|
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: 551.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVL 81
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYdPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALA 161
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTE 241
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250
|
....*...
gi 517187183 242 NYITGRFG 249
Cdd:COG1117 251 DYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-248 |
1.26e-169 |
|
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: 467.54 E-value: 1.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVL 81
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYdKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALA 161
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTE 241
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 517187183 242 NYITGRF 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 |
2.31e-145 |
|
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: 405.41 E-value: 2.31e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVLR 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYdLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNksALGMSGGQQQRLCIARALAI 162
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-249 |
7.15e-134 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 377.19 E-value: 7.15e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVLR 82
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYsPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTEN 242
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 517187183 243 YITGRFG 249
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-249 |
4.13e-132 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 373.35 E-value: 4.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVL 81
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYaPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGPRTHGIhnKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALA 161
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFF---------LLGEIVEYNKTSQLF 232
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIF 247
|
250
....*....|....*..
gi 517187183 233 SMPQDERTENYITGRFG 249
Cdd:PRK14243 248 NSPQQQATRDYVSGRFG 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-249 |
5.93e-103 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 299.64 E-value: 5.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVY-RDLDINVLR 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLV--IELKKKYTIVMVTHNMQQAVRISDKTAFF-----LLGEIVEYNKTSQLFSMP 235
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 517187183 236 QDERTENYITGRFG 249
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-249 |
1.12e-101 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 295.98 E-value: 1.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVYR-DLDIN 79
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHG-IHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIA 157
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 158 RALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQD 237
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|..
gi 517187183 238 ERTENYITGRFG 249
Cdd:PRK14267 242 ELTEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
5.71e-101 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 294.13 E-value: 5.71e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVYRdLDINV 80
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK-MDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGI-HNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIAR 158
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDE 238
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*....
gi 517187183 239 RTENYITGR 247
Cdd:PRK14247 240 LTEKYVTGR 248
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-247 |
1.98e-79 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 239.56 E-value: 1.98e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKN-CRITGEVTLDKEDVYRdLDINVLRKK 84
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIFQ-IDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:PRK14246 92 VGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENY 243
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
....
gi 517187183 244 ITGR 247
Cdd:PRK14246 252 VIGR 255
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-240 |
1.98e-78 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 236.04 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDV-YRDLDINVL 81
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLE------EPDsGTITVDGEDLtDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARAL 160
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDER 239
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
.
gi 517187183 240 T 240
Cdd:COG1126 232 T 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-249 |
2.89e-77 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 234.61 E-value: 2.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 8 NLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVYRDLDINVLRKKVGM 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 88 VFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVL 167
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 168 LMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENYITGR 247
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
..
gi 517187183 248 FG 249
Cdd:PRK14271 266 SG 267
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-241 |
1.31e-67 |
|
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: 217.08 E-value: 1.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDV--YRD 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL------RPTsGSILFDGKDLtkLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDINVLRKKVGMVFQKP----NPFpMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRlnkSALGMSGGQQ 151
Cdd:COG1123 335 RSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR---YPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTS 229
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250
....*....|..
gi 517187183 230 QLFSMPQDERTE 241
Cdd:COG1123 491 EVFANPQHPYTR 502
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-233 |
1.27e-64 |
|
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: 200.64 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRitGEVTLDKEDVyRDLDINVLR 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG---LLKPTS--GEVLVDGKDI-TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQkpNP----FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDevkdRLNKSALGMSGGQQQRLCIAR 158
Cdd:COG1122 75 RKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEH----LADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-222 |
1.54e-63 |
|
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: 197.37 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDVYRDL-DINVL 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE------EPDsGTIIIDGLKLTDDKkNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGPRT-HGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:cd03262 75 RQKVGMVFQQFNLFPhLTVLENITLAPIKvKGM-SKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-244 |
4.20e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 196.85 E-value: 4.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVLR 82
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTS-----GRILIDGEDI-RDLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIAFGPRTHG-----IHNKVqlDEIVER-SLKQaaiwDEVKDRLNKSalgMSGGQQQRLC 155
Cdd:COG1125 76 RRIGYVIQQIGLFPhMTVAENIATVPRLLGwdkerIRARV--DELLELvGLDP----EEYRDRYPHE---LSGGQQQRVG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:COG1125 147 VARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILA 226
|
250
....*....|.
gi 517187183 234 MPQDERTENYI 244
Cdd:COG1125 227 NPANDFVADFV 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-224 |
5.61e-62 |
|
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: 193.50 E-value: 5.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyrdLDINVLRK 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP-----DSGEILIDGRDV---TGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:cd03259 73 NIGMVFQDYALFPhLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKK--KYTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-221 |
3.29e-61 |
|
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: 190.48 E-value: 3.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKncRITGEVTLDKEDVYR-DLDINVLR 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG---LEE--PDSGSILIDGEDLTDlEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIAFGprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARALA 161
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAFFLLGE 221
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
4.03e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 193.00 E-value: 4.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRI--------TGEVTLD 68
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLL-------------RLiaglekptSGEVLVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 69 KEDVYRdldinvLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLkqaaiwDEV--KDRLNK--SA 143
Cdd:COG1116 72 GKPVTG------PGPDRGVVFQEPALLPwLTVLDNVALGLELRGV-PKAERRERARELL------ELVglAGFEDAypHQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 144 LgmSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDK 213
Cdd:COG1116 139 L--SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADR 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-224 |
3.15e-60 |
|
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: 189.64 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrMNDLVKncRITGEVTLDKEDVYR--DLDINVL 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLR--PDSGEVLIDGEDISGlsEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPF-PMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARAL 160
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-240 |
4.40e-60 |
|
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: 190.01 E-value: 4.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG----DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVYRDLDiN 79
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRRRR-K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKP----NPFpMSIYDNIAFGPRTHGIHNKvqlDEIVERSLKQAAIWDEVKDRLnKSALgmSGGQQQRLC 155
Cdd:COG1124 76 AFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRY-PHQL--SGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
....*..
gi 517187183 234 MPQDERT 240
Cdd:COG1124 229 GPKHPYT 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-226 |
6.60e-60 |
|
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: 188.87 E-value: 6.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVY--RDLD 77
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLklSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKKVGMVFQKP----NPFpMSIYDNIAFGPRTHGIHNKVQldeivERSLKQAAIWDEV---KDRLNKSALGMSGGQ 150
Cdd:cd03257 77 RKIRRKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKE-----ARKEAVLLLLVGVglpEEVLNRYPHELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYN 226
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-244 |
2.44e-59 |
|
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: 187.49 E-value: 2.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKncRITGEVTLDKEDVYR--DLDIN 79
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLR--PDSGEILVDGQDITGlsEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPF-PMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAaiwdEVKDRLNK--SALgmSGGQQQRLCI 156
Cdd:COG1127 79 ELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELV----GLPGAADKmpSEL--SGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 157 ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSM 234
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
250
....*....|
gi 517187183 235 PqDERTENYI 244
Cdd:COG1127 233 D-DPWVRQFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-213 |
2.72e-59 |
|
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: 186.91 E-value: 2.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRI--------TGEVTLDKED 71
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLL-------------RIiaglerptSGEVLVDGEP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 72 VyrdldiNVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAaiwdEVKDRLNK--SALgmSG 148
Cdd:cd03293 68 V------TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKA-EARERAEELLELV----GLSGFENAypHQL--SG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 149 GQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDK 213
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-247 |
2.73e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 191.08 E-value: 2.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnRMndlvkncrI-------TGEVTLDKEDVy 73
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RM--------IagfetpdSGRILLDGRDV- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 RDLDINvlRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLkqaaiwdevkDRLNKSALG------M 146
Cdd:COG3842 70 TGLPPE--KRNVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELL----------ELVGLEGLAdryphqL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDpistAKI-EDLVIELKK-----KYTIVMVTHNMQQAVRISDKTAFFLLG 220
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALD----AKLrEEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDG 212
|
250 260 270
....*....|....*....|....*....|...
gi 517187183 221 EIVEYNKTSQLFSMPQDER------TENYITGR 247
Cdd:COG3842 213 RIEQVGTPEEIYERPATRFvadfigEANLLPGT 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-236 |
2.54e-58 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 192.81 E-value: 2.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndLVKNCRITGEVTLDKEDVyRDLDINVL 81
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDL-LELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKP--NPFPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:COG1123 82 GRRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
3.62e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.48 E-value: 3.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDvYRDLDINVLRK 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKP-LSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFPMSIYDNIAFGPRthgIHNKVQLDEIVERSLKQAAIWDEVkdrLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:COG4619 75 QVAYVPQEPALWGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDI---LDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKT 214
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRV 201
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-236 |
4.34e-58 |
|
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: 187.18 E-value: 4.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCRITGEVTLDKEDVyRDLDIN 79
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDL-LKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLR----KKVGMVFQKP----NPFpMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIwDEVKDRLNKSALGMSGGQQ 151
Cdd:COG0444 79 ELRkirgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTS 229
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*..
gi 517187183 230 QLFSMPQ 236
Cdd:COG0444 237 ELFENPR 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
6.97e-58 |
|
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: 183.05 E-value: 6.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDF--KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVyRDLDINVLR 82
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-----PTSGEVLVDGKDL-TKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDevkdRLNKSALGMSGGQQQRLCIARAL 160
Cdd:cd03225 75 RKVGLVFQNPDDqfFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFF 217
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-233 |
2.79e-57 |
|
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: 183.42 E-value: 2.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-----DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNcrITGEVTLDKEDVYRD--L 76
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN---GLLKP--TSGTVTIDGRDITAKkkK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKDRlnkSALGMSGGQQQRL 154
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGL-SEEEAEERVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
.
gi 517187183 233 S 233
Cdd:TIGR04521 232 S 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-231 |
1.32e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVkncRIT-GEVTLDKEDVYRDLDInvLR 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL---GLL---RPTsGEVRVLGEDVARDPAE--VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIARALA 161
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-244 |
1.35e-56 |
|
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: 180.57 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvkncrIT---GEVTLDKEDVyRDLDIN 79
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--------IEptsGEIFIDGEDI-REQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRThgihNKVQLDEIVERSLKQAAIWD----EVKDRLNKSalgMSGGQQQRL 154
Cdd:cd03295 72 ELRRKIGYVIQQIGLFPhMTVEENIALVPKL----LKWPKEKIRERADELLALVGldpaEFADRYPHE---LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
250
....*....|..
gi 517187183 233 SMPQDERTENYI 244
Cdd:cd03295 225 RSPANDFVAEFV 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-213 |
1.97e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 183.42 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRI--------TGEVTLDKEDVYRD 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLL-------------RIiagletpdSGRIVLNGRDLFTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDinVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRtHGIHNKVQLDEIVERSLK--QAaiwDEVKDRLnKSALgmSGGQQQ 152
Cdd:COG1118 70 LP--PRERRVGFVFQHYALFPhMTVAENIAFGLR-VRPPSKAEIRARVEELLElvQL---EGLADRY-PSQL--SGGQRQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDK 213
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADR 203
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-222 |
2.33e-55 |
|
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: 176.91 E-value: 2.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVY----RD 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTS-----GEVRVDGTDISklseKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDiNVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRL 154
Cdd:cd03255 76 LA-AFRRRHIGFVFQSFNLLPdLTALENVELPLLLAGVPKK-ERRERAEELLERVGL----GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMqQAVRISDKTAFFLLGEI 222
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-223 |
3.59e-54 |
|
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: 174.85 E-value: 3.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINVLRK 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKP-----SSGEVLLDGRDL-ASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPN-PFPMSIYDNIAFG--PRTHGIHNKVQLD-EIVERSLKQAAIWDeVKDRlnkSALGMSGGQQQRLCIARA 159
Cdd:COG1120 76 RIAYVPQEPPaPFGLTVRELVALGryPHLGLFGRPSAEDrEAVEEALERTGLEH-LADR---PVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKtaFFLL--GEIV 223
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADR--LVLLkdGRIV 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-237 |
4.42e-54 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 177.57 E-value: 4.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnRMndlvkncrI-------TGEVTLDKEDVy 73
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RM--------IagledptSGEILIGGRDV- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 rdLDINVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHgihnKVQLDEIVERsLKQAAiwDEVK--DRLNKSALGMSGGQ 150
Cdd:COG3839 68 --TDLPPKDRNIAMVFQSYALYPhMTVYENIAFPLKLR----KVPKAEIDRR-VREAA--ELLGleDLLDRKPKQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDpistAKI-EDLVIELKK-----KYTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLD----AKLrVEMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQ 214
|
250
....*....|...
gi 517187183 225 YNKTSQLFSMPQD 237
Cdd:COG3839 215 VGTPEELYDRPAN 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
8.05e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 8.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDV--YRDL 76
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE------RPTsGSVLVDGVDLtaLSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLkqaaiwDEV--KDRLNK--SALgmSGGQQ 151
Cdd:COG1135 76 ELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGV-PKAEIRKRVAELL------ELVglSDKADAypSQL--SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAffLL--GEIVEYNK 227
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVA--VLenGRIVEQGP 224
|
250
....*....|....*..
gi 517187183 228 TSQLFSMPQDERTENYI 244
Cdd:COG1135 225 VLDVFANPQSELTRRFL 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
1.73e-53 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 170.26 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDF--KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVL 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTS-----GEILIDGVDL-RDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIafgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARALA 161
Cdd:cd03228 75 RKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDK 213
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRL-STIRDADR 163
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-244 |
1.63e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.19 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMnDLVKN--CRITGEvTLDKEDVYRDLDINVL 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-ETPDSgqLNIAGH-QFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGP-RTHGIhNKVQLDEIVERSLKQAaiwdEVKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:COG4161 81 RQKVGMVFQQYNLWPhLTVMENLIEAPcKVLGL-SKEQAREKAMKLLARL----RLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNkTSQLFSMPQDE 238
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTE 234
|
....*.
gi 517187183 239 RTENYI 244
Cdd:COG4161 235 AFAHYL 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-224 |
3.34e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.07 E-value: 3.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkNC-----RIT-GEVTLDKEDVY 73
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-----------NIlggldRPTsGEVLIDGQDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 RdLDINVL----RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIwdevKDRLNKSALGMSG 148
Cdd:COG1136 74 S-LSERELarlrRRHIGFVFQFFNLLPeLTALENVALPLLLAGVSRK-ERRERARELLERVGL----GDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 149 GQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAvRISDKTAFFLLGEIVE 224
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-224 |
5.68e-51 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 176.56 E-value: 5.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFK--ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVL 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS-----GRILIDGIDL-RQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGprthgiHNKVQLDEIVErSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRL 154
Cdd:COG2274 548 RRQIGVVLQDVFLFSGTIRENITLG------DPDATDEEIIE-AARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTafFLL--GEIVE 224
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRI--IVLdkGRIVE 689
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-240 |
7.25e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 7.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrMNDLVKncRITGEVTLDKEDVYRDldinvlRK 83
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVRLFGKPPRRA------RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPN---PFPMSIYDNIAFG--PRT--HGIHNKVQlDEIVERSLKQAAIWDeVKDRLnksaLG-MSGGQQQRLC 155
Cdd:COG1121 76 RIGYVPQRAEvdwDFPITVRDVVLMGryGRRglFRRPSRAD-REAVDEALERVGLED-LADRP----IGeLSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAfFLLGEIVEYNKTSQLFSM 234
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEVLTP 228
|
....*.
gi 517187183 235 PQDERT 240
Cdd:COG1121 229 ENLSRA 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-236 |
1.46e-50 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 165.06 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDV--YRDL 76
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLE------RPTsGSVLVDGTDLtlLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPF-PMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLC 155
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADAYPAQ----LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 517187183 234 MPQ 236
Cdd:cd03258 231 NPQ 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-224 |
3.35e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 172.66 E-value: 3.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVLR 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS-----GRILIDGVDI-RDLTLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRLC 155
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIRYGRPDAT-------DEEVEEAAKAAQAHEFIEAlpdgydtVVGERGVNLSGGQRQRIA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRL-STIRNADRILVLDDGRIVE 554
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-245 |
7.65e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 7.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvkncritgEV----TLDKEDVYRDL--- 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----------EMprsgTLNIAGNHFDFskt 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 ----DINVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRthgihnKVQ-LDEivERSLKQAaiwDEVKDRL------NKSAL 144
Cdd:PRK11124 72 psdkAIRELRRNVGMVFQQYNLWPhLTVQQNLIEAPC------RVLgLSK--DQALARA---EKLLERLrlkpyaDRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 145 GMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
250 260
....*....|....*....|..
gi 517187183 224 EYNkTSQLFSMPQDERTENYIT 245
Cdd:PRK11124 221 EQG-DASCFTQPQTEAFKNYLS 241
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
14-246 |
9.96e-50 |
|
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: 166.95 E-value: 9.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 14 GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRitGEVTLDKEDVYRDLDI---NVLRKKVGMVFQ 90
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIEPTA--GQIFIDGENIMKQSPVelrEVRRKKIGMVFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 91 KPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIARALAIEPDVLLM 169
Cdd:TIGR01186 79 QFALFPhMTILQNTSLGPELLGW-PEQERKEKALELLKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDILLM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 170 DEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENYITG 246
Cdd:TIGR01186 154 DEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
1.81e-49 |
|
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: 162.02 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyrdLDINVLRK 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS-----GEILLDGKDI---TNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:cd03300 73 PVNTVFQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL----EGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDpistAKI-EDLVIELKKKY-----TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:cd03300 148 EPKVLLLDEPLGALD----LKLrKDMQLELKRLQkelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-233 |
1.72e-48 |
|
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: 160.01 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY---GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINV 80
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDI-RDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAFG--PRThgihnkvqlDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQ 151
Cdd:cd03249 75 LRSQIGLVSQEPVLFDGTIAENIRYGkpDAT---------DEEVEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
..
gi 517187183 232 FS 233
Cdd:cd03249 225 MA 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-244 |
2.50e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 159.92 E-value: 2.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEdvyRDLD--- 77
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTA---RSLSqqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 --INVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRthgihnkvqldeIVERSLKQAAIwDEVKDRLNKSALG--------- 145
Cdd:PRK11264 78 glIRQLRQHVGFVFQNFNLFPhRTVLENIIEGPV------------IVKGEPKEEAT-ARARELLAKVGLAgketsyprr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|
gi 517187183 225 YNKTSQLFSMPQDERTENYI 244
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFL 244
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-246 |
3.96e-48 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 159.73 E-value: 3.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRitGEVTLDKEDVY----RDLdINVLRKKVGMVFQKPN 93
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAamsrKEL-RELRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 94 PFP-MSIYDNIAFGPRTHGIHNKVQLdEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:cd03294 113 LLPhRTVLENVAFGLEVQGVPRAERE-ERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 173 TSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENYITG 246
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
1.29e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.91 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDL-YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV--YRDLDINV 80
Cdd:COG3638 3 LELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GEILVDGQDVtaLRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFG--PRTHGIhnkvqldeiveRSL--------KQAAIW--DEV--KDRLNKSALG 145
Cdd:COG3638 78 LRRRIGMIFQQFNLVPrLSVLTNVLAGrlGRTSTW-----------RSLlglfppedRERALEalERVglADKAYQRADQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISD 212
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRYAD 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-224 |
6.83e-47 |
|
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: 163.39 E-value: 6.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINVLR 82
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-----YSGSILINGVDL-SDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRLC 155
Cdd:COG4988 411 RQIAWVPQNPYLFAGTIRENLRLGRPDAS-------DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRL-ALLAQADRILVLDDGRIVE 551
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-239 |
7.77e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 155.64 E-value: 7.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncrIT-GEVTLDKEDVY-RDLDINVL 81
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEE------ITsGDLIVDGLKVNdPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGPRthgihnKVqldeiveRSLKQAAIWDEVKDRLNKSALG---------MSGGQQ 151
Cdd:PRK09493 76 RQEAGMVFQQFYLFPhLTALENVMFGPL------RV-------RGASKEEAEKQARELLAKVGLAerahhypseLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKI----EDLVIElkkKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNK 227
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVlkvmQDLAEE---GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
250
....*....|..
gi 517187183 228 TSQLFSMPQDER 239
Cdd:PRK09493 220 PQVLIKNPPSQR 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-215 |
8.16e-47 |
|
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: 154.61 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCRitGEVTLDKEDVYRDldinvlRKK 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLKPTS--GSIRVFGKPLEKE------RKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQKPN---PFPMSIYDNIAFGPRTH----GIHNKVQlDEIVERSLKQAAIwDEVKDRLnksaLG-MSGGQQQRLCI 156
Cdd:cd03235 70 IGYVPQRRSidrDFPISVRDVVLMGLYGHkglfRRLSKAD-KAKVDEALERVGL-SELADRQ----IGeLSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 157 ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTA 215
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-174 |
9.03e-47 |
|
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: 152.42 E-value: 9.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVYRDlDINVLRKKVGMVFQKPNPFP-M 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-----TEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPrL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 98 SIYDNIAFGPRTHGIHNKVQLDEiVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTS 174
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-231 |
1.85e-46 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 154.65 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV--YRDLDINV 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS-----GSVLIDGTDInkLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFG--PRTHGIHNKVQLdeiVERSLKQAAI--WDEV--KDRLNKSALGMSGGQQQR 153
Cdd:cd03256 76 LRRQIGMIFQQFNLIErLSVLENVLSGrlGRRSTWRSLFGL---FPKEEKQRALaaLERVglLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-224 |
1.92e-46 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 153.95 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnRMndlvkncrITGEVTLDKEDVY-RDLDINVLR 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTL----RM--------IAGLEEPTSGRIYiGGRDVTDLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KK---VGMVFQKPNPFP-MSIYDNIAFGPRTHgihnKVQLDEIVERSLKQAAIW--DEVKDRLNKSalgMSGGQQQRLCI 156
Cdd:cd03301 69 PKdrdIAMVFQNYALYPhMTVYDNIAFGLKLR----KVPKDEIDERVREVAELLqiEHLLDRKPKQ---LSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 157 ARALAIEPDVLLMDEPTSALDpistAKI-EDLVIELKK-----KYTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLD----AKLrVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-222 |
2.61e-46 |
|
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: 152.17 E-value: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNcriTGEVTLDKEDVYRDldINVLRK 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDIKKE--PEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgmSGGQQQRLCIARALAI 162
Cdd:cd03230 74 RIGYLPEEPSLYEnLTVRENLKL-----------------------------------------SGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKY-TIVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
3.91e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 153.37 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFkaLKNINLEIASNEITAFIGPSGCGKSTLLkSLnrmndlvkncrI-------TGEVTLDKEDVyrdL 76
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLL-NL-----------IagflppdSGRILWNGQDL---T 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPFP-MSIYDNIAFGprthgIHNKVQLDEIVERSLKQAAiwdevkDRLNKSALG------MSGG 149
Cdd:COG3840 65 ALPPAERPVSMLFQENNLFPhLTVAQNIGLG-----LRPGLKLTAEQRAQVEQAL------ERVGLAGLLdrlpgqLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNK 227
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
250
....*....|....*..
gi 517187183 228 TSQLFSMPQDERTENYI 244
Cdd:COG3840 214 TAALLDGEPPPALAAYL 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-221 |
5.34e-46 |
|
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: 150.86 E-value: 5.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVLRKK 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS-----GEILIDGKDI-AKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQkpnpfpmsiydniafgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARALAIEP 164
Cdd:cd00267 75 IGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 165 DVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDKTAFFLLGE 221
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-223 |
4.45e-45 |
|
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: 150.66 E-value: 4.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNdLVKncRITGEVTLDKEDVYRDLDINVLRK 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MG-LLP--PRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGI-HNKVQLDEIVERslkqaaiWDEVKDRLNKSALGMSGGQQQRLCIARALA 161
Cdd:cd03224 76 GIGYVPEGRRIFPeLTVEENLLLGAYARRRaKRKARLERVYEL-------FPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-233 |
5.34e-45 |
|
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: 151.81 E-value: 5.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVK----NCRITGEVTLDKEDVYrdlD 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLN---GLLLptsgKVTVDGLDTLDEENLW---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 InvlRKKVGMVFQKP-NPFPMSIY-DNIAFGPRTHGihnkVQLDEIVER---SLKQAAIWDevkdRLNKSALGMSGGQQQ 152
Cdd:TIGR04520 75 I---RKKVGMVFQNPdNQFVGATVeDDVAFGLENLG----VPREEMRKRvdeALKLVGMED----FRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQ 230
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
...
gi 517187183 231 LFS 233
Cdd:TIGR04520 223 IFS 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-223 |
1.23e-44 |
|
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: 147.97 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVLRKK 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS-----GEILLDGKDL-ASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQkpnpfpmsiydniafgprthgIHNKVQLDEIVERSLKQaaiwdevkdrlnksalgMSGGQQQRLCIARALAIEP 164
Cdd:cd03214 75 IAYVPQ---------------------ALELLGLAHLADRPFNE-----------------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 165 DVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-244 |
1.44e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 152.65 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRIT-GEVTLDKEDV--YRDL 76
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE------RPTsGRVLVDGQDLtaLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPfpMS---IYDNIAF-----GPRTHGIHNKV-QLDEIVERSlkqaaiwdevkDRLNKSALGMS 147
Cdd:PRK11153 76 ELRKARRQIGMIFQHFNL--LSsrtVFDNVALplelaGTPKAEIKARVtELLELVGLS-----------DKADRYPAQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
250
....*....|....*....
gi 517187183 226 NKTSQLFSMPQDERTENYI 244
Cdd:PRK11153 223 GTVSEVFSHPKHPLTREFI 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-231 |
2.39e-44 |
|
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: 149.24 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNcriTGEVTLDKEDVYRDLdiNVLRK 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRML--AGLLKPD---SGSILIDGEDVRKEP--REARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIWDEvkdrLNKSALGMSGGQQQRLCIARALAI 162
Cdd:COG4555 75 QIGVLPDERGLYDrLTVRENIRYFAELYGLFDE-ELKKRIEELIELLGLEEF----LDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-205 |
5.63e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.89 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvknCRIT-GEVTLDKEDVyRDL---DI 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE------ERPTsGQVLVNGQDL-SRLkrrEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NVLRKKVGMVFQK----PNpfpMSIYDNIAFGPRTHGIHNKvqldEIVERSlkqAAIWDEV--KDRLNKSALGMSGGQQQ 152
Cdd:COG2884 75 PYLRRRIGVVFQDfrllPD---RTVYENVALPLRVTGKSRK----EIRRRV---REVLDLVglSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQ 205
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLE 198
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-231 |
7.67e-44 |
|
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: 148.22 E-value: 7.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV--YRDLDINV 80
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS-----GSILLEGTDItkLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFGpRThGIHNKVQL------DEIVERSLkqaAIWDEV--KDRLNKSALGMSGGQQ 151
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIErLTVLENVLHG-RL-GYKPTWRSllgrfsEEDKERAL---SALERVglADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTS 229
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPS 231
|
..
gi 517187183 230 QL 231
Cdd:TIGR02315 232 EL 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
3.39e-43 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 146.33 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYrdlDINVLRK 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS-----GTILFGGEDAT---DVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVER--SLKQAAIWDEVKDRLNKSalgMSGGQQQRLCIARAL 160
Cdd:cd03296 75 NVGFVFQHYALFRhMTVFDNVAFGLRVKPRSERPPEAEIRAKvhELLKLVQLDWLADRYPAQ---LSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 161 AIEPDVLLMDEPTSALDpistAKI-EDLVIELKKKY-----TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSM 234
Cdd:cd03296 152 AVEPKVLLLDEPFGALD----AKVrKELRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
..
gi 517187183 235 PQ 236
Cdd:cd03296 228 PA 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
4.68e-43 |
|
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: 145.94 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKaLKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNcrITGEVTLDKEDVyrdLDINVLRK 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIA---GFIKP--DSGKILLNGKDI---TNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRtHGIHNKVQLDEIVERSLKQAAIwDEVkdrLNKSALGMSGGQQQRLCIARALAI 162
Cdd:cd03299 72 DISYVPQNYALFPhMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHL---LNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERT 240
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
....
gi 517187183 241 ENYI 244
Cdd:cd03299 227 AEFL 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
6.32e-43 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 145.27 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkNCrITGEVTLDKEDV-YRDLDINVL- 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-----------NL-ISGFLRPTSGSVlFDGEDITGLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 -----RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHN---------KVQLDEIVERSLKQAAIWDevkdRLNKSALGM 146
Cdd:cd03219 69 pheiaRLGIGRTFQIPRLFPeLTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLAD----LADRPAGEL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADR 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-235 |
2.76e-42 |
|
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: 147.11 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVYRdldINVLRK 83
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDITR---LPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDrlnKSALGMSGGQQQRLCIARALAI 162
Cdd:TIGR03265 77 DYGIVFQSYALFPnLTVADNIAYGLKNRGM-GRAEVAERVAELLDLVGL-PGSER---KYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 163 EPDVLLMDEPTSALDpistAKI-EDLVIELKK-----KYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMP 235
Cdd:TIGR03265 152 SPGLLLLDEPLSALD----ARVrEHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-223 |
7.78e-42 |
|
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: 142.43 E-value: 7.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNdLVKncRITGEVTLDKEDV-----YRdldin 79
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SG-LLP--PRSGSIRFDGEDItglppHR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGihNKVQLDEIVERslkqaaIWD---EVKDRLNKSALGMSGGQQQRLC 155
Cdd:COG0410 75 IARLGIGYVPEGRRIFPsLTVEENLLLGAYARR--DRAEVRADLER------VYElfpRLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKtaFFLL--GEIV 223
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR--AYVLerGRIV 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-239 |
1.23e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 142.63 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRitGEVTLDKEDVY----RDLDI 78
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINL---LETPDS--GEIRVGGEEIRlkpdRDGEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NV--------LRKKVGMVFQKPNPFP-MSIYDNIAFGPrthgIH-NKVQLDEIVERS---LKQAAIWDevkdRLNKSALG 145
Cdd:COG4598 83 VPadrrqlqrIRTRLGMVFQSFNLWShMTVLENVIEAP----VHvLGRPKAEAIERAealLAKVGLAD----KRDAYPAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPistakieDLVIE-LK-------KKYTIVMVTHNMQQAVRISDKTAFF 217
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmrdlaeEGRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260
....*....|....*....|..
gi 517187183 218 LLGEIVEYNKTSQLFSMPQDER 239
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSER 249
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-223 |
1.43e-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: 146.02 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGD-----FKALK-------------------NINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlv 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKrperaLKLLDqgkskdeilektgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 57 kncrIT-GEVTLDKEDVY----RDLdINVLRKKVGMVFQK----PNpfpMSIYDNIAFGPRTHGIhNKVQLDEIVERSLK 127
Cdd:COG4175 79 ----PTaGEVLIDGEDITklskKEL-RELRRKKMSMVFQHfallPH---RTVLENVAFGLEIQGV-PKAERRERAREALE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 128 QaaiwdeV--KDRLNK--SALgmSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVT 201
Cdd:COG4175 150 L------VglAGWEDSypDEL--SGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELqaKLKKTIVFIT 221
|
250 260
....*....|....*....|..
gi 517187183 202 HNMQQAVRISDKTAFFLLGEIV 223
Cdd:COG4175 222 HDLDEALRLGDRIAIMKDGRIV 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
2.14e-41 |
|
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: 141.10 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD--FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNcriTGEVTLDKEDVYRDldINVL 81
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRPT---SGTAYINGYSIRTD--RKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQaaiwDEVKDRLNKSALGMSGGQQQRLCIARAL 160
Cdd:cd03263 74 RQSLGYCPQFDALFDeLTVREHLRFYARLKGLPKS-EIKEEVELLLRV----LGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-213 |
2.68e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 142.88 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-----DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCriTGEVTLDKEDVY-RDLD 77
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLLKPT--SGKIIIDGVDITdKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKKVGMVFQKP--NPFPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAI-WDEVKDrlnKSALGMSGGQQQRL 154
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGL-SEEEIENRVKRAMNIVGLdYEDYKD---KSPFELSGGQKRRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDK 213
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADR 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-223 |
1.70e-40 |
|
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: 138.66 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvknCRIT-GEVTLDKEDVYRDLDiNVlR 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL------LKPTsGRATVAGHDVVREPR-EV-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVqLDEIVERSLKQAAIWdEVKDRLNKSalgMSGGQQQRLCIARALA 161
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-231 |
5.23e-40 |
|
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: 137.75 E-value: 5.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyRDLDINVLR 82
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI-REVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGprthgihNKVQLDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRLC 155
Cdd:cd03253 75 RAIGVVPQDTVLFNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRfpdgydtIVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQL 231
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-239 |
7.09e-40 |
|
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: 144.52 E-value: 7.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVL 81
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS-----GSITLGGVDL-RDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFG-PR-ThgihnkvqlDEIVERSLKQAAIWDEVK---DRLNkSALG-----MSGGQQ 151
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLRLArPDaT---------DEELWAALERVGLGDWLAalpDGLD-TWLGeggrrLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTH------NMQQAVRISDktaffllGEIVEY 225
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHrlagleRMDRILVLED-------GRIVEQ 550
|
250
....*....|....
gi 517187183 226 NKTSQLfsMPQDER 239
Cdd:COG4987 551 GTHEEL--LAQNGR 562
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-237 |
2.94e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.46 E-value: 2.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCRitGEVTLDKEDVY---RDLDINVLRKKVGMVFQKPN 93
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLN---GLLQPTS--GTVTIGERVITagkKNKKLKPLRKKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 94 P--FPMSIYDNIAFGPRTHGIHnkvqldeiVERSLKQAAIWDEV----KDRLNKSALGMSGGQQQRLCIARALAIEPDVL 167
Cdd:PRK13634 96 HqlFEETVEKDICFGPMNFGVS--------EEDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 168 LMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQD 237
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-236 |
5.04e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 137.94 E-value: 5.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-----------GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncrIT-GEVTLDKED 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE------PTsGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 72 V--YRDLDINVLRKKVGMVFQKP----NPfPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLkqaaiwDEVkdRLNKSALG 145
Cdd:COG4608 82 ItgLSGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELL------ELV--GLRPEHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 -----MSGGQQQRLCIARALAIEPDVLLMDEPTSALDpIST-AKIEDLVIELKKKY--TIVMVTHNMqQAVR-ISDKTAF 216
Cdd:COG4608 153 rypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIqAQVLNLLEDLQDELglTYLFISHDL-SVVRhISDRVAV 230
|
250 260
....*....|....*....|
gi 517187183 217 FLLGEIVEYNKTSQLFSMPQ 236
Cdd:COG4608 231 MYLGKIVEIAPRDELYARPL 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-246 |
6.92e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.87 E-value: 6.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRitGEVTLDKEDVY--RDLD-- 77
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINF---LEKPSE--GSIVVNGQTINlvRDKDgq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 --------INVLRKKVGMVFQKPNPFP-MSIYDNIAFGP-RTHGIhNKVQLDEIVERSLKQAAIWDEVKDrlnKSALGMS 147
Cdd:PRK10619 79 lkvadknqLRLLRTRLTMVFQHFNLWShMTVLENVMEAPiQVLGL-SKQEARERAVKYLAKVGIDERAQG---KYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYN 226
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
250 260
....*....|....*....|
gi 517187183 227 KTSQLFSMPQDERTENYITG 246
Cdd:PRK10619 235 APEQLFGNPQSPRLQQFLKG 254
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-232 |
8.77e-39 |
|
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: 134.66 E-value: 8.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVL 81
Cdd:cd03254 2 EIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK-----GQILIDGIDI-RDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGprthgiHNKVQlDEIVERSLKQAAIWDEVKDR-------LNKSALGMSGGQQQRL 154
Cdd:cd03254 76 RSMIGVVLQDTFLFSGTIMENIRLG------RPNAT-DEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
9.11e-39 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.37 E-value: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFK----ALKNINLEIASNEITAFIGPSGCGKSTLLkslNRMNDLVKNCriTGEVTLDKEDVY--- 73
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGFLAPS--SGEITLDGVPVTgpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 --RdldinvlrkkvGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLK--------QAAIWDevkdrlnks 142
Cdd:COG4525 76 adR-----------GVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLAlvgladfaRRRIWQ--------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 143 algMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAV 208
Cdd:COG4525 135 ---LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEAL 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-213 |
3.17e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 134.01 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkNCrIT-------GEVTLDKEDV----- 72
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLF-----------NL-ITgfyrptsGRILFDGRDItglpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 73 YRdldinVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQ-AAIWDEV---------KDRLNK 141
Cdd:COG0411 74 HR-----IARLGIARTFQNPRLFPeLTVLENVLVAAHARLGRGLLAALLRLPRARREeREARERAeellervglADRADE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 142 SALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKK--KYTIVMVTHNMQQAVRISDK 213
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADR 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-202 |
7.32e-38 |
|
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: 138.57 E-value: 7.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyRDLDINVLR 82
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPL-ADADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGprthgihNKVQLDEIVERSLKQAAIWDEVKDR-------LNKSALGMSGGQQQRLC 155
Cdd:TIGR02857 396 DQIAWVPQHPFLFAGTIAENIRLA-------RPDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTH 202
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-223 |
7.48e-38 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 134.05 E-value: 7.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmndlvknCRIT---GEVTLDKEDVYRDLDinVLRKKVGMV 88
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLT--------TLLRptsGTARVAGYDVVREPR--KVRRSIGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 89 FQKPNPFP-MSIYDNIAFGPRTHGIHNKVqLDEIVERSLKQAAIWdEVKDRLNKsalGMSGGQQQRLCIARALAIEPDVL 167
Cdd:TIGR01188 72 PQYASVDEdLTGRENLEMMGRLYGLPKDE-AEERAEELLELFELG-EAADRPVG---TYSGGMRRRLDIAASLIHQPDVL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 168 LMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:TIGR01188 147 FLDEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-240 |
3.77e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 136.74 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-----------GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvkncRITGEVTLDKEDV 72
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 73 --YRDLDINVLRKKVGMVFQKP----NPfPMSIYDNIAFGPRTHGIH-NKVQLDEIVERSLkqaaiwDEVkdRLNKSALG 145
Cdd:COG4172 350 dgLSRRALRPLRRRMQVVFQDPfgslSP-RMTVGQIIAEGLRVHGPGlSAAERRARVAEAL------EEV--GLDPAARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 -----MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMqQAVR-ISDKTAFF 217
Cdd:COG4172 421 rypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDL-AVVRaLAHRVMVM 499
|
250 260
....*....|....*....|...
gi 517187183 218 LLGEIVEYNKTSQLFSMPQDERT 240
Cdd:COG4172 500 KDGKVVEQGPTEQVFDAPQHPYT 522
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-232 |
6.88e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 131.02 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvknCRITGEVTLDKEDVYRD---LDINVLRKKVGMVFQKPN 93
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLITSTsknKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 94 P--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKDrlnKSALGMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:PRK13649 96 SqlFEETVLKDVAFGPQNFGV-SQEEAEALAREKLALVGISESLFE---KNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 172 PTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-213 |
7.82e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 132.90 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLK---SLNRMNdlvkncriTGEVTLDKEDVYRdldINV 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRiiaGLEHQT--------SGHIRFHGTDVSR---LHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFG---------PRTHGIHNKV-QLDEIVErsLKQAAiwdevkdrlNKSALGMSGG 149
Cdd:PRK10851 72 RDRKVGFVFQHYALFRhMTVFDNIAFGltvlprrerPNAAAIKAKVtQLLEMVQ--LAHLA---------DRYPAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDpistAKIEDlviELKK---------KYTIVMVTHNMQQAVRISDK 213
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALD----AQVRK---ELRRwlrqlheelKFTSVFVTHDQEEAMEVADR 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
8.76e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 131.36 E-value: 8.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYG-----DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRM------------NDLVKNCR----- 60
Cdd:PRK13651 2 QIKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifKDEKNKKKtkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 61 -ITGEVTLDKEDVYRDLDINVLRKKVGMVFQ--KPNPFPMSIYDNIAFGPRTHGIHNKvqldEIVERSLKQAAIWDEVKD 137
Cdd:PRK13651 82 kVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 138 RLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAF 216
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|..
gi 517187183 217 FLLGEIVEYNKT 228
Cdd:PRK13651 238 FKDGKIIKDGDT 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-237 |
2.74e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 131.69 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEdvyRDLDINV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGDLFIGEK---RMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVErslkQAAIWDEVKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:PRK11000 73 AERGVGMVFQSYALYPhLSVAENMSFGLKLAGA-KKEEINQRVN----QVAEVLQLAHLLDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQD 237
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
4.45e-36 |
|
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: 127.73 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD--FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyRDLDINVL 81
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDV-RDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRL 154
Cdd:cd03251 75 RRQIGLVSQDVFLFNDTVAENIAYGRPGAT-------REEVEEAARAANAHEFIMElpegydtVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRL-STIENADRIVVLEDGKIVE 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-237 |
4.58e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.98 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFK--ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVYrdlDIn 79
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW---DV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 vlRKKVGMVFQKP-NPF-PMSIYDNIAFGPRTHGIHNkvqlDEIVERSlkQAAIwDEV--KDRLNKSALGMSGGQQQRLC 155
Cdd:PRK13635 80 --RRQVGMVFQNPdNQFvGATVQDDVAFGLENIGVPR----EEMVERV--DQAL-RQVgmEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
....
gi 517187183 234 MPQD 237
Cdd:PRK13635 230 SGHM 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-240 |
9.36e-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: 132.89 E-value: 9.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKS-TLLKSLNRMNDlvKNCRITGEVTLDKEDVyRDLDI 78
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPD--PAAHPSGSILFDGQDL-LGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NVLRK----KVGMVFQKP----NPFpMSIYDNIAFGPRTH-GIHNKVQLDEIVERsLKQAAIwDEVKDRLNKSALGMSGG 149
Cdd:COG4172 84 RELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHrGLSGAAARARALEL-LERVGI-PDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNK 227
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250
....*....|...
gi 517187183 228 TSQLFSMPQDERT 240
Cdd:COG4172 241 TAELFAAPQHPYT 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-212 |
2.25e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 127.16 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdLVKNCRIT---GEVTLDKEdvyrdld 77
Cdd:PRK13647 3 NIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKvmgREVNAENE------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 iNVLRKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDeVKDrlnKSALGMSGGQQQRLC 155
Cdd:PRK13647 75 -KWVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWD-FRD---KPPYHLSYGQKKRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISD 212
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWAD 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-207 |
3.71e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.52 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmNDLVKNCRITGEVTLDKEDVYrdlDINVLRKK 84
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLT---ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQKPNPFP-MSIYDNIAFG-PRTHGIHNKvqlDEIVERSLKQAaiwdEVKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlPPTIGRAQR---RARVEQALEEA----GLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQA 207
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDA 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-225 |
5.15e-35 |
|
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: 124.33 E-value: 5.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIA---SNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKE---DVYRDLDINVLRKKVGMVFQ 90
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDG-----GTIVLNGTvlfDSRKKINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 91 KPNPFP-MSIYDNIAFG-PRTHGIHNKVQLDEIVERslkqAAIwDEVKDRlnkSALGMSGGQQQRLCIARALAIEPDVLL 168
Cdd:cd03297 83 QYALFPhLNVRENLAFGlKRKRNREDRISVDELLDL----LGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 169 MDEPTSALDPISTAKIEDLVIELKKKYTIVM--VTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVifVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-205 |
8.42e-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: 123.90 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDL-YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV--YRDLDINV 80
Cdd:TIGR02673 2 IEFHNVSKaYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSR-----GQVRIAGEDVnrLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:TIGR02673 77 LRRRIGVVFQDFRLLPdRTVYENVALPLEVRGK-KEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQ 205
Cdd:TIGR02673 152 IVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATHDLS 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-222 |
1.09e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyrdLDINVLRK 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI---THVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFG------------PRTHGIHNKVQLDEIVERSLKQaaiwdevkdrlnksalgMSGGQ 150
Cdd:PRK09452 87 HVNTVFQSYALFPhMTVFENVAFGlrmqktpaaeitPRVMEALRMVQLEEFAQRKPHQ-----------------LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDpistAKI-EDLVIELK---KKY--TIVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD----YKLrKQMQNELKalqRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-207 |
1.19e-34 |
|
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: 122.92 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNcrITGEVTLDKEDV-YRDLDINVLRKKVGMVFQ 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN---GLLRP--QSGAVLIDGEPLdYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 91 KPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIARALAIEPDVLL 168
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNLGL-SEAEVERRVREALTAVGA-SGLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517187183 169 MDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQA 207
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-243 |
2.02e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 124.89 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 15 DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCriTGEVTLDKEDVY---RDLDINVLRKKVGMVFQK 91
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNIN---ALLKPT--TGTVTVDDITIThktKDKYIRPVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 92 PNP--FPMSIYDNIAFGPRTHGIHnkvqLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLM 169
Cdd:PRK13646 94 PESqlFEDTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 170 DEPTSALDPISTAKIEDLV--IELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSmpQDERTENY 243
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADW 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-203 |
2.61e-34 |
|
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: 122.52 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDV--YRDLDINV 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL-----PTSGTIRVNGQDVsdLRGRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvqldEIVERSlkqAAIWDEV--KDRLNKSALGMSGGQQQRLCIA 157
Cdd:cd03292 76 LRRKIGVVFQDFRLLPdRNVYENVAFALEVTGVPPR----EIRKRV---PAALELVglSHKHRALPAELSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517187183 158 RALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHN 203
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHA 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
1.78e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFK--ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNcrITGEVTLDKEDVYRDlDINVL 81
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILT---GLLKP--QSGEIKIDGITISKE-NLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKP-NPF-PMSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:PRK13632 82 RKKIGIIFQNPdNQFiGATVEDDIAFGLENKKVPPK-KMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVrISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-242 |
2.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.72 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV-YRDLDINVL 81
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS-----GEVLIKGEPIkYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:PRK13639 77 RKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDE 238
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
....
gi 517187183 239 RTEN 242
Cdd:PRK13639 232 RKAN 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-246 |
3.72e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.99 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGD-----FK-------------------ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKn 58
Cdd:PRK10070 4 KLEIKNLYKIFGEhpqraFKyieqglskeqilektglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 59 critGEVTLDKEDVYRDLDIN---VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVErSLKQAAIWDE 134
Cdd:PRK10070 83 ----GQVLIDGVDIAKISDAElreVRRKKIAMVFQSFALMPhMTVLDNTAFGMELAGINAEERREKALD-ALRQVGLENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 135 VKDRLNKsalgMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISD 212
Cdd:PRK10070 158 AHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGD 233
|
250 260 270
....*....|....*....|....*....|....
gi 517187183 213 KTAFFLLGEIVEYNKTSQLFSMPQDERTENYITG 246
Cdd:PRK10070 234 RIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-204 |
3.92e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.49 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNcrITGEVTLDKEDV-YRDLDIN 79
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN---GILKP--SSGRILFDGKPIdYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIwDEVKdrlNKSALGMSGGQQQRLCIA 157
Cdd:PRK13636 79 KLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPED-EVRKRVDNALKRTGI-EHLK---DKPTHCLSFGQKKRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 158 RALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNM 204
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDI 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-223 |
4.98e-33 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 119.13 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDfkALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmnDLVKNCRI--TGEVTLDKEDVYRdldINVL 81
Cdd:cd03298 1 VRLDKIRFSYGE--QPMHFDLTFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLINGVDVTA---APPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFP-MSIYDNIAFGpRTHGIHNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIARAL 160
Cdd:cd03298 69 DRPVSMLFQENNLFAhLTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGL-AGLEKRLPGE---LSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-204 |
1.47e-32 |
|
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: 116.93 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKA--LKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndLVKNCRIT-GEVTLDKEDVyRDLDINV 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARL------ILGLLRPTsGRVRLDGADI-SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIafgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARAL 160
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNM 204
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRP 156
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-244 |
1.54e-32 |
|
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: 120.68 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 35 IGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyrdldINV--LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHG 111
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDV-----TNVppHLRHINMVFQSYALFPhMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 112 IHNkvqlDEIVERsLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDpistAKIEDLV-IE 190
Cdd:TIGR01187 72 VPR----AEIKPR-VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMqLE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 191 LKKKY-----TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENYI 244
Cdd:TIGR01187 143 LKTIQeqlgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4-212 |
1.85e-32 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 121.36 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIkNLDLYYGDFkALkNINLEIASNEITAFIGPSGCGKSTLLKS---LNRMNDlvkncritGEVTLDKEDVY-RDLDIN 79
Cdd:COG4148 3 LEV-DFRLRRGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERPDS--------GRIRLGGEVLQdSARGIF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VL--RKKVGMVFQKPNPFP-MSIYDNIAFG-PRTHGIHNKVQLDEIVErslkqaaiWDEVKDRLNKSALGMSGGQQQRLC 155
Cdd:COG4148 72 LPphRRRIGYVFQEARLFPhLSVRGNLLYGrKRAPRAERRISFDEVVE--------LLGIGHLLDRRPATLSGGERQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISD 212
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLAD 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-225 |
2.21e-32 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 117.59 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDL-YYGDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINV 80
Cdd:cd03244 2 DIEFKNVSLrYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS-----GSILIDGVDI-SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAFgprtHGIHNkvqlDEIVERSLKQAAIWDEVKDRLNK-------SALGMSGGQQQR 153
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLDP----FGEYS----DEELWQALERVGLKEFVESLPGGldtvveeGGENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHnmqqavRI-----SDKTAFFLLGEIVEY 225
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVVEF 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
4.07e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.57 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLN----------RMNDLVKNCRITGEVTLD 68
Cdd:PRK13631 22 LRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNglikskygtiQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 69 KEDVYRDLDINVLRKKVGMVFQKP--NPFPMSIYDNIAFGPRTHGIHNkvqldeivERSLKQAAIWDEV----KDRLNKS 142
Cdd:PRK13631 102 NPYSKKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK--------SEAKKLAKFYLNKmgldDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 143 ALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGE 221
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|.
gi 517187183 222 IVEYNKTSQLF 232
Cdd:PRK13631 254 ILKTGTPYEIF 264
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
4.20e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 118.37 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLD-LYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCriTGEVTLDKEDVYRDlDIN 79
Cdd:PRK13652 1 MHLIETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN---GILKPT--SGSVLIRGEPITKE-NIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIA 157
Cdd:PRK13652 75 EVRKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 158 RALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMP 235
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-235 |
4.44e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.21 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKslnrmndLVKNCR--ITGEVTLDKEDVyrdLDIN 79
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDV---THRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNkvqlDEIVERslkqaaiwdeVKDRLNKSALG---------MSGG 149
Cdd:PRK11432 75 IQQRDICMVFQSYALFPhMSLGENVGYGLKMLGVPK----EERKQR----------VKEALELVDLAgfedryvdqISGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNK 227
Cdd:PRK11432 141 QQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
....*...
gi 517187183 228 TSQLFSMP 235
Cdd:PRK11432 221 PQELYRQP 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
5.23e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.83 E-value: 5.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKncRITGEVTLDKEDVYRDLDINVLRK 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS---GLYK--PDSGEILVDGKEVSFASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQkpnpfpmsiydniafgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARALAIE 163
Cdd:cd03216 76 GIAMVYQ-------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-236 |
5.50e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.39 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-----DFKALKNINLEIASNEITAFIGPSGCGKSTLLKslnRMNDLVKNCriTGEVTLDKEDVYRDL-- 76
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQ---HFNALLKPS--SGTITIAGYHITPETgn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 -DINVLRKKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIWDEVkdrLNKSALGMSGGQQQR 153
Cdd:PRK13641 78 kNLKKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
....
gi 517187183 233 SMPQ 236
Cdd:PRK13641 234 SDKE 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-232 |
5.86e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 118.68 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDvyRDLDINVLRKKVGMVFQKPNP-- 94
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS--KQKEIKPVRKKVGVVFQFPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdeVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTS 174
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGI-PKEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 175 ALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-212 |
7.67e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 7.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLN---RMNdlvkncriTGEVTLDKEDVYRDLDINV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyQPD--------SGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIAFG--PRTHGIHNKVQLDEIVERSLKQ--AAI--WDEVKDrlnksalgMSGGQQQR 153
Cdd:COG1129 77 QAAGIAIIHQELNLVPnLSVAENIFLGrePRRGGLIDWRAMRRRARELLARlgLDIdpDTPVGD--------LSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISD 212
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIAD 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-233 |
9.35e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 117.80 E-value: 9.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 15 DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLdKEDVYRDLDINVLRKKVGMVFQKP-- 92
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLKKIKEVKRLRKEIGLVFQFPey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 NPFPMSIYDNIAFGPRTHGiHNKVQLDEIVERSLKQAAIwdeVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:PRK13645 102 QLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 173 TSALDPISTAKIEDLVIELKKKYT--IVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-224 |
1.34e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 114.33 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG--DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmnDLVKNcriTGEVTLDKEDV--YRDLdin 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVsdLEKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 vLRKKVGMVFQKPNPFPMSIYDNIafGPRthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARA 159
Cdd:cd03247 73 -LSSLISVLNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIM 176
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-202 |
1.35e-31 |
|
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: 116.34 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRIT--GEvTLDKEDVyRDLdinvl 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfGE-RRGGEDV-WEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMV---FQKPNPFPMSIYDNI---AFGprTHGIHNKVQlDEIVERSLKQAAIWDeVKDRLNKSALGMSGGQQQRLC 155
Cdd:COG1119 77 RKRIGLVspaLQLRFPRDETVLDVVlsgFFD--SIGLYREPT-DEQRERARELLELLG-LAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTH 202
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH 201
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-231 |
1.38e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.99 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGD--FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndLVKNCRITGEVTLDKEDVyRDLDINV 80
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDL-AGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAfgprthgIHNKVQLDEIVErSLKQAAIWDEVKDR-------LNKSALGMSGGQQQR 153
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIA-------GGAPLTLDEAWE-AARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAkiedLVIE-LKK-KYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQA----IVSEsLERlKVTRIVIAHRL-STIRNADRIYVLDAGRVVQQGTYDEL 671
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-212 |
1.40e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDvYRDLDINVLR 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-----SGTVFLGDKP-ISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQK-PNPFPMSIYDNIAFGPRTHGIH--NKVQLDE-IVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIAR 158
Cdd:PRK11231 76 RRLALLPQHhLTPEGITVRELVAYGRSPWLSLwgRLSAEDNaRVNQAMEQTRI-NHLADRRLTD---LSGGQRQRAFLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISD 212
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCD 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-202 |
1.76e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 114.98 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIaSNEITAFIGPSGCGKSTLLKSLnrmndlvknCRIT----GEVTLDKEDVYRDLDin 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRIL---------ATLTppssGTIRIDGQDVLKQPQ-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIAR 158
Cdd:cd03264 69 KLRRRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSK-EVKARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTH 202
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-204 |
1.87e-31 |
|
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: 115.38 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGD--FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDvYRDLDINV 80
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS-----GSVLLDGTD-IRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAFGprtHGIHNkvqlDEIVERSLKQAAIWDEVKDRLNKSAL-------GMSGGQQQR 153
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLG---APLAD----DERILRAAELAGVTDFVNKHPNGLDLqigergrGLSGGQRQA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNM 204
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-231 |
4.71e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndlvkncrIT----GEVTLDKEDVyRDLDIN 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG---------ILapdsGEVLWDGEPL-DPEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 V---------LRKKvgmvfqkpnpfpMSIYDNIAFGPRTHGIHN---KVQLDEIVERsLkqaaiwdEVKDRLNKSALGMS 147
Cdd:COG4152 72 RigylpeergLYPK------------MKVGEQLVYLARLKGLSKaeaKRRADEWLER-L-------GLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYN 226
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*
gi 517187183 227 KTSQL 231
Cdd:COG4152 212 SVDEI 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-223 |
1.05e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 112.74 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDL-YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRdldiNVLRK 83
Cdd:cd03226 1 RIENISFsYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS-----GSILLNGKPIKA----KERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNP--FPMSIYDNIAFGPRthGIHNKvqlDEIVERSLKQAAIWDEvKDRLNKSalgMSGGQQQRLCIARALA 161
Cdd:cd03226 72 SIGYVMQDVDYqlFTDSVREELLLGLK--ELDAG---NEQAETVLKDLDLYAL-KERHPLS---LSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-244 |
1.07e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.86 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYrdlDINVLRK 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTA-----GQIMLDGVDLS---HVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRthgiHNKVQLDEIVERSLKQAAIWdEVKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:PRK11607 92 PINMMFQSYALFPhMTVEQNIAFGLK----QDKLPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERT 240
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
....
gi 517187183 241 ENYI 244
Cdd:PRK11607 247 AEFI 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-236 |
1.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFK--ALKNINLEIASNEITAFIGPSGCGKSTLLKSLN--RMNDLVKNCRITGE-VTLDKEDVYrdl 76
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINglLLPDDNPNSKITVDgITLTAKTVW--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DInvlRKKVGMVFQKP-NPF-PMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKdrlnKSALGMSGGQQQRL 154
Cdd:PRK13640 81 DI---REKVGIVFQNPdNQFvGATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYID----SEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVrISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIF 231
|
....
gi 517187183 233 SMPQ 236
Cdd:PRK13640 232 SKVE 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-208 |
2.66e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.03 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFK------ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndLVKNcriTGEVTLDKEDVYRD 75
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPS---EGKVYVDGLDTSDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDINVLRKKVGMVFQKP-NPFPMSIYD-NIAFGPRTHGIHNKvQLDEIVERSLKQAAIWDevkdrLNKSALGM-SGGQQQ 152
Cdd:PRK13633 78 ENLWDIRNKAGMVFQNPdNQIVATIVEeDVAFGPENLGIPPE-EIRERVDESLKKVGMYE-----YRRHAPHLlSGGQKQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAV 208
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAV 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-224 |
3.82e-30 |
|
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: 112.23 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNdLVKNCRitGEVTLDKEDVYRDLDINVLRKK 84
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MG-LLPVKS--GSIRLDGEDITKLPPHERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERslkqaaiWDEVKDRLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:TIGR03410 77 IAYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL-------FPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-231 |
5.60e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 117.52 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYY---GDFKALKNINLEIASNEITAFIGPSGCGKST---LLKSLNRMNdlvkncriTGEVTLDKEDVyRDL 76
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPT--------GGQVLLDGVPL-VQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIWDEVKDRLN--KSALG-----MSGG 149
Cdd:TIGR00958 549 DHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-------DEEIMAAAKAANAHDFIMEFPNgyDTEVGekgsqLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDpistAKIEDLVIELKKKY--TIVMVTHNMqQAVRISDKTAFFLLGEIVEYNK 227
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRAsrTVLLIAHRL-STVERADQILVLKKGSVVEMGT 696
|
....
gi 517187183 228 TSQL 231
Cdd:TIGR00958 697 HKQL 700
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-210 |
1.31e-29 |
|
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: 110.64 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYY---GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDIN 79
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG-----GQVLLDGKPI-SQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFPMSIYDNIAFGPRThgihnkVQLDEIVERSLKQAA----------IWDEVKDRLNKsalgMSGG 149
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS------CSFECVKEAAQKAHAhsfiselasgYDTEVGEKGSQ----LSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNM---QQAVRI 210
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLstvERADQI 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-233 |
1.68e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 110.65 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG--DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndLVKNcriTGEVTLDKEDVyRDLDINVL 81
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPE---NGRVLVDGHDL-ALADPAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAF---GPRTHGIHNKVQLDEIVERSLKQAAIWDEVkdrLNKSALGMSGGQQQRLCIAR 158
Cdd:cd03252 75 RRQVGVVLQENVLFNRSIRDNIALadpGMSMERVIEAAKLAGAHDFISELPEGYDTI---VGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-228 |
3.13e-29 |
|
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: 109.18 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 23 NLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVYRdldINVLRKKVGMVFQKPNPFP-MSIYD 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPA-----SGSIKVNDQSHTG---LAPYQRPVSMLFQENNLFAhLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 102 NIAFGprthgIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPIST 181
Cdd:TIGR01277 90 NIGLG-----LHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 182 AKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKT 228
Cdd:TIGR01277 165 EEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-205 |
3.46e-29 |
|
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: 115.35 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDL-YYGDF-KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINV 80
Cdd:TIGR03375 463 EIEFRNVSFaYPGQEtPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE-----GSVLLDGVDI-RQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIWDEVKD-------RLNKSALGMSGGQQQR 153
Cdd:TIGR03375 537 LRRNIGYVPQDPRLFYGTLRDNIALGAPYAD-------DEEILRAAELAGVTEFVRRhpdgldmQIGERGRSLSGGQRQA 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQ 205
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-237 |
3.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKI-EIKNLDLYY---GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKN-CRITGEvTLDKEDVYRd 75
Cdd:PRK13642 1 MNKIlEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkVKIDGE-LLTAENVWN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 ldinvLRKKVGMVFQKP-NPF-PMSIYDNIAFGPRTHGIHNkvqlDEIVERsLKQAAIWDEVKDRLNKSALGMSGGQQQR 153
Cdd:PRK13642 79 -----LRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPR----EEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQL 231
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
....*.
gi 517187183 232 FSMPQD 237
Cdd:PRK13642 228 FATSED 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-224 |
4.28e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 114.67 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVyRDLDINVLRKKVGMVFQK 91
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD-----PQSGRILIDGTDI-RTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 92 PNPFPMSIYDNIAFGPRThgihnkvQLDEIVERSLKQAAIWDEVKDRLNK--SALG-----MSGGQQQRLCIARALAIEP 164
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPD-------ATDEEMRAAAERAQAHDFIERKPDGydTVVGergrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 165 DVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-203 |
7.35e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 113.61 E-value: 7.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYrDLDINVLRKKVGMVFQK 91
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 92 PNPFPMSIYDNIAFGprthgihNKVQLDEIVERSLKQA--AIW-DEVKDRLNKSALGM----SGGQQQRLCIARALAIEP 164
Cdd:TIGR02868 418 AHLFDTTVRENLRLA-------RPDATDEELWAALERVglADWlRALPDGLDTVLGEGgarlSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517187183 165 DVLLMDEPTSALDPiSTAK--IEDLVIELKKKyTIVMVTHN 203
Cdd:TIGR02868 491 PILLLDEPTEHLDA-ETADelLEDLLAALSGR-TVVLITHH 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-233 |
1.05e-28 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 113.66 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYG--DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINV 80
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS-----GQILLDGHDL-ADYTLAS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIAFGprthgihnkvQLDEIVERSLKQAAIWDEVKDRLNKSALG-----------MSGG 149
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYG----------RTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTS 229
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHN 552
|
....
gi 517187183 230 QLFS 233
Cdd:TIGR02203 553 ELLA 556
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-224 |
1.23e-28 |
|
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: 107.69 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLK---SLNRMNdlvkncriTGEVTLDKEDVYRDLDINv 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKiilGLIKPD--------SGEITFDGKSYQKNIEAL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 lrKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhnkvqLDEIVERSLKQAAIWDEVKDRLNKSALGMsggqQQRLCIARA 159
Cdd:cd03268 72 --RRIGALIEAPGFYPnLTARENLRLLARLLGI-----RKKRIDEVLDVVGLKDSAKKKVKGFSLGM----KQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-246 |
1.24e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.08 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKslnrmndlvkncRITGEVTLDKEDVYRDLDiNV 80
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLR------------LIGGQIAPDHGEILFDGE-NI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 ----------LRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHgihnkVQLDEIVERS---LKQAAIWDEVKDRLNKSALgm 146
Cdd:PRK11831 72 pamsrsrlytVRKRMSMLFQSGALFTdMNVFDNVAYPLREH-----TQLPAPLLHStvmMKLEAVGLRGAAKLMPSEL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKtAFFLLGEIVE 224
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIADH-AYIVADKKIV 223
|
250 260
....*....|....*....|..
gi 517187183 225 YNKTSQLFSMPQDERTENYITG 246
Cdd:PRK11831 224 AHGSAQALQANPDPRVRQFLDG 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-237 |
1.46e-28 |
|
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: 109.12 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRdLD---INVLRKKVGMVFQKP--- 92
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQ-----GTVSFRGQDLYQ-LDrkqRRAFRRDVQLVFQDSpsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 -NPfPMSIYDNIAfgprtHGIHNKVQLDEiVERSLKQAAIWDEVK---DRLNKSALGMSGGQQQRLCIARALAIEPDVLL 168
Cdd:TIGR02769 101 vNP-RMTVRQIIG-----EPLRHLTSLDE-SEQKARIAELLDMVGlrsEDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 169 MDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQD 237
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHP 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-202 |
1.51e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 110.70 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNL-DLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnRMndlVKNC-RIT-GEVTLDKEDVY---- 73
Cdd:PRK11650 1 MAGLKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL----RM---VAGLeRITsGEIWIGGRVVNelep 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 RDLDInvlrkkvGMVFQKPNPFP-MSIYDNIAFGPRTHGihnkVQLDEIVERSLKQAAIWdEVKDRLNKSALGMSGGQQQ 152
Cdd:PRK11650 74 ADRDI-------AMVFQNYALYPhMSVRENMAYGLKIRG----MPKAEIEERVAEAARIL-ELEPLLDRKPRELSGGQRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDpistAKIE-DLVIELKK-----KYTIVMVTH 202
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD----AKLRvQMRLEIQRlhrrlKTTSLYVTH 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-206 |
2.25e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 112.63 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKAL-KNINLEIASNEITAFIGPSGCGKSTLLkslnrmNDLVKNCRITGEVTLDKEDVyRDLDINVLR 82
Cdd:PRK11174 350 IEAEDLEILSPDGKTLaGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIEL-RELDPESWR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGprthgihnKVQL-DEIVERSLKQAAIWD-----------EVKDRlnksALGMSGGQ 150
Cdd:PRK11174 423 KHLSWVGQNPQLPHGTLRDNVLLG--------NPDAsDEQLQQALENAWVSEflpllpqgldtPIGDQ----AAGLSVGQ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQ 206
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-205 |
2.77e-28 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 106.40 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVYrdldi 78
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA------------LLGELEKLSGSVS----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 nvLRKKVGMVFQKPNPFPMSIYDNIAFGPRthgiHNKVQLDEIV-----ERSLKQAAIWD--EVKDRlnksALGMSGGQQ 151
Cdd:cd03250 64 --VPGSIAYVSQEPWIQNGTIRENILFGKP----FDEERYEKVIkacalEPDLEILPDGDltEIGEK----GINLSGGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVI--ELKKKYTIVMVTHNMQ 205
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQ 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-223 |
8.30e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.91 E-value: 8.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCriTGEVTLDKEDVYRDlDIN 79
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA---GLLEPD--AGFATVDGFDVVKE-PAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKkVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHN---KVQLDEIVERSlkqaaiwdEVKDRLNKSALGMSGGQQQRLC 155
Cdd:cd03266 76 ARRR-LGFVSDSTGLYDrLTARENLEYFAGLYGLKGdelTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
1.03e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKncRITGEVTLDKEDVyRDLDINVLRK 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---LLP--PDSGEVLVDGLDV-ATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKpNPFPM--SIYDNIAFG--PRTHGIHNKvQLDEIVERSLKQAAIwDEVKDR-LNKsalgMSGGQQQRLCIAR 158
Cdd:COG4604 76 RLAILRQE-NHINSrlTVRELVAFGrfPYSKGRLTA-EDREIIDEAIAYLDL-EDLADRyLDE----LSGGQRQRAFIAM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 159 ALAIEPDVLLMDEPTSALDP---ISTAKI-EDLVIELKKkyTIVMVTHNMQQAVRISD 212
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMkhsVQMMKLlRRLADELGK--TVVIVLHDINFASCYAD 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-202 |
1.05e-27 |
|
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: 105.25 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRI--------TGEVTLDKEDVYRD 75
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLL-------------RIlagllppsAGEVLWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDInvLRKKVGMVFQKPNPFP-MSIYDNIAFgprTHGIHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRL 154
Cdd:COG4133 70 RED--YRRRLAYLGHADGLKPeLTVRENLRF---WAALYGLRADREAIDEALEAVGL----AGLADLPVRQLSAGQKRRV 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIE-LKKKYTIVMVTH 202
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-202 |
1.69e-27 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 104.80 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDV----YRDlDINVLRKKVGMVFQKP 92
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSL-----DSGSLTLAGKEVtnlsYSQ-KIILRRELIGYIFQSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 NPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:NF038007 93 NLIPhLSIFDNVALPLKYRGV-AKKERIERVNQVLNLFGI----DNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADE 167
|
170 180 190
....*....|....*....|....*....|..
gi 517187183 172 PTSALDPIST-AKIEDLVIELKKKYTIVMVTH 202
Cdd:NF038007 168 PTGNLDSKNArAVLQQLKYINQKGTTIIMVTH 199
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-210 |
2.24e-27 |
|
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: 104.23 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLDI---NVLR 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDS-----GQVYLNGQETPPLNSKkasKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKpnpFPM----SIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIAR 158
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGLKYKKL-SKKEKREKKKEALEKVGL----NLKLKQKIYELSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNM---QQAVRI 210
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-223 |
2.36e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.84 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 7 KNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLDINVLRkKVG 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH-----GHVWLDGEHIQHYASKEVAR-RIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 87 MVFQKP-NPFPMSIYDNIAFGPRTHG---IHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:PRK10253 85 LLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI----THLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-235 |
2.58e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.12 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCRITGEVTLDKEDV--YR 74
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREIlnLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 75 DLDINVLR-KKVGMVFQKP----NPFpMSIYDNIAfgpRTHGIHNKVQLDEIVERSLK--QAAIWDEVKDRLNKSALGMS 147
Cdd:PRK09473 88 EKELNKLRaEQISMIFQDPmtslNPY-MRVGEQLM---EVLMLHKGMSKAEAFEESVRmlDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250
....*....|
gi 517187183 226 NKTSQLFSMP 235
Cdd:PRK09473 244 GNARDVFYQP 253
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-202 |
2.86e-27 |
|
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: 103.78 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCRITGEVTLDKedvyRDLDINVLRKKVGMVFQkpnpfpms 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---GRRTGLGVSGEVLING----RPLDKRSFRKIIGYVPQ-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 iyDNIAFGPRThgihnkvqldeiVERSLKQAAiwdEVKdrlnksalGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDP 178
Cdd:cd03213 90 --DDILHPTLT------------VRETLMFAA---KLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180
....*....|....*....|....*
gi 517187183 179 ISTAKIEDLVIELKKK-YTIVMVTH 202
Cdd:cd03213 145 SSALQVMSLLRRLADTgRTIICSIH 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-233 |
4.53e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 23 NLEIASNEITAFIGPSGCGKSTLLkSLnrmndlvkncrITGEVTLDKEDVYrdldIN--------VLRKKVGMVFQKPNP 94
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL-NL-----------IAGFLTPASGSLT----LNgqdhtttpPSRRPVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FP-MSIYDNIAFGprthgIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPT 173
Cdd:PRK10771 83 FShLTVAQNIGLG-----LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 174 SALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-224 |
4.82e-27 |
|
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: 104.05 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKA----LKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRI--------TGEVTLDKED 71
Cdd:COG4181 9 IELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLL-------------GLlagldrptSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 72 VYRdLDIN----VLRKKVGMVFQK----PNpfpMSIYDNIAfgprthgihnkVQLdEIVERS--LKQAAIW-DEV--KDR 138
Cdd:COG4181 76 LFA-LDEDararLRARHVGFVFQSfqllPT---LTALENVM-----------LPL-ELAGRRdaRARARALlERVglGHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 139 LNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQA------VRI 210
Cdd:COG4181 140 LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAarcdrvLRL 219
|
250
....*....|....
gi 517187183 211 SDktaffllGEIVE 224
Cdd:COG4181 220 RA-------GRLVE 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-208 |
6.80e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.45 E-value: 6.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYY-GDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvkncritgEVTLDKEDVYRDLDIN 79
Cdd:PRK13648 6 SIIVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----------EKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 V-----LRKKVGMVFQKP-NPFPMSI--YDnIAFGPRTHGI-HNKVQldEIVERSLKQAaiwdEVKDRLNKSALGMSGGQ 150
Cdd:PRK13648 75 DdnfekLRKHIGIVFQNPdNQFVGSIvkYD-VAFGLENHAVpYDEMH--RRVSEALKQV----DMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELK--KKYTIVMVTHNMQQAV 208
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAM 207
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-224 |
1.79e-26 |
|
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: 107.34 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKA--LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLD---KEDVYRDld 77
Cdd:TIGR03796 477 YVELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ-----PWSGEILFDgipREEIPRE-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 inVLRKKVGMVFQKPNPFPMSIYDNIAFGPRThgihnkvQLDEIVERSLKQAAIWDEVKDR-------LNKSALGMSGGQ 150
Cdd:TIGR03796 550 --VLANSVAMVDQDIFLFEGTVRDNLTLWDPT-------IPDADLVRACKDAAIHDVITSRpggydaeLAEGGANLSGGQ 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDlviELKKK-YTIVMVTHNMqQAVRISDKTAFFLLGEIVE 224
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDPETEKIIDD---NLRRRgCTCIIVAHRL-STIRDCDEIIVLERGKVVQ 691
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-223 |
1.81e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.65 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmNDLVKNCRIT-GEVTLDKEDVYRDLDINVLR 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLL------GTLCGDPRATsGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIAFGPRthgIHNKVQLDEIVERSLkqaAIWDEVKDRLNKSALGMSGGQQQRLCIARALA 161
Cdd:PRK11614 80 EAVAIVPEGRRVFSrMTVEENLAMGGF---FAERDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-224 |
2.25e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 102.16 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLkslNRMNDLVKNCriTGEVTLDKEDVYR-DLDINVlrkkvgmVFQKPNPFP- 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL---NLISGLAQPT--SGGVILEGKQITEpGPDRMV-------VFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 MSIYDNIAFG-PRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIARALAIEPDVLLMDEPTSA 175
Cdd:TIGR01184 69 LTVRENIALAvDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 176 LDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISDKTAFFL------LGEIVE 224
Cdd:TIGR01184 145 LDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTngpaanIGQILE 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-224 |
2.50e-26 |
|
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: 107.13 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVyRDLDINVLR 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSL-KDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFPMSIYDNIAFGPRthgihNKVQLDEIVeRSLKQAAIWDEVKD-------RLNKSALGMSGGQQQRLC 155
Cdd:TIGR01193 548 QFINYLPQEPYIFSGSILENLLLGAK-----ENVSQDEIW-AACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKyTIVMVTHNMQQAVRiSDKTAFFLLGEIVE 224
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-239 |
3.25e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.45 E-value: 3.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD--FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINVL 81
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP-----QQGEILLNGQPI-ADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFG------PRTHGIHNKVQLDEIVERslkqaaiwdevKDRLNkSALG-----MSGGQ 150
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLLLAapnasdEALIEVLQQVGLEKLLED-----------DKGLN-AWLGeggrqLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHN------MQQAVRISDktaffllGEIVE 224
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRltgleqFDRICVMDN-------GQIIE 553
|
250
....*....|....*
gi 517187183 225 YNKTSQLfsMPQDER 239
Cdd:PRK11160 554 QGTHQEL--LAQQGR 566
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-240 |
6.63e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.71 E-value: 6.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKE--DVYRDLDINVLRKKVGMVFQKP--- 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG-----GEIIFNGQriDTLSPGKLQALRRDIQFIFQDPyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 -NPfPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKSalgMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:PRK10261 414 lDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 172 PTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERT 240
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-236 |
7.33e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCriTGEVTLDKEDVYR--DLDINVLRKKVGMVFQKP-- 92
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKAT--DGEVAWLGKDLLGmkDDEWRAVRSDIQMIFQDPla 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 --NPfPMSIYDNIAFGPRTHgiHNKVQLDEIVERslkqaaiwdeVKDRLNKSAL----------GMSGGQQQRLCIARAL 160
Cdd:PRK15079 110 slNP-RMTIGEIIAEPLRTY--HPKLSRQEVKDR----------VKAMMLKVGLlpnlinryphEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-225 |
7.68e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.43 E-value: 7.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndlvkncritgevtldkedvyrdldinVLRK 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG----------------------------IILP 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFPMSIYDNIAFGPRTHGIHNKVQLDEIVE-----RSLKQAAIWDEVKDRLNKSALG---------MSGG 149
Cdd:cd03269 53 DSGEVLFDGKPLDIAARNRIGYLPEERGLYPKMKVIDQLVylaqlKGLKKEEARRRIDEWLERLELSeyankrveeLSKG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:cd03269 133 NQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-231 |
8.74e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 105.10 E-value: 8.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVL 81
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE-----GEILLDGHDL-RDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFGPRthgihNKVQLDEIvERSLKQAAIWD---EVKDRLN----KSALGMSGGQQQRL 154
Cdd:PRK11176 416 RNQVALVSQNVHLFNDTIANNIAYART-----EQYSREQI-EEAARMAYAMDfinKMDNGLDtvigENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHnmqqavRIS--DKTAFFLL---GEIVEYNKTS 229
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStiEKADEILVvedGEIVERGTHA 563
|
..
gi 517187183 230 QL 231
Cdd:PRK11176 564 EL 565
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-178 |
1.16e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.96 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmnDLVKNcriTGEVTLDKEDVyRDLDINVLRK 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL-AAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPN-PFPMSIYDNIAFGpRTHGIHNKVQLDEIVERSLKQAAIWDeVKDRlnkSALGMSGGQQQRLCIARALA- 161
Cdd:COG4559 76 RRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGR---SYQTLSGGEQQRVQLARVLAq 150
|
170 180
....*....|....*....|...
gi 517187183 162 ------IEPDVLLMDEPTSALDP 178
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDL 173
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-224 |
1.56e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslNRMNDLVKNCriTGEVTLDKEDVyrdldiNVLRK 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVPYQ--HGSITLDGKPV------EGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAA--------IWDevkdrlnksalgMSGGQQQRL 154
Cdd:PRK11248 71 ERGVVFQNEGLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGlegaekryIWQ------------LSGGQRQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAVRISdkTAFFLL----GEIVE 224
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEAVFMA--TELVLLspgpGRVVE 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-225 |
1.76e-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: 99.41 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDF--KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINV 80
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-----EEGKIEIDGIDI-STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIafgprthGIHNKVQLDEIVErSLkqaaiwdevkdRLNKSALGMSGGQQQRLCIARAL 160
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNL-------DPFDEYSDEEIYG-AL-----------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEY 225
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRL-RTIIDYDKILVMDAGEVKEY 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-222 |
3.64e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 99.75 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKedvyrdldinvLRKKV 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----------AREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 86 GMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVErslkqaaiwdeVKDRLNKSALGMSGGQQQRLCIARALAIEP 164
Cdd:PRK11247 84 RLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVG-----------LADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 165 DVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-223 |
4.46e-25 |
|
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: 98.88 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNcrITGEVTLDKEDVYRDLdinvLRKKVGMVFQKPNPFP 96
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT--TSGQILFNGQPRKPDQ----FQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 -MSIYDNIAFGP--RTHGIHNKVQLDEIVE-RSLKQAAIWDeVKDRLNKsalGMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:cd03234 95 gLTVRETLTYTAilRLPRKSSDAIRKKRVEdVLLRDLALTR-IGGNLVK---GISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517187183 173 TSALDPISTAKIEDLVIELKKKYTIVMVT-HNMQQAV-RISDKTAFFLLGEIV 223
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTiHQPRSDLfRLFDRILLLSSGEIV 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-213 |
5.91e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.56 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTllkSLNRMNDLVKNCRitGEVTLDKEDV-----YRd 75
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGLVKPDS--GRIFLDGEDIthlpmHK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 ldinvlRKKVGM--------VFQKpnpfpMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLnksALGMS 147
Cdd:COG1137 75 ------RARLGIgylpqeasIFRK-----LTVEDNILAVLELRKL-SKKEREERLEELLEEFGI-THLRKSK---AYSLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVT-HNMQQAVRISDK 213
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNVRETLGICDR 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-213 |
6.18e-25 |
|
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: 100.96 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 13 YGDFkALKnINLEIASNEITAFIGPSGCGKSTLLkslNRMNDLVKNCRitGEVTLDKE---DVYRDLDINVLRKKVGMVF 89
Cdd:TIGR02142 9 LGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLI---RLIAGLTRPDE--GEIVLNGRtlfDSRKGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 90 QKPNPFP-MSIYDNIAFG-PRTHGIHNKVQLDEIVErslkQAAIwDEVKDRLNKSalgMSGGQQQRLCIARALAIEPDVL 167
Cdd:TIGR02142 82 QEARLFPhLSVRGNLRYGmKRARPSERRISFERVIE----LLGI-GHLLGRLPGR---LSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517187183 168 LMDEPTSALDPISTAKI----EDLVIELkkKYTIVMVTHNMQQAVRISDK 213
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRLADR 201
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-223 |
8.94e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 8.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTLDKEDVY---RDLD--- 77
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL------------SGELSPDSGEVRlngRPLAdws 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 -------INVLRKKVGMVFqkpnPFPMSiyDNIAFGpRTHGIHNKVQLDEIVERSLKQAAIWDeVKDRlnkSALGMSGGQ 150
Cdd:PRK13548 71 paelarrRAVLPQHSSLSF----PFTVE--EVVAMG-RAPHGLSRAEDDALVAAALAQVDLAH-LAGR---DYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 151 QQRLCIARALA------IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAffLL--G 220
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYADRIV--LLhqG 217
|
...
gi 517187183 221 EIV 223
Cdd:PRK13548 218 RLV 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-223 |
1.70e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYG-----DFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkNCrITGEVTLDKEDVYRDlDI 78
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLL-----------NA-IAGSLPPDSGSILID-GK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NVLRKK-------VGMVFQkpNPF----P-MSIYDNIAF-----GPRTHGI-HNKVQLDEIVERsLKQAAIWDEvkDRLN 140
Cdd:COG1101 69 DVTKLPeykrakyIGRVFQ--DPMmgtaPsMTIEENLALayrrgKRRGLRRgLTKKRRELFREL-LATLGLGLE--NRLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 141 KSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDL---VIElKKKYTIVMVTHNMQQAVRISDKTAFF 217
Cdd:COG1101 144 TKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELtekIVE-ENNLTTLMVTHNMEQALDYGNRLIMM 222
|
....*.
gi 517187183 218 LLGEIV 223
Cdd:COG1101 223 HEGRII 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-237 |
2.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYG---DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndLVKNcriTGEVTLDKEDVYRDld 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAE---SGQIIIDGDLLTEE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 iNV--LRKKVGMVFQKP-NPF-PMSIYDNIAFGPRTHGIhnkvQLDEIVERsLKQAAIWDEVKDRLNKSALGMSGGQQQR 153
Cdd:PRK13650 75 -NVwdIRHKIGMVFQNPdNQFvGATVEDDVAFGLENKGI----PHEEMKER-VNEALELVGMQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQaVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
....*.
gi 517187183 232 FSMPQD 237
Cdd:PRK13650 228 FSRGND 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-242 |
3.38e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 97.08 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYyGDFKALKNINLEIASNEITAFIGPSGCGKS-TLLKSLNRMNDLVKncRITGEVTLDKEDVYrdldINVL 81
Cdd:PRK10418 4 QIELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVR--QTAGRVLLDGKPVA----PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 R-KKVGMVFQKPNPfpmsiydniAFGP----RTHGIHNKVQL----DEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQ 152
Cdd:PRK10418 77 RgRKIATIMQNPRS---------AFNPlhtmHTHARETCLALgkpaDDATLTAALEAVGLENAARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYT--IVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQ 230
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
250
....*....|..
gi 517187183 231 LFSMPQDERTEN 242
Cdd:PRK10418 228 LFNAPKHAVTRS 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-235 |
3.41e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGD-FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLDINVLR 82
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK-----GKVLVSGIDTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNP--FPMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIARAL 160
Cdd:PRK13644 77 KLVGIVFQNPETqfVGRTVEEDLAFGPENLCL-PPIEIRKRVDRALAEIGL-EKYRHRSPKT---LSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQaVRISDKTAFFLLGEIVEYNKTSQLFSMP 235
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-239 |
3.75e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 100.26 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLV--------------------------K 57
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyhvalcekcgyverpskvgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 58 NCRITGEvTLDKEDV-YRDLDINV---LRKKVGMVFQKPnpfpMSIYDNIAFgprthgIHNKVQ-LDEI---VERSLKQA 129
Cdd:TIGR03269 81 PCPVCGG-TLEPEEVdFWNLSDKLrrrIRKRIAIMLQRT----FALYGDDTV------LDNVLEaLEEIgyeGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 130 A-IWDEVK--DRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMV--THNM 204
Cdd:TIGR03269 150 VdLIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 517187183 205 QQAVRISDKTAFFLLGEIVE-------YNKTSQLFSMPQDER 239
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEegtpdevVAVFMEGVSEVEKEC 271
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-236 |
4.94e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.11 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLlkslNRMNDLVKnCRITGEVTLDKEDV--YRDLDINVLRKKVGMVFQkpNP 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTMIE-TPTGGELYYQGQDLlkADPEAQKLLRQKIQIVFQ--NP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FPmsiydniAFGPRthgihNKV--QLDE--IVERSLKQAAIWDEVKDRLNKSALG---------M-SGGQQQRLCIARAL 160
Cdd:PRK11308 102 YG-------SLNPR-----KKVgqILEEplLINTSLSAAERREKALAMMAKVGLRpehydryphMfSGGQRQRIAIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-236 |
6.51e-24 |
|
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: 95.80 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTllkSLNRMNDLVKNcrITGEVTLDKEDVyRDLDINvLRKKV 85
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVRP--DAGKILIDGQDI-THLPMH-ERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 86 GMVF--QKPNPF-PMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:TIGR04406 77 GIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVT-HNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-217 |
1.09e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 99.72 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYY---GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRI------------------ 61
Cdd:PTZ00265 1165 KIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 62 -------------------------------TGEVTLDKEDVYrDLDINVLRKKVGMVFQKPNPFPMSIYDNIAFGPRTH 110
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDIC-DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 111 GIhnkvqldEIVERSLKQAAIWDEVKDRLNK--SALG-----MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAK 183
Cdd:PTZ00265 1324 TR-------EDVKRACKFAAIDEFIESLPNKydTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*.
gi 517187183 184 IEDLVIELKKK--YTIVMVTHNMqQAVRISDKTAFF 217
Cdd:PTZ00265 1397 IEKTIVDIKDKadKTIITIAHRI-ASIKRSDKIVVF 1431
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-213 |
2.86e-23 |
|
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: 94.15 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVY-RDLDINVL- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYM------------IVGLVKPDSGKILlDGQDITKLp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 ---RKKVGMVF--QKPNPF-PMSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIwDEVKDRLnksALGMSGGQQQRLC 155
Cdd:cd03218 69 mhkRARLGIGYlpQEASIFrKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVE 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVT-HNMQQAVRISDK 213
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDR 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-203 |
4.80e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 4.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVyRDLDINVLRK 83
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-----PTSGTLLFEGEDI-STLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFPMSIYDNIAFgprTHGIHNKVQLDEIVERSLKQAAIWDEVkdrLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIF---PWQIRNQQPDPAIFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHN 203
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHD 197
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-213 |
5.67e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLlkslnrMN--------DlvkncriTGEVTLDKEDVyrd 75
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDGKPV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 lDIN----VLRKKVGMVFQKPNPFP-MSIYDNIAFG--PRTHGIHNKVQLDEIVERSLKQ--------AAIWDevkdrln 140
Cdd:COG3845 70 -RIRsprdAIALGIGMVHQHFMLVPnLTVAENIVLGlePTKGGRLDRKAARARIRELSERygldvdpdAKVED------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 141 ksalgMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:COG3845 142 -----LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADR 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-213 |
6.20e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTllkslnrmndlVKNCrITG-------EVTLDKEDVYRDL 76
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTT-----------VFNC-LTGfykptggTILLRGQHIEGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLRKKVGMVFQKPNPF-PMSIYDNIAFGPRTH-------GIHNKVQLDEIVERSLKQAAIWDEV---KDRLNKSALG 145
Cdd:PRK11300 74 GHQIARMGVVRTFQHVRLFrEMTVIENLLVAQHQQlktglfsGLLKTPAFRRAESEALDRAATWLERvglLEHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDK 213
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-236 |
8.19e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 21 NINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDKEDVYrDLDINVLRK----KVGMVFQKP---- 92
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLL-HASEQTLRGvrgnKIAMIFQEPmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 NPFpmsiydniafgprtHGIHNkvQLDEIV--ERSLKQAAIWDEV------------KDRLNKSALGMSGGQQQRLCIAR 158
Cdd:PRK15134 106 NPL--------------HTLEK--QLYEVLslHRGMRREAARGEIlncldrvgirqaAKRLTDYPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVM--VTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQ 236
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLlfITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-213 |
8.40e-23 |
|
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: 96.74 E-value: 8.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlVKNCRIT-GEVTLDKEDVYRdLDINVLRKKVGMVFQKPNPFPM 97
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLL------VGVWPPTaGSVRLDGADLSQ-WDREELGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIA-FGPRThgihnkvqlDEIVERSLKQAAIwDEVKDRLNK--------SALGMSGGQQQRLCIARALAIEPDVLL 168
Cdd:COG4618 421 TIAENIArFGDAD---------PEKVVAAAKLAGV-HEMILRLPDgydtrigeGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517187183 169 MDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMqQAVRISDK 213
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP-SLLAAVDK 535
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-215 |
1.33e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 13 YGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGevtldkedVYRDLDINVLRK---KVGMVF 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKV------------LAG--------VLRPTSGTVRRAggaRVAYVP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 90 QK---PNPFPMSIYDNIAFG-------PRTHGIHNKVqldeIVERSLKQAAIwdevkDRLNKSALG-MSGGQQQRLCIAR 158
Cdd:NF040873 62 QRsevPDSLPLTVRDLVAMGrwarrglWRRLTRDDