----LTVEDNILAVLELRK-LSKKEREERLEE------LLEEfgithLRKSK--- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 143 AFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDR 213
Cdd:COG1137 134 AYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKeRGIGVLITDHNVRETLGICDR 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-239 |
8.55e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.85 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDL--IEGVTI---------------------- 61
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 62 ---KGKLDMDGTNIYGNIDV--ADLRIRVGMVFQKPnpFPM----SIYENVAYGLRAQGIKDKKYIDEVVEsslrsaaLW 132
Cdd:TIGR03269 83 pvcGGTLEPEEVDFWNLSDKlrRRIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAVD-------LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 133 DEVK--DRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQAR 208
Cdd:TIGR03269 154 EMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIE 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1327251791 209 RISDRTAFFLMGELVEHNETSVI-------FSEPKDDR 239
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVvavfmegVSEVEKEC 271
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-222 |
1.00e-18 |
|
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: 81.68 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTIK--GKLDMDGTNIYGNidvaDLRi 83
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLK-------MITGILRPtsGEIIFDGHPWTRK----DLH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP-MSIYENVAYGLRAQGIKDKKyIDEVvessLRSAALwdEVKDRLKAHAFGLsgGQQQRLCIARTIAM 162
Cdd:TIGR03740 71 KIGSLIESPPLYEnLTARENLKVHTTLLGLPDSR-IDEV----LNIVDL--TNTGKKKAKQFSL--GMKQRLGIAIALLN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGEL 222
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-213 |
1.32e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvTIKgkldMDGTNIYGnidVADLRI-R 84
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG-TIL----LRGQHIEG---LPGHQIaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMV--FQKPNPF-PMSIYEN--VAY------GLRAQGIKDKKYIDEVVESsLRSAALWDEVKDRLKA---HAFGLSGGQ 150
Cdd:PRK11300 80 MGVVrtFQHVRLFrEMTVIENllVAQhqqlktGLFSGLLKTPAFRRAESEA-LDRAATWLERVGLLEHanrQAGNLAYGQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 151 QQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
23-202 |
1.87e-18 |
|
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: 84.22 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 23 NLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGV--TIKGKLDMDGTNIyGNIDVADLRIRVGMVFQKPNPFPMSIY 100
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIAK-------LVAGLyqPWSGEILFDGIPR-EEIPREVLANSVAMVDQDIFLFEGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 101 ENVAyglraqgIKDKKYIDEVVESSLRSAALWDEVKDRLKAHAF-------GLSGGQQQRLCIARTIAMEPDVILMDEPT 173
Cdd:TIGR03796 571 DNLT-------LWDPTIPDADLVRACKDAAIHDVITSRPGGYDAelaeggaNLSGGQRQRLEIARALVRNPSILILDEAT 643
|
170 180 190
....*....|....*....|....*....|
gi 1327251791 174 SALDPiATHKIeeLMEDLKK-DFTIVIVTH 202
Cdd:TIGR03796 644 SALDP-ETEKI--IDDNLRRrGCTCIIVAH 670
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-245 |
1.89e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrMNDLIEGVTIKGKLDMDGTNIYgNIDVAD 80
Cdd:PRK09473 14 DVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREIL-NLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 L-RIR---VGMVFQKP----NPFpMSIYENVAYGLRAQGIKDKKyidEVVESSLR--SAALWDEVKDRLKAHAFGLSGGQ 150
Cdd:PRK09473 91 LnKLRaeqISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKA---EAFEESVRmlDAVKMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 151 QQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEHNET 228
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250
....*....|....*..
gi 1327251791 229 SVIFSEPKDDRTKGYVN 245
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLN 263
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-203 |
3.31e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmnDLIEGVTikGKLDMDGTniygniDVADL-----RIRVGMV 88
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA---SLISPTS--GTLLFEGE------DISTLkpeiyRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 89 FQKPNPFPMSIYENVA--YGLRAQGIKDKKYIDEVVESSLRSAALWDEVKDrlkahafgLSGGQQQRLCIARTIAMEPDV 166
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLERFALPDTILTKNIAE--------LSGGEKQRISLIRNLQFMPKV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327251791 167 ILMDEPTSALDPIATHKIEELMEDLKKDFTIVI--VTHS 203
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-225 |
5.51e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMDGtniyGNIDVADlRI 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA------------GELEPDS----GTVKLGE-TV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFP--MSIYENVAYGLraqgikdkkyiDEVVESSLRS---------AALWDEVKDrlkahafgLSGGQQQ 152
Cdd:COG0488 379 KIGYFDQHQEELDpdKTVLDELRDGA-----------PGGTEQEVRGylgrflfsgDDAFKPVGV--------LSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDpIAThkIEELmEDLKKDF--TIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLD-IET--LEAL-EEALDDFpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-202 |
1.02e-17 |
|
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: 77.10 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKldmdgtniygnidvadlRIRV 85
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------------TVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQkpnpfpmsiyenvayglraqgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIAMEPD 165
Cdd:cd03221 66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDLKKdfTIVIVTH 202
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-208 |
1.64e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.61 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYG---DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGkldmDGTNIyGNID 77
Cdd:PTZ00265 380 IKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNL-KDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 78 VADLRIRVGMVFQKPNPFPMSIYENVAYGLRAqgIKDKKYID-------------------------------------- 119
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYS--LKDLEALSnyynedgndsqenknkrnscrakcagdlndmsnttdsn 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 120 ---------------EVVESSLR------SAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDP 178
Cdd:PTZ00265 533 eliemrknyqtikdsEVVDVSKKvlihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270
....*....|....*....|....*....|..
gi 1327251791 179 IATHKIEELMEDLK--KDFTIVIVTHSMQQAR 208
Cdd:PTZ00265 613 KSEYLVQKTINNLKgnENRITIIIAHRLSTIR 644
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-202 |
3.48e-17 |
|
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: 77.18 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKLD---MDGTNIYGNIDVADL- 81
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK------------TIMGHPKyevTEGEILFKGEDITDLp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 ---RIRVG--MVFQKPNPFPmsiyenvayglraqGIKDKKYIDEVVEsslrsaalwdevkdrlkahafGLSGGQQQRLCI 156
Cdd:cd03217 71 peeRARLGifLAFQYPPEIP--------------GVKNADFLRYVNE---------------------GFSGGEKKRNEI 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327251791 157 ARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTH 202
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITH 162
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-202 |
3.59e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.08 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGV--TIKGKLDMDGTNIYgNIDVADLRIRVGMVFQKPNPFP 96
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLAR-------LIVGIwpPTSGSVRLDGADLK-QWDRETFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYENVAY---GLRAQGIKDKKYIDEVVESSLRSAALWDEVkdrLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPT 173
Cdd:TIGR01842 406 GTVAENIARfgeNADPEKIIEAAKLAGVHELILRLPDGYDTV---IGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190
....*....|....*....|....*....|
gi 1327251791 174 SALDPIATHKIEELMEDLKK-DFTIVIVTH 202
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
3.60e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdGTNIYGNIDVADLRIR-VGMVFQKPNPFP 96
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQ----PMSKLSSAAKAELRNQkLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 -MSIYENVAYGLRAQGIKDKKyIDEVVESSLRSAALWDEVKDRLKAhafgLSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:PRK11629 101 dFTALENVAMPLLIGKKKPAE-INSRALEMLAAVGLEHRANHRPSE----LSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327251791 176 LDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRIS 211
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-213 |
9.19e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 9.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtnIYGNIDVAD-LRI 83
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGtITINNI-------NYNKLDHKLaAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPF-PMSIYENVAYG-LRAQGIKDKKYIDeVVESSLRSAALWDEV--KDRLKAHAFGLSGGQQQRLCIART 159
Cdd:PRK09700 81 GIGIIYQELSVIdELTVLENLYIGrHLTKKVCGVNIID-WREMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFT-IVIVTHSMQQARRISDR 213
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDR 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-202 |
9.73e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQ-ALKSINLPIPTRQVTALIGPSGCGKSTLlrclnrmNDLIEG--VTIKGKLDMDGTNIyGNIDVADL 81
Cdd:PRK10790 342 DIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTL-------ASLLMGyyPLTEGEIRLDGRPL-SSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNPFPMSIYENVAYGlraQGIKDKKYID--EVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIART 159
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQalETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-204 |
2.95e-16 |
|
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: 78.06 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygnidvadlrirVGMVFQKP 92
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMKGS--------------------VAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSIYENVAYGlraQGIKDKKYidevvESSLRSAALWDEVK-----DRLKAHAFG--LSGGQQQRLCIARTIAMEPD 165
Cdd:TIGR00957 709 WIQNDSLRENILFG---KALNEKYY-----QQVLEACALLPDLEilpsgDRTEIGEKGvnLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327251791 166 VILMDEPTSALDP-IATHKIEELM--EDLKKDFTIVIVTHSM 204
Cdd:TIGR00957 781 IYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGI 822
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-222 |
3.40e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.75 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGkldmdGTNIYGNIDVadLRIRVGMVFQKPNPFP- 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-----GKDIETNLDA--VRQSLGMCPQHNILFHh 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYENVAYGLRAQGIKDKkyidevvESSLRSAALWDE--VKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWE-------EAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327251791 175 ALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGEL 222
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-223 |
8.52e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIkgkldMDGTNIYGNIDVADLRI 83
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-----LDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFPMSIYENVAYG-------LRAQGIKDKKYIDEVVesslrsaalwDEVKDRLKAHAF--GLSGGQQQRL 154
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGrypwhgaLGRFGAADREKVEEAI----------SLVGLKPLAHRLvdSLSGGERQRA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 155 CIARTIAMEPDVILMDEPTSALDpIAtHKIE--ELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALD-IA-HQVDvlALVHRLsqERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-212 |
1.09e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.65 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrMNDLIEGVTikGKLDMDGTNIYgNIDVADLRIR 84
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA---INGTLTPTA--GTVLVAGDDVE-ALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPN-PFPMSIYENVAYGlRAQGIKDKKYIDEVVESSLRSAAlwdevkDRLKAHAFG------LSGGQQQRLCIA 157
Cdd:PRK09536 79 VASVPQDTSlSFEFDVRQVVEMG-RTPHRSRFDTWTETDRAAVERAM------ERTGVAQFAdrpvtsLSGGERQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 158 RTIAMEPDVILMDEPTSALDpiATHKIE--ELMEDLKKD-FTIVIVTHSMQQARRISD 212
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD--INHQVRtlELVRRLVDDgKTAVAAIHDLDLAARYCD 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-203 |
1.94e-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: 71.42 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQAL-KSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIegvtiKGKLDM-DGTNIYgnidvadlri 83
Cdd:cd03223 3 LENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGMpEGEDLL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 rvgMVFQKPnpfpmsiyenvayglraqgikdkkYIdevVESSLRSAAL--WDEVkdrlkahafgLSGGQQQRLCIARTIA 161
Cdd:cd03223 68 ---FLPQRP------------------------YL---PLGTLREQLIypWDDV----------LSGGEQQRLAFARLLL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLKkdFTIVIVTHS 203
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-202 |
2.71e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliegvtikgkldMDGTNIYGNIDVADlrirvgmvfqkpNPFP-- 96
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA--------------LKGTPVAGCVDVPD------------NQFGre 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 MSIYENVAyglRAQGIKDKKYIDEVVesSLRSAALWdevKDRLKAhafgLSGGQQQRLCIARTIAMEPDVILMDEPTSAL 176
Cdd:COG2401 100 ASLIDAIG---RKGDFKDAVELLNAV--GLSDAVLW---LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|
gi 1327251791 177 DP----IATHKIEELMEDLKKdfTIVIVTH 202
Cdd:COG2401 168 DRqtakRVARNLQKLARRAGI--TLVVATH 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-241 |
3.80e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQ----ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGKLDMDGTNiYGNIDVADL 81
Cdd:PRK10261 15 VENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS-RQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 ------RIR---VGMVFQKP----NP-FPMSiyENVAYGLRA-QGIKDkkyidevvESSLRSAA-LWDEVK-----DRLK 140
Cdd:PRK10261 94 saaqmrHVRgadMAMIFQEPmtslNPvFTVG--EQIAESIRLhQGASR--------EEAMVEAKrMLDQVRipeaqTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 141 AHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFT--IVIVTHSMQQARRISDRTAFFL 218
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMY 243
|
250 260
....*....|....*....|...
gi 1327251791 219 MGELVEHNETSVIFSEPKDDRTK 241
Cdd:PRK10261 244 QGEAVETGSVEQIFHAPQHPYTR 266
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-209 |
4.32e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEGVTI--KGKLDMDGtniyGNIDVADLRI 83
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEVLG----GDMADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVG-----MvfqkP-----NPFP-MSIYENVA-----YGLRAQgiKDKKYIDEVvessLRSAALwDEVKDRLkahAFGLS 147
Cdd:NF033858 73 AVCpriayM----PqglgkNLYPtLSVFENLDffgrlFGQDAA--ERRRRIDEL----LRATGL-APFADRP---AGKLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 148 GGQQQR--LCIArtIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD---FTIVIVTHSMQQARR 209
Cdd:NF033858 139 GGMKQKlgLCCA--LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-202 |
4.93e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.98 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVtIKgkldmdgtniYGNIDVADLRI-----RVGMVF 89
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD-IR----------FHDIPLTKLQLdswrsRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 90 QKPNPFPMSIYENVAYG---LRAQGIKDKKYIDEVVESSLRSAALWD-EVKDRlkahAFGLSGGQQQRLCIARTIAMEPD 165
Cdd:PRK10789 396 QTPFLFSDTVANNIALGrpdATQQEIEHVARLASVHDDILRLPQGYDtEVGER----GVMLSGGQKQRISIARALLLNAE 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-241 |
5.04e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.24 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDN----QALKSINLPIPTRQVTALIGPSGCGKStlLRCLNRMNdLIE--GVTIKGKLDMDGTNIYg 74
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMG-LIDypGRVMAEKLEFNGQDLQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 75 NIDVADLRIRVG----MVFQKP----NPFPMSIYEnVAYGLRA-QGIKDKKYIDEVVESsLRSAALWDEvKDRLKAHAFG 145
Cdd:PRK11022 77 RISEKERRNLVGaevaMIFQDPmtslNPCYTVGFQ-IMEAIKVhQGGNKKTRRQRAIDL-LNQVGIPDP-ASRLDVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL--KKDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250
....*....|....*...
gi 1327251791 224 EHNETSVIFSEPKDDRTK 241
Cdd:PRK11022 234 ETGKAHDIFRAPRHPYTQ 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-205 |
1.14e-14 |
|
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: 71.42 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFY--GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliegVTIKGKLDMDGTNiYGNIDVADLRI 83
Cdd:cd03289 5 VKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS-WNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNPFPMSIYENV-AYGLRaqgiKDKKYIDEVVESSLRSA--ALWDEVKDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLdPYGKW----SDEEIWKVAEEVGLKSVieQFPGQLDFVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQ 205
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-231 |
3.94e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIYGNIDVADLRIRVGMVFQKPNPFP 96
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMK-------IIAGIVPpdSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 97 -MSIYENVAYGLrAQGIKDKKyidevvesslRSAALWDEVKDRLKAH--AFGLSGGQQQRLCIARTIAMEPDVILMDEPT 173
Cdd:PRK15439 100 nLSVKENILFGL-PKRQASMQ----------KMKQLLAALGCQLDLDssAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 174 SALDPIATH----KIEELmedLKKDFTIVIVTHSMQQARRISDRT------AFFLMGELVEHNETSVI 231
Cdd:PRK15439 169 ASLTPAETErlfsRIREL---LAQGVGIVFISHKLPEIRQLADRIsvmrdgTIALSGKTADLSTDDII 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-210 |
4.53e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLlrcLNRMNDLIEGvtiKGKLDMDGTNIyGNIDVADL-RIRVGMVFQKPNPFPMSIYENVAYGLR 108
Cdd:COG4138 23 ELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPL-SDWSAAELaRHRAYLSQQQSPPFAMPVFQYLALHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 109 AQGikDKKYIDEVVESSLRSAALwdevKDRLKAHAFGLSGGQQQRLCIARTI-----AMEPD--VILMDEPTSALDpIAt 181
Cdd:COG4138 96 AGA--SSEAVEQLLAQLAEALGL----EDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLD-VA- 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1327251791 182 HKIeeLMEDLKKDF-----TIVI----VTHSMQQARRI 210
Cdd:COG4138 168 QQA--ALDRLLRELcqqgiTVVMsshdLNHTLRHADRV 203
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-193 |
4.53e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.42 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCL-NRMNDlieGVtIKGKLDMDGTNIygnidVADLRIRVGMVFQKP 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTA---GV-ITGEILINGRPL-----DKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSiyenvayglraqgikdkkyidEVVESSLRSAALwdevkdRlkahafGLSGGQQQRLCIARTIAMEPDVILMDEP 172
Cdd:cd03232 89 VHSPNL---------------------TVREALRFSALL------R------GLSVEQRKRLTIGVELAAKPSILFLDEP 135
|
170 180
....*....|....*....|.
gi 1327251791 173 TSALDPIATHKIeelMEDLKK 193
Cdd:cd03232 136 TSGLDSQAAYNI---VRFLKK 153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-229 |
4.93e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.52 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 7 ENLDLfygdnqALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIyGNIDVADLRIRVG 86
Cdd:TIGR00957 1296 EDLDL------VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI-AKIGLHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 87 MVFQKPNPFPMSIYENV-AYGlraqgikdkKYIDEVVESSLRSAALWDEVK---DRLKAH-AFG---LSGGQQQRLCIAR 158
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLdPFS---------QYSDEEVWWALELAHLKTFVSalpDKLDHEcAEGgenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQarrISDRTAFFLM--GELVEHNETS 229
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTRVIVLdkGEVAEFGAPS 1504
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-234 |
5.52e-14 |
|
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: 70.99 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVT--IKGKLDMDGTNIYgnIDVADLRIR--------VG 86
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK-------IIAGVLepTSGEVNVRVGDEW--VDMTKPGPDgrgrakryIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 87 MVFQKPNPFP-MSIYENVAYGLRAQGIKDKKYIDEVVesSLRSAALWDE-VKDRLKAHAFGLSGGQQQRLCIARTIAMEP 164
Cdd:TIGR03269 369 ILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAVI--TLKMVGFDEEkAEEILDKYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 165 DVILMDEPTSALDPIA----THKIEELMEDLKKDFtiVIVTHSMQQARRISDRTAFFLMGELVEHNETSVIFSE 234
Cdd:TIGR03269 447 RIVILDEPTGTMDPITkvdvTHSILKAREEMEQTF--IIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-248 |
1.53e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVTIK--GKLDMDGTNIYGNIDV 78
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFY-------MVVGIVPRdaGNIIIDDEDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVGMVFQKPNPFP-MSIYENVAYGLRaqgIKDKKYIDEVVEsslRSAALWDE-----VKDRLKAhafGLSGGQQQ 152
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRrLSVYDNLMAVLQ---IRDDLSAEQRED---RANELMEEfhiehLRDSMGQ---SLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNETSVI 231
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
250
....*....|....*..
gi 1327251791 232 FSEPKDDRTkgYVNGDF 248
Cdd:PRK10895 225 LQDEHVKRV--YLGEDF 239
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-202 |
2.08e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrMNdlIEGVTI-KGKLDMDGTNIyGNIDVaDLRIR 84
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MG--HPKYEVtSGSILLDGEDI-LELSP-DERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VG--MVFQKPNPFP-MSiyenVAYGLRAQgikdkkyIDEVVESSLRSAALWDEVKDRLK----AHAF-------GLSGGQ 150
Cdd:COG0396 77 AGifLAFQYPVEIPgVS----VSNFLRTA-------LNARRGEELSAREFLKLLKEKMKelglDEDFldryvneGFSGGE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 151 QQRLCIARTIAMEPDVILMDEPTSALDpIATHKI--EELMEDLKKDFTIVIVTH 202
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLD-IDALRIvaEGVNKLRSPDRGILIITH 198
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-213 |
2.15e-13 |
|
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: 67.36 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMDGtniyGNIDVADLR---------I 83
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS------------GLLQPTS----GEVRVAGLVpwkrrkkflR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQKPNP--FPMSIYENVAYGLRAQGIKDKKY---IDEVVEsslrsaALwdEVKDRLKAHAFGLSGGQQQRLCIAR 158
Cdd:cd03267 95 RIGVVFGQKTQlwWDLPVIDSFYLLAAIYDLPPARFkkrLDELSE------LL--DLEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSMQQARRISDR 213
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARR 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-213 |
5.85e-13 |
|
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: 65.15 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIYGNID-----VADLRIRVGMVFQk 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGeITLDGK-PVTRRSPRDAIRagiayVPEDRKREGLVLD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 pnpfpMSIYENVAygLRAQgikdkkyidevvesslrsaalwdevkdrlkahafgLSGGQQQRLCIARTIAMEPDVILMDE 171
Cdd:cd03215 93 -----LSVAENIA--LSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 172 PTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDR 173
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-201 |
9.87e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRCLnrMNDLIEGVTIKGKLDMDGTNIygniDVADLRIRVGMVFQKPNPFPM-SIYENVAYG----L 107
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTlTVREHLMFQahlrM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 108 RAQGIKDKKY--IDEVVES-SLRSAA-LWDEVKDRLKahafGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHK 183
Cdd:TIGR00955 129 PRRVTKKEKRerVDEVLQAlGLRKCAnTRIGVPGRVK----GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170
....*....|....*...
gi 1327251791 184 IEELMEDLKKDFTIVIVT 201
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICT 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
1.29e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmnDLIegvtikgkLDmDGTNIY-GNIDVA 79
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG--EVL--------LD-DGRIIYeQDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRirvgmvfQKPnpfPM----SIYENVAYGLRAQGIKDKKY--IDEVVESS---------------LRSAALW---DEV 135
Cdd:PRK11147 70 RLQ-------QDP---PRnvegTVYDFVAEGIEEQAEYLKRYhdISHLVETDpseknlnelaklqeqLDHHNLWqleNRI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 136 KDRLK-----AHAF--GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDpIAThkIEELmEDLKKDF--TIVIVTH---- 202
Cdd:PRK11147 140 NEVLAqlgldPDAAlsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWL-EGFLKTFqgSIIFISHdrsf 215
|
250
....*....|..
gi 1327251791 203 --SMqqARRISD 212
Cdd:PRK11147 216 irNM--ATRIVD 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-234 |
1.41e-12 |
|
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: 65.32 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFYGDN--QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGvtikgKLDMDGTNIyGNIDVAD 80
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDG-----KIVIDGIDI-SKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFPMSIYENVAyglraqgiKDKKYIDEVVESSLRSAALwdevKDRLKAHAFGL-----------SGG 149
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLD--------PECKCTDDRLWEALEIAQL----KNMVKSLPGGLdavvteggenfSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 150 QQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVEHNETS 229
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPE 239
|
....*
gi 1327251791 230 VIFSE 234
Cdd:cd03288 240 NLLAQ 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-225 |
1.51e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgTNIYGNIdVADLRIRVGMVFQKPNPF 95
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGsILIDGQ-----EMRFAST-TAALAAGVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 96 P-MSIYENVAYGLRAQ--GIKDKKYIdeVVESSLRSAALWDEV--KDRLKAhafgLSGGQQQRLCIARTIAMEPDVILMD 170
Cdd:PRK11288 92 PeMTVAENLYLGQLPHkgGIVNRRLL--NYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 171 EPTSALDPIATHKIEELMEDLKKDFTIVI-VTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-205 |
2.35e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.47 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFY--GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMndliegVTIKGKLDMDGTNiYGNIDVAD 80
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDGVS-WNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 LRIRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVvesSLRSA--ALWDEVKDRLKAHAFGLSGGQQQRLCIAR 158
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEV---GLKSVieQFPDKLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327251791 159 TIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQ 205
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-203 |
9.13e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRclnrmndLIEGV--TIKGKLDMDGtniyGNIDVADLRIRV-------GMvfqKPNpfpMSIY 100
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLR-------LIAGLlpPAAGTIKLDG----GDIDDPDVAEAChylghrnAM---KPA---LTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 101 ENVAY--GLRAQGikdkkyiDEVVESSLRSAALwDEVKDRlkahAFG-LSGGQQQRLCIARTIAMEPDVILMDEPTSALD 177
Cdd:PRK13539 92 ENLEFwaAFLGGE-------ELDIAAALEAVGL-APLAHL----PFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 1327251791 178 PIATHKIEELMED-LKKDFTIVIVTHS 203
Cdd:PRK13539 160 AAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-202 |
6.70e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMND--LIEG-VTIKGK--LDMDGTNIYGNidva 79
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGtVEFKGKdlLELSPEDRAGE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 dlriRVGMVFQKP-------NPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRsaaLWDEVKDRL-KAHAFGLSGGQQ 151
Cdd:PRK09580 79 ----GIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIA---LLKMPEDLLtRSVNVGFSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 152 QRLCIARTIAMEPDVILMDEPTSALD----PIATHKIEELmEDLKKDFtiVIVTH 202
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDidalKIVADGVNSL-RDGKRSF--IIVTH 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-202 |
7.53e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNqALKSINLPIPTR-QVTALIGPSGCGKSTLLRCLN-----RMNDLIEGVTIKGKLDM-DGTNIYGNI-DVADLRIR 84
Cdd:PRK13409 83 YGVN-GFKLYGLPIPKEgKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEPSWDEVLKRfRGTELQNYFkKLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQKPNPFPMSIYENVAYGLRaqGIKDKKYIDEVVESsLRSAALWD-EVKDrlkahafgLSGGQQQRLCIARTIAME 163
Cdd:PRK13409 162 VVHKPQYVDLIPKVFKGKVRELLK--KVDERGKLDEVVER-LGLENILDrDISE--------LSGGELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*....
gi 1327251791 164 PDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTH 202
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-203 |
2.23e-10 |
|
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: 60.15 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQAL-KSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKgklDMDGTNIYgnidvad 80
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---PAKGKLFY------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 81 lrirvgmVFQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESSLRSAAL---------WDEVKDRLKAhafgLSGGQQ 151
Cdd:TIGR00954 520 -------VPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDV----LSGGEK 588
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 152 QRLCIARTIAMEPDVILMDEPTSALDPiathKIEELMEDLKKDFTIVIVTHS 203
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVS 636
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-249 |
2.41e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 1 MNKFDIENLDLFY----GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndlIEGVTiKGKLDMDGTNI-YGN 75
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKA-------ICGVT-KDNWRVTADRMrFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 76 IDVADLRIR---------VGMVFQKPNPFpMSIYENVAYGLrAQGIKDKKY----IDEVVESSLRSAALWDEV-----KD 137
Cdd:PRK15093 73 IDLLRLSPRerrklvghnVSMIFQEPQSC-LDPSERVGRQL-MQNIPGWTYkgrwWQRFGWRKRRAIELLHRVgikdhKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 138 RLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD--FTIVIVTHSMQQARRISDRTA 215
Cdd:PRK15093 151 AMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKIN 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 1327251791 216 FFLMGELVEHNETSVIFSEPKDDRTKGYVNG--DFG 249
Cdd:PRK15093 231 VLYCGQTVETAPSKELVTTPHHPYTQALIRAipDFG 266
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-210 |
3.00e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndliegvtikgkldMDGTNIYGNIDVADLRIRVGMVFQKPNP 94
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISA------------------MLGELSHAETSSVVIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYENVAYGLRAQGIKDKKYID-EVVESSLRSAALWD--EVKDRlkahAFGLSGGQQQRLCIARTIAMEPDVILMDE 171
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDvTALQHDLDLLPGRDltEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 172 PTSALDPIATHKI-EELMEDLKKDFTIVIVT---HSMQQARRI 210
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTnqlHFLPLMDRI 809
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-177 |
3.66e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLlrcLNRMNDLIEGvtiKGKLDMDGTNIyGNIDVADL-RIRVGMVFQKPNPFPMSIYENVAYGLRAQGI 112
Cdd:PRK03695 27 LVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPL-EAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTLHQPDKTR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 113 KD--KKYIDEVVEsSLRsaalwdeVKDRLKAHAFGLSGGQQQR-------LCIARTIAMEPDVILMDEPTSALD 177
Cdd:PRK03695 100 TEavASALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLD 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-225 |
4.52e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 10 DLFY--GDNQ---ALKSINLPIPTRQVTALIGPSGCGKSTLlrclnrmNDLIEGVTI--KGKLDMDGTniygnidVADLR 82
Cdd:PRK13545 26 DLFFrsKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTL-------SNLIAGVTMpnKGTVDIKGS-------AALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRVGMVFQkpnpfpMSIYENVAYGLRAQGIKdKKYIDEVVESSLRSAALWDEVKDRLKAHafglSGGQQQRLCIARTIAM 162
Cdd:PRK13545 92 ISSGLNGQ------LTGIENIELKGLMMGLT-KEKIKEIIPEIIEFADIGKFIYQPVKTY----SSGMKSRLGFAISVHI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELVEH 225
Cdd:PRK13545 161 NPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEY 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-210 |
4.77e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLrclNRMNDLIEGVTIKGKLDMDGTNIYGNIdvadLRiRVGMVFQKPNPFP-MSIYENVAYG-- 106
Cdd:PLN03211 95 EILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQI----LK-RTGFVTQDDILYPhLTVRETLVFCsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 107 LRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHAF--GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKI 184
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELGL-TKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|....*..
gi 1327251791 185 EELMEDL-KKDFTIVIVTHsmQQARRI 210
Cdd:PLN03211 246 VLTLGSLaQKGKTIVTSMH--QPSSRV 270
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-205 |
5.49e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndliegvtiKGKLDMDGTniygnidvadlRI 83
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM------------LGQLQADSG-----------RI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 84 RVGMVFQkpnpfpmsiyenVAY--GLRAQGIKDKKYIDEVVESSlrsaalwDEV----KDRlkaHAFG------------ 145
Cdd:PRK11147 377 HCGTKLE------------VAYfdQHRAELDPEKTVMDNLAEGK-------QEVmvngRPR---HVLGylqdflfhpkra 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 146 ------LSGGQQQRLCIARTIAMEPDVILMDEPTSALDpiathkIE--ELMEDLKKDF--TIVIVTHSMQ 205
Cdd:PRK11147 435 mtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLD------VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
96-213 |
5.52e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 96 PMSIYENVAYGLRAQ----GIKDKKYIDEVVES-----SLRSAALWDEVKDrlkahafgLSGGQQQRLCIARTIAMEPDV 166
Cdd:COG1129 344 DLSIRENITLASLDRlsrgGLLDRRRERALAEEyikrlRIKTPSPEQPVGN--------LSGGNQQKVVLAKWLATDPKV 415
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1327251791 167 ILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLSDR 463
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-202 |
1.33e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.96 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCL--NRMNDLIEG-VTIKGK--LDMDgtniygnidv 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGdILFKGEsiLDLE---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 79 ADLRIRVG--MVFQKPNPFPMSIYEN---VAYGLR--AQGIKDK------KYIDEVVE-SSLRSAALWDEVKDrlkahaf 144
Cdd:CHL00131 78 PEERAHLGifLAFQYPIEIPGVSNADflrLAYNSKrkFQGLPELdpleflEIINEKLKlVGMDPSFLSRNVNE------- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 145 GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTH 202
Cdd:CHL00131 151 GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITH 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
140-229 |
1.35e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 140 KAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFF- 217
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMs 465
|
90
....*....|....
gi 1327251791 218 --LMGELVEHNETS 229
Cdd:PRK10982 466 ngLVAGIVDTKTTT 479
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-239 |
1.93e-09 |
|
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: 56.79 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 16 NQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrMNDLIEGVTIKGKLDMDGtniygnidvadlriRVGMVFQKPNPF 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLL-----MLILGELEPSEGKIKHSG--------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 96 PMSIYENVAYGLRAQGIKDKKYIDEV-VESSLrsAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACqLEEDI--TKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 175 ALDpIATHK--IEELMEDLKKDFTIVIVTHSMQQARRiSDRTafflmgeLVEHNETSVI---FSEPKDDR 239
Cdd:cd03291 189 YLD-VFTEKeiFESCVCKLMANKTRILVTSKMEHLKK-ADKI-------LILHEGSSYFygtFSELQSLR 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-209 |
2.14e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLrclnrMNDLIEGVTIKGKLDMDGtniygnidvadlriRVGMVFQKPNPFPMS 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLL-----MMIMGELEPSEGKIKHSG--------------RISFSPQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 99 IYENVAYGLRaqgikdkkyIDEVVESSLRSAALWDE------VKDR--LKAHAFGLSGGQQQRLCIARTIAMEPDVILMD 170
Cdd:TIGR01271 503 IKDNIIFGLS---------YDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1327251791 171 EPTSALDPIATHKI-EELMEDLKKDFTIVIVTHSMQQARR 209
Cdd:TIGR01271 574 SPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-210 |
2.25e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 14 GDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKL-DMDGTNIYgnidvadLRIRVGMVFQKP 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS------------AMLGELpPRSDASVV-------IRGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSIYENVAYGLRAQGIKDKKYIDevVESSLRSAALW-----DEVKDRlkahAFGLSGGQQQRLCIARTIAMEPDVI 167
Cdd:PLN03130 689 WIFNATVRDNILFGSPFDPERYERAID--VTALQHDLDLLpggdlTEIGER----GVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1327251791 168 LMDEPTSALDP-IATHKIEELMEDLKKDFTIVIVT---HSMQQARRI 210
Cdd:PLN03130 763 IFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVDRI 809
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
33-211 |
2.99e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.06 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRclnrmndLIEGVTI--KGKLDMDGTNIYgniDVADLRIRV--------GMvfqKPNpfpMSIYEN 102
Cdd:TIGR01189 30 QVTGPNGIGKTTLLR-------ILAGLLRpdSGEVRWNGTPLA---EQRDEPHENilylghlpGL---KPE---LSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 103 VAYgLRAqgikDKKYIDEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATH 182
Cdd:TIGR01189 94 LHF-WAA----IHGGAQRTIEDALAAVGL-TGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|...
gi 1327251791 183 KIEELMED-LKKDFTIVIVTH---SMQQARRIS 211
Cdd:TIGR01189 165 LLAGLLRAhLARGGIVLLTTHqdlGLVEARELR 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-202 |
3.00e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrMNDLiegvtikgkldmdgTNIYGNIDVADl 81
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGEL--------------EPDSGTVKWSE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKPNP-FP--MSIYENVAYglraqgIKDKKYIDEVVESSL-RSAALWDEVKDRLKAhafgLSGGQQQRLCIA 157
Cdd:PRK15064 381 NANIGYYAQDHAYdFEndLTLFDWMSQ------WRQEGDDEQAVRGTLgRLLFSQDDIKKSVKV----LSGGEKGRMLFG 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327251791 158 RTIAMEPDVILMDEPTSALDpiaTHKIEELMEDLKK-DFTIVIVTH 202
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD---MESIESLNMALEKyEGTLIFVSH 493
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-214 |
3.36e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtniygNIDVADLRIRVGMVFQKPN--- 93
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkISILGQ----------PTRQALQKNLVAYVPQSEEvdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 94 PFPMSIYENVAYG-------LRAQGIKDKkyidEVVESSLRSAALWDevkdrLKAHAFG-LSGGQQQRLCIARTIAMEPD 165
Cdd:PRK15056 92 SFPVLVEDVVMMGryghmgwLRRAKKRDR----QIVTAALARVDMVE-----FRHRQIGeLSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 166 VILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRT 214
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYT 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-202 |
5.64e-09 |
|
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: 55.95 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNqALKSINLPIPTR-QVTALIGPSGCGKSTLLRCLNrmndlieGVTIK--GKLDMD-----------GTNIYGNI-D 77
Cdd:COG1245 83 YGEN-GFRLYGLPVPKKgKVTGILGPNGIGKSTALKILS-------GELKPnlGDYDEEpswdevlkrfrGTELQDYFkK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 78 VADLRIRVGMVFQKPNPFPMSIYENVAYGLRaqGIKDKKYIDEVVESsLRSAALWD-EVKDrlkahafgLSGGQQQRLCI 156
Cdd:COG1245 155 LANGEIKVAHKPQYVDLIPKVFKGTVRELLE--KVDERGKLDELAEK-LGLENILDrDISE--------LSGGELQRVAI 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327251791 157 ARTIAMEPDVILMDEPTSALD---PIATHK-IEELMEDLKkdfTIVIVTH 202
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDiyqRLNVARlIRELAEEGK---YVLVVEH 270
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-232 |
6.79e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 27 PTRQVtALIGPSGCGKSTLLRCLNRMNDLIegvtiKGKLDMDGTNIyGNIDVADLRIRVGMVFQKPNPFPMSIYENvayg 106
Cdd:PLN03232 1261 PSEKV-GVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDV-AKFGLTDLRRVLSIIPQSPVLFSGTVRFN---- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 107 lraqgikdkkyIDEVVESSlrSAALWD-----EVKDRLKAHAFGL-----------SGGQQQRLCIARTIAMEPDVILMD 170
Cdd:PLN03232 1330 -----------IDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 171 EPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQQARRiSDRTAFFLMGELVEH--------NETSVIF 232
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYdspqellsRDTSAFF 1465
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
31-184 |
1.34e-08 |
|
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: 53.42 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 31 VTALIGPSGCGKSTLLRCLNrmNDLIEGVTIKGKLdmdgtnIYGNIDVADLRirvgmvfqkpNPFPMSIYENVAyglraq 110
Cdd:cd03233 35 MVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDI------HYNGIPYKEFA----------EKYPGEIIYVSE------ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 111 giKDKKYIDEVVESSLRSAAlwdevkdRLKAHAF--GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKI 184
Cdd:cd03233 91 --EDVHFPTLTVRETLDFAL-------RCKGNEFvrGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-212 |
1.63e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.45 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTIKGklDMDGTNIYGNIDVADLRIR------VG 86
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS-------GVYPHG--TWDGEIYWSGSPLKASNIRdteragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 87 MVFQKPNPFP-MSIYENVAYGlraQGIKDKKYIDEVVESSLRSAALWDEVK---DRLKAHAFGLSGGQQQRLCIARTIAM 162
Cdd:TIGR02633 82 IIHQELTLVPeLSVAENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 163 EPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISD 212
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKaHGVACVYISHKLNEVKAVCD 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-202 |
1.87e-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: 54.56 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLLRclnrmndliegvtIKGKLDMDgtniYGNIDVADLRIRVGMVFQKPNPFP-MSIYENVAYGLRAqgI 112
Cdd:TIGR03719 36 VLGLNGAGKSTLLR-------------IMAGVDKD----FNGEARPQPGIKVGYLPQEPQLDPtKTVRENVEEGVAE--I 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 113 KDK---------KYIDEV------------VESSLRSAALWD-EVKDRLKAHAF----------GLSGGQQQRLCIARTI 160
Cdd:TIGR03719 97 KDAldrfneisaKYAEPDadfdklaaeqaeLQEIIDAADAWDlDSQLEIAMDALrcppwdadvtKLSGGERRRVALCRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKdfTIVIVTH 202
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-224 |
2.68e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFygDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIYGNIdvadlr 82
Cdd:PRK09700 266 FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGeIRLNGK-DISPRSPLDAV------ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 iRVGMVFQKPNP-----FP-MSIYENVAYglrAQGIKDKKY------IDEVVESSLRSAAlwdEVKDRLKAHAFG----- 145
Cdd:PRK09700 337 -KKGMAYITESRrdngfFPnFSIAQNMAI---SRSLKDGGYkgamglFHEVDEQRTAENQ---RELLALKCHSVNqnite 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELVE 224
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-223 |
2.69e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLN--------RMNDLIEGVTIKGKLDMDGTNIygnidvadlrirvGMV 88
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTgiytrdagSILYLGKEVTFNGPKSSQEAGI-------------GII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 89 FQKPNPFP-MSIYENVAYGL----RAQGIKDKKYIDEvvesslrSAALWDEVKDRLKAHAF--GLSGGQQQRLCIARTIA 161
Cdd:PRK10762 85 HQELNLIPqLTIAENIFLGRefvnRFGRIDWKKMYAE-------ADKLLARLNLRFSSDKLvgELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 162 MEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:PRK10762 158 FESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-202 |
3.33e-08 |
|
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: 52.11 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRclnrmndLIEGVTIK--GKLDMDGTniygnidvadlrirvGMVFQKPnpfpmSIYENVAYGL 107
Cdd:cd03231 27 EALQVTGPNGSGKTTLLR-------ILAGLSPPlaGRVLLNGG---------------PLDFQRD-----SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 108 RAQGIKDKKYI------------DEVVESSLRSAALwDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSA 175
Cdd:cd03231 80 HAPGIKTTLSVlenlrfwhadhsDEQVEEALARVGL-NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 1327251791 176 LDPIATHKIEELM-EDLKKDFTIVIVTH 202
Cdd:cd03231 156 LDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-212 |
3.88e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTIK--GKLDMDGTNIYGNIDVADLRIRVGMVFQKPNP 94
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLF-------GIYQKdsGSILFQGKEIDFKSSKEALENGISMVHQELNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 F-PMSIYENV---AYGLRAQGIKDKKYIDEvvesslrSAALWDEVKDRL--KAHAFGLSGGQQQRLCIARTIAMEPDVIL 168
Cdd:PRK10982 85 VlQRSVMDNMwlgRYPTKGMFVDQDKMYRD-------TKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1327251791 169 MDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISD 212
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCD 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-234 |
3.94e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDliegvTIKGKLDMDGTNIyGNIDVADLRIRVGMVFQKPNPFPMS 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREI-GAYGLRELRRQFSMIPQDPVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 99 IYENVayglraqgikdkkyiDEVVESSlrSAALWDEV-----KDRLKAHAFGL-----------SGGQQQRLCIARTIAM 162
Cdd:PTZ00243 1400 VRQNV---------------DPFLEAS--SAEVWAALelvglRERVASESEGIdsrvleggsnySVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 163 E-PDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHSMQ---QARRI--SDRTAFFLMG---ELVEHneTSVIFS 233
Cdd:PTZ00243 1463 KgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHtvaQYDKIivMDHGAVAEMGsprELVMN--RQSIFH 1540
|
.
gi 1327251791 234 E 234
Cdd:PTZ00243 1541 S 1541
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-213 |
4.05e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRCLnrmndliegvtiKGKLDMDGTNIYGNIDVAdlrirvgmvfQKPnpfpmsiyenvayglra 109
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLL------------AGVLKPDEGEVDPELKIS----------YKP----------------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 110 QGIKDKKyiDEVVESSLRSAA-------LWDEVKDRLKAHAF------GLSGGQQQRLCIARTIAMEPDVILMDEPTSAL 176
Cdd:PRK13409 407 QYIKPDY--DGTVEDLLRSITddlgssyYKSEIIKPLQLERLldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327251791 177 DP----IATHKIEELMEdlKKDFTIVIVTHSMQQARRISDR 213
Cdd:PRK13409 485 DVeqrlAVAKAIRRIAE--EREATALVVDHDIYMIDYISDR 523
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
146-213 |
4.27e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 4.27e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDR 464
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-213 |
4.51e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLLRclnrmndLIEGVTIK--GKLDMDGTNIygNIDVADLRIRVGMVF-----QKPNPFPM-SIYENVA- 104
Cdd:PRK11288 284 LFGLVGAGRSELMK-------LLYGATRRtaGQVYLDGKPI--DIRSPRDAIRAGIMLcpedrKAEGIIPVhSVADNINi 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 105 ----YGLRAQGIKDKKYIDEVVESSLRSAAlwdeVKDRLKAHAFG-LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPI 179
Cdd:PRK11288 355 sarrHHLRAGCLINNRWEAENADRFIRSLN----IKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190
....*....|....*....|....*....|....*
gi 1327251791 180 ATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDR 213
Cdd:PRK11288 431 AKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADR 465
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-211 |
5.07e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 35 IGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIygnidvaDLRIRVGMVFQKpnpFpmSIYE------NVA--- 104
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGeAWLFGQ-PVDAGDI-------ATRRRVGYMSQA---F--SLYGeltvrqNLElha 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 105 --YGLRAQGIKdkKYIDEVVES-SLRsaalwdEVKDRLKAhafGLSGGQQQRLCIArtIAM--EPDVILMDEPTSALDPI 179
Cdd:NF033858 365 rlFHLPAAEIA--ARVAEMLERfDLA------DVADALPD---SLPLGIRQRLSLA--VAVihKPELLILDEPTSGVDPV 431
|
170 180 190
....*....|....*....|....*....|....*..
gi 1327251791 180 ATHKIEELMEDL--KKDFTIVIVTHSMQQA-R--RIS 211
Cdd:NF033858 432 ARDMFWRLLIELsrEDGVTIFISTHFMNEAeRcdRIS 468
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-217 |
5.76e-08 |
|
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: 52.03 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRCLnrmndliegvtiKGKLDMDGtniyGNIDVAdlrirVGMVFQKPN----PFPMSIYENVAy 105
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKML------------AGVLKPDE----GDIEIE-----LDTVSYKPQyikaDYEGTVRDLLS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 106 glraqGIKDKKYIDEVVESSLRSAALWDEVKDRLKAHafgLSGGQQQRLCIARTIAMEPDVILMDEPTSALDP----IAT 181
Cdd:cd03237 84 -----SITKDFYTHPYFKTEIAKPLQIEQILDREVPE---LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMAS 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327251791 182 HKIEELMEDLKKdfTIVIVTHSMQQARRISDRTAFF 217
Cdd:cd03237 156 KVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVF 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
145-222 |
6.29e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 6.29e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 145 GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHS-MQQARRISDRTAFFLMGEL 222
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSdLEEIEQMADRVLVMHQGEI 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
138-228 |
8.15e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 138 RLKAHAF-------GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARR 209
Cdd:TIGR02633 389 RLKVKTAspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLG 468
|
90 100
....*....|....*....|...
gi 1327251791 210 ISDRTAFF----LMGELVEHNET 228
Cdd:TIGR02633 469 LSDRVLVIgegkLKGDFVNHALT 491
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-202 |
1.04e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNqALKSINLPIPTR-QVTALIGPSGCGKSTLLRCLNrmNDLIEGVtikGKLDMDG------TNIYGN------IDVA 79
Cdd:cd03236 10 YGPN-SFKLHRLPVPREgQVLGLVGPNGIGKSTALKILA--GKLKPNL---GKFDDPPdwdeilDEFRGSelqnyfTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 80 DLRIRVGMVFQKPNPFPMSIYENVAYGLRAQGIKDKKyiDEVVESSlrsaalwdEVKDRLKAHAFGLSGGQQQRLCIART 159
Cdd:cd03236 84 EGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKL--DELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1327251791 160 IAMEPDVILMDEPTSALDpI-----ATHKIEELMEDLKkdfTIVIVTH 202
Cdd:cd03236 154 LARDADFYFFDEPSSYLD-IkqrlnAARLIRELAEDDN---YVLVVEH 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-220 |
1.30e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 33 ALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKldmdgtNIYGNIdvADLRIRVGMV--FQKPNPFpMSIYENVAYGLRA 109
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGK------SILTNI--SDVHQNMGYCpqFDAIDDL-LTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 110 QGIKDKKyIDEVVESSLRSAALwDEVKDRLkahAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKI-EELM 188
Cdd:TIGR01257 2040 RGVPAEE-IEKVANWSIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIV 2114
|
170 180 190
....*....|....*....|....*....|..
gi 1327251791 189 EDLKKDFTIVIVTHSMQQARRISDRTAFFLMG 220
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-223 |
1.48e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG-VTIKGKlDMDGTNIYGNID-----VADLRIRVGMVfqk 91
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGsIRLDGE-DITGLSPRERRRlgvayIPEDRLGRGLV--- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 92 PNpfpMSIYENVA------YGLRAQGIKDKKYIDEVVES-----SLRSAALWDEVKdrlkahafGLSGGQQQRLCIARTI 160
Cdd:COG3845 349 PD---MSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEElieefDVRTPGPDTPAR--------SLSGGNQQKVILAREL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKI-EELMEDLKKDFTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIhQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-228 |
2.32e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 30 QVTALIGPSGCGKSTLLRCL-NRMNdliEGVTIKG-------KLDMDGTNIYGNIDVADLRI-----RVGMVF----QKP 92
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLaERVT---TGVITGGdrlvngrPLDSSFQRSIGYVQQQDLHLptstvRESLRFsaylRQP 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPfpMSIYEnvayglraqgiKDKkYIDEVVE-SSLRSAAlwDEVkdrLKAHAFGLSGGQQQRLCIARTIAMEPDVIL-MD 170
Cdd:TIGR00956 867 KS--VSKSE-----------KME-YVEEVIKlLEMESYA--DAV---VGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 171 EPTSALDPIATHKIEELMEDLKKD-FTIVIVTHS-----MQQARRI-----SDRTAFFlmGELVEHNET 228
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQpsailFEEFDRLlllqkGGQTVYF--GDLGENSHT 994
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-180 |
3.48e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 31 VTALIGPSGCGKSTLLRCL--NRMNDLIEG-VTIKG--KLDMDGTNIYGNIDVADLrirvgmvfQKPNpfpMSIYENVAY 105
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLagRKTGGYIEGdIRISGfpKKQETFARISGYCEQNDI--------HSPQ---VTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 106 G----LRAQGIKDKK--YIDEVVEsslrsAALWDEVKDRLKAHA--FGLSGGQQQRLCIARTIAMEPDVILMDEPTSALD 177
Cdd:PLN03140 977 SaflrLPKEVSKEEKmmFVDEVME-----LVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
...
gi 1327251791 178 PIA 180
Cdd:PLN03140 1052 ARA 1054
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-213 |
4.01e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 31 VTALIGPSGCGKSTLLRCLNrmndliegvtikGKLDMDGTNIYGNIDVAdlrirvgmvfQKPnpfpmsiyenvayglraQ 110
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILA------------GVLKPDEGEVDEDLKIS----------YKP-----------------Q 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 111 GIKDKkyIDEVVESSLRSAA--------LWDEVKDRLKAHAF------GLSGGQQQRLCIARTIAMEPDVILMDEPTSAL 176
Cdd:COG1245 409 YISPD--YDGTVEEFLRSANtddfgssyYKTEIIKPLGLEKLldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1327251791 177 DP----IATHKIEELMEDLKKdfTIVIVTHSMQQARRISDR 213
Cdd:COG1245 487 DVeqrlAVAKAIRRFAENRGK--TAMVVDHDIYLIDYISDR 525
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-225 |
4.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 27 PTRQVtALIGPSGCGKSTLLRCLNRMNDLIegvtiKGKLDMDGTNIyGNIDVADLRIRVGMVFQKPNPFPMSIYENvayg 106
Cdd:PLN03130 1264 PSEKV-GIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDI-SKFGLMDLRKVLGIIPQAPVLFSGTVRFN---- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 107 lraqgikdkkyIDEVVESSlrSAALWD-----EVKDRLKAHAFGL-----------SGGQQQRLCIARTIAMEPDVILMD 170
Cdd:PLN03130 1333 -----------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 171 EPTSALDPIATHKIEELMEDLKKDFTIVIVTHsmqqarRI-----SDRTAFFLMGELVEH 225
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFKSCTMLIIAH------RLntiidCDRILVLDAGRVVEF 1453
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-204 |
5.01e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 6 IENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKgkldmdgtniygnidvaDLRIRV 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR-----------------NGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 86 GMVFQKPN-----PFPMSIYENVAYGLRAQGIKDKkyIDEVVESSLRSAALWDevkdrlkahafgLSGGQQQRLCIARTI 160
Cdd:PRK09544 70 GYVPQKLYldttlPLTVNRFLRLRPGTKKEDILPA--LKRVQAGHLIDAPMQK------------LSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1327251791 161 AMEPDVILMDEPTSALDPIATHKIEELMEDLKKDF--TIVIVTHSM 204
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-212 |
6.17e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGVTIKGklDMDGtNIYgnIDVADLR---IR----- 84
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-------GVYPHG--TYEG-EII--FEGEELQasnIRdtera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 -VGMVFQK----PNpfpMSIYENVAYG--LRAQGIKDkkyIDEVVessLRSAALWDEVKDRLKAHA--FGLSGGQQQRLC 155
Cdd:PRK13549 83 gIAIIHQElalvKE---LSVLENIFLGneITPGGIMD---YDAMY---LRAQKLLAQLKLDINPATpvGNLGLGQQQLVE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 156 IARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISD 212
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISD 211
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-227 |
6.27e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKLDMDGTNIYGNIDVADLRIRVGMVFQkpnpfpM 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSN------------IIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ------L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 98 SIYENVAYGLRAQGIKDK---KYIDEVVESSLRSAALWDEVKDrlkahafgLSGGQQQRLCIARTIAMEPDVILMDEPTS 174
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKeikAMTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 175 ALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRTAFFLMGELVEHNE 227
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
132-239 |
1.09e-06 |
|
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: 47.57 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 132 WDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDP----IATHKIEELMEDLKKdfTIVIVTHSMQQA 207
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKK--TALVVEHDLAVL 135
|
90 100 110
....*....|....*....|....*....|....
gi 1327251791 208 RRISDRTAFFlmgelveHNETSV--IFSEPKDDR 239
Cdd:cd03222 136 DYLSDRIHVF-------EGEPGVygIASQPKGTR 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-202 |
1.55e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKLDMDGtniyGNIDVADlRIR 84
Cdd:TIGR03719 324 EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR------------MITGQEQPDS----GTIEIGE-TVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQK-----PNPfpmSIYENVAYGLRAqgIKDKKYidevvesslrsaalwdEVKDRLKAHAFG------------LS 147
Cdd:TIGR03719 387 LAYVDQSrdaldPNK---TVWEEISGGLDI--IKLGKR----------------EIPSRAYVGRFNfkgsdqqkkvgqLS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 148 GGQQQRLCIARTIAMEPDVILMDEPTSALDpiathkIEEL--MEDLKKDF--TIVIVTH 202
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLD------VETLraLEEALLNFagCAVVISH 498
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
146-228 |
1.73e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIVTHSMQQARRISDRTAFF----LMG 220
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDRVLVMhegkLKG 485
|
....*...
gi 1327251791 221 ELVEHNET 228
Cdd:PRK13549 486 DLINHNLT 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-177 |
2.64e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRClnrmndlIEGVTIKGKLDMDGTNIYGNIDVADL--RIRVGMVF--QKP 92
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKT-------IASNTDGFHIGVEGVITYDGITPEEIkkHYRGDVVYnaETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFP-MSIYENVAY-------GLRAQGIKDKKYIDEVVESSLRSAALwDEVKDRLKAHAF--GLSGGQQQRLCIARTIAM 162
Cdd:TIGR00956 148 VHFPhLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVYMATYGL-SHTRNTKVGNDFvrGVSGGERKRVSIAEASLG 226
|
170
....*....|....*
gi 1327251791 163 EPDVILMDEPTSALD 177
Cdd:TIGR00956 227 GAKIQCWDNATRGLD 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-202 |
3.73e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 31 VTALIGPSGCGKSTLLRCLNrmndliegVTIKGKLDMDGTNIYGNIDVA---DLRIRVGMVFQKPNPFPM------SIYE 101
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK--------YALTGELPPNSKGGAHDPKLIregEVRAQVKLAFENANGKKYtitrslAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 102 NVAYgLRaQGIKDKKYIDEVvesslrsaalwdevkDRLkahafglSGGQQQ------RLCIARTIAMEPDVILMDEPTSA 175
Cdd:cd03240 96 NVIF-CH-QGESNWPLLDMR---------------GRC-------SGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|
gi 1327251791 176 LDPI-ATHKIEELMEDLKKD--FTIVIVTH 202
Cdd:cd03240 152 LDEEnIEESLAEIIEERKSQknFQLIVITH 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-191 |
3.97e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIKGK---------LDMDGTnIYGNI------DVADLR- 82
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERsiayvpqqaWIMNAT-VRGNIlffdeeDAARLAd 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 -IRVGMVfqkpnpfpmsiyenvayglraqgikdkkyidevvESSLR--SAALWDEVKDRlkahAFGLSGGQQQRLCIART 159
Cdd:PTZ00243 755 aVRVSQL----------------------------------EADLAqlGGGLETEIGEK----GVNLSGGQKARVSLARA 796
|
170 180 190
....*....|....*....|....*....|..
gi 1327251791 160 IAMEPDVILMDEPTSALDpiaTHKIEELMEDL 191
Cdd:PTZ00243 797 VYANRDVYLLDDPLSALD---AHVGERVVEEC 825
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-177 |
4.51e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 3 KFDIENLDLFygdnqalkSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGVtikgkldMDGTNiyGNIDVADLR 82
Cdd:PRK13541 8 QFNIEQKNLF--------DLSITFLPSAITYIKGANGCGKSSLLR-------MIAGI-------MQPSS--GNIYYKNCN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 83 IRvgmvfQKPNPFPMSIYENVAYGLRAQGIKDKKYIDEVVESS--LRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTI 160
Cdd:PRK13541 64 IN-----NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAetLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLI 138
|
170
....*....|....*..
gi 1327251791 161 AMEPDVILMDEPTSALD 177
Cdd:PRK13541 139 ACQSDLWLLDEVETNLS 155
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
147-203 |
1.12e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.12e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327251791 147 SGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMedLKKDFTIVIVTHS 203
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHA 400
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
147-223 |
1.53e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327251791 147 SGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKD-FTIVIVTHSMQQARRISDRTAFFLMGELV 223
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
146-212 |
1.58e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 1.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVIL--MDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTH---SMQQARRISD 212
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHdedTIRAADHVID 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-216 |
1.59e-05 |
|
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: 43.90 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 28 TRQVTALIGPSGCGKSTLLRCLnrmndliegvtikgkldmdgtniygnidvadlrirvgmvfqkpnpfpmsiyenvaygL 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL---------------------------------------------------------A 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 108 RAQGIKDKKYIdEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEEL 187
Cdd:smart00382 24 RELGPPGGGVI-YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327251791 188 -------MEDLKKDFTIVIVTHSMQQARRISDRTAF 216
Cdd:smart00382 103 eelrlllLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-201 |
2.41e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 4 FDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGV--TIKGKLDMDGTNIygNIDVADL 81
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLK-------LIAGLlnPEKGEILFERQSI--KKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 82 RIRVGMVFQKP--NPFpMSIYENVAYGLRAQGIKDKkyIDEVVesSLRSAALWDEVKDRLkahafgLSGGQQQRLCIART 159
Cdd:PRK13540 73 QKQLCFVGHRSgiNPY-LTLRENCLYDIHFSPGAVG--ITELC--RLFSLEHLIDYPCGL------LSSGQKRQVALLRL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVT 201
Cdd:PRK13540 142 WMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLT 183
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
146-212 |
2.75e-05 |
|
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: 43.47 E-value: 2.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 146 LSGGQQQRLCIARTIAMEPD--VILMDEPTSALDPIathKIEELMEDLKK----DFTIVIVTHS---MQQARRISD 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ---DINQLLEVIKGlidlGNTVILIEHNldvLSSADWIID 160
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
112-203 |
3.01e-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: 44.30 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 112 IKDKKYIDEVVESSLRSAALWDEVKDRLKAHAFGLSGGQQQRLCIA---RTIAMEPDVILMDEPTSALDPIATHKIEELM 188
Cdd:pfam13304 203 GEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELL 282
|
90
....*....|....*.
gi 1327251791 189 EDLKKDFT-IVIVTHS 203
Cdd:pfam13304 283 KELSRNGAqLILTTHS 298
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-203 |
3.03e-05 |
|
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: 44.22 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPtRQVTALIGPSGCGKSTLLRCLNRMNDLIEGVTIkgkldmDGTNIYGNIDVADLRIRVGMVFQKP------ 92
Cdd:COG3593 14 IKDLSIELS-DDLTVLVGENNSGKSSILEALRLLLGPSSSRKF------DEEDFYLGDDPDLPEIEIELTFGSLlsrllr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 NPFPMSIYENVAYGLR------AQGIKD-KKYIDEVVESSLRSAAL-----WDEVKDRLKAHAFGLSGGQ---------- 150
Cdd:COG3593 87 LLLKEEDKEELEEALEelneelKEALKAlNELLSEYLKELLDGLDLelelsLDELEDLLKSLSLRIEDGKelpldrlgsg 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327251791 151 QQRLCI---ARTIAM-----EPDVILMDEPTSALDPIATHK-IEELMEDLKKDFTIVIVTHS 203
Cdd:COG3593 167 FQRLILlalLSALAElkrapANPILLIEEPEAHLHPQAQRRlLKLLKELSEKPNQVIITTHS 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-202 |
5.37e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 34 LIGPSGCGKSTLLRCLNRMNDLIEGVTIKgkldMDGtniygnidvadlrIRVGMVFQKP--NPfPMSIYENVAYGLraQG 111
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP----APG-------------IKVGYLPQEPqlDP-EKTVRENVEEGV--AE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 112 IKDKK---------------YIDEV------VESSLRSAALWD-EVKDRLKAHAFG----------LSGGQQQRLCIART 159
Cdd:PRK11819 98 VKAALdrfneiyaayaepdaDFDALaaeqgeLQEIIDAADAWDlDSQLEIAMDALRcppwdakvtkLSGGERRRVALCRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLKKdfTIVIVTH 202
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG--TVVAVTH 218
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
20-58 |
6.90e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 6.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1327251791 20 KSI-NLPIPTRQVTALIGPSGCGKSTLLRCLNRMNDLIEG 58
Cdd:COG4637 11 KSLrDLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARG 50
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-212 |
6.96e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 13 YGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLnrmndliegvtiKGKLdmdgTNIYGNIDVADlRIRVG------ 86
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL------------AGEL----APVSGEIGLAK-GIKLGyfaqhq 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 87 MVFQKPNPFPMSIYENVAYGLRAQGIKDkkYI-------DEVVESSLRsaalwdevkdrlkahafgLSGGQQQRLCIART 159
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELEQKLRD--YLggfgfqgDKVTEETRR------------------FSGGEKARLVLALI 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 160 IAMEPDVILMDEPTSALDPIATHKIEELMEDLkkDFTIVIVTHSMQQARRISD 212
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHDRHLLRSTTD 495
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-218 |
7.57e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 5 DIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndliegvTIKGKLDMDGtniyGNIDVADlRIR 84
Cdd:PRK11819 326 EAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK------------MITGQEQPDS----GTIKIGE-TVK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 85 VGMVFQ-----KPNPfpmSIYENVAYGLRAqgIKDKKYidevvesslrsaalwdEVKDRLKAHAFG------------LS 147
Cdd:PRK11819 389 LAYVDQsrdalDPNK---TVWEEISGGLDI--IKVGNR----------------EIPSRAYVGRFNfkggdqqkkvgvLS 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 148 GGQQQRLCIARTIAMEPDVILMDEPTSALDpiathkIEEL--MEDLKKDF--TIVIVTHsmqqarrisDRtaFFL 218
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD------VETLraLEEALLEFpgCAVVISH---------DR--WFL 505
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-204 |
9.63e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLL-----RCLNRMNDLieGVTIKGKLDM-DGtniYGNIDvadlriRVGMVFQKP 92
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHL--KKEQPGNHDRiEG---LEHID------KVIVIDQSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 93 -------NPfpmSIYENVAYGLRA---QGIKDKKY-------------IDEVVESSLRSAALWDE----VKDRLKA---- 141
Cdd:cd03271 80 igrtprsNP---ATYTGVFDEIRElfcEVCKGKRYnretlevrykgksIADVLDMTVEEALEFFEnipkIARKLQTlcdv 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 142 ---------HAFGLSGGQQQRLCIARTIAME---PDVILMDEPTSALDpiaTHKIEELMEDL----KKDFTIVIVTHSM 204
Cdd:cd03271 157 glgyiklgqPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLH---FHDVKKLLEVLqrlvDKGNTVVVIEHNL 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-212 |
2.97e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVI--LMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQ---ARRISD 212
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMislADRIID 549
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
5.72e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 2 NKFDIENLDLFYGDNQALKSINLPIPTRQVTALIGPSGCGKSTLLrclnrmnDLIEG---------VTIKGKLDMDGTNI 72
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-------SLITGdhpqgysndLTLFGRRRGSGETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 73 YgnidvaDLRIRVGMVfqkpnpfpmsiyenvayglraqgiKDKKYIDEVVESSLR---------SAALWDEVKDRLKAHA 143
Cdd:PRK10938 332 W------DIKKHIGYV------------------------SSSLHLDYRVSTSVRnvilsgffdSIGIYQAVSDRQQKLA 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327251791 144 -----------------F-GLSGGQQQRLCIARTIAMEPDVILMDEPTSALDPI 179
Cdd:PRK10938 382 qqwldilgidkrtadapFhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-191 |
6.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 20 KSINLPIPTRQVTALIGPSGCGKSTLLRclnrmndLIEGvtikgkldmdgtniygnidvaDLRIRVGMVFQKPNpFPMSI 99
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILK-------LISG---------------------ELQPSSGTVFRSAK-VRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 100 YenvayglraqgikDKKYIDEVVESS---LRSAALWDEV-KDRLKAH--AFG------------LSGGQQQRLCIARTIA 161
Cdd:PLN03073 577 F-------------SQHHVDGLDLSSnplLYMMRCFPGVpEQKLRAHlgSFGvtgnlalqpmytLSGGQKSRVAFAKITF 643
|
170 180 190
....*....|....*....|....*....|
gi 1327251791 162 MEPDVILMDEPTSALDPIAthkIEELMEDL 191
Cdd:PLN03073 644 KKPHILLLDEPSNHLDLDA---VEALIQGL 670
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
146-213 |
7.99e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327251791 146 LSGGQQQRLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLKKDFTIVIVTHS-MQQARRISDR 213
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSeLPELLGMCDR 473
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-202 |
8.38e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 8.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327251791 144 FGLSGGQQQRLCIA-----RTIAMEPdVILMDEPTSALDPIATHKIEE-LMEDLKKDFTIVIVTH 202
Cdd:cd03227 76 LQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEaILEHLVKGAQVIVITH 139
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-214 |
1.30e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 18 ALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNrmndlieGV----TIKGKLDMDGtniygniDVADLR-IR----VGMV 88
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-------GVyphgSYEGEILFDG-------EVCRFKdIRdseaLGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 89 F--QKPNPFP-MSIYENVAYGlraQGIKDKKYIDevvesslrsaalWDEVKDRLKA--HAFGLS----------G-GQQQ 152
Cdd:NF040905 82 IihQELALIPyLSIAENIFLG---NERAKRGVID------------WNETNRRAREllAKVGLDespdtlvtdiGvGKQQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327251791 153 RLCIARTIAMEPDVILMDEPTSALDPIATHKIEELMEDLK-KDFTIVIVTHSMQQARRISDRT 214
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-204 |
2.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327251791 146 LSGGQQQRLCIARTI---AMEPDVILMDEPTSALDpiaTHKIEELMEDLK----KDFTIVIVTHSM 204
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH---THDIKALIYVLQslthQGHTVVIIEHNM 872
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
17-46 |
2.56e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1327251791 17 QALKSIN--------LPIPTRQVTALIGPSGCGKSTLL 46
Cdd:pfam13555 2 TRLQLINwgtfdghtIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-46 |
3.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.32e-03
10 20
....*....|....*....|....*...
gi 1327251791 19 LKSINLPIPTRQVTALIGPSGCGKSTLL 46
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
17-51 |
3.32e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 38.40 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 1327251791 17 QALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNR 51
Cdd:TIGR00602 98 TWLKAQVLENAPKRILLITGPSGCGKSTTIKILSK 132
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
28-76 |
3.52e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.55 E-value: 3.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1327251791 28 TRQVTALIGPSGCGKSTLLRCLNRMNDL--IEGVTIKGKLDMDGTNIYGNI 76
Cdd:pfam13401 4 GAGILVLTGESGTGKTTLLRRLLEQLPEvrDSVVFVDLPSGTSPKDLLRAL 54
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
26-49 |
6.74e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 37.19 E-value: 6.74e-03
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-200 |
8.32e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 36.92 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 15 DNQALKSINLPIPTRQVTALIGPSGCGKSTLLRCLNRmndliEGVTIKGKLDMDGTNIYgNIDVADLRIRVGMVFQKPNP 94
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG-----ELPLLSGERQSQFSHIT-RLSFEQLQKLVSDEWQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327251791 95 FPMSIYEnvayglraqgikdkkyidevvESSLRSAA--LWDEVKDRLK----AHAFG-----------LSGGQQQRLCIA 157
Cdd:PRK10938 89 DMLSPGE---------------------DDTGRTTAeiIQDEVKDPARceqlAQQFGitalldrrfkyLSTGETRKTLLC 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1327251791 158 RTIAMEPDVILMDEPTSALDPIATHKIEELMEDL-KKDFTIVIV 200
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLhQSGITLVLV 191
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|
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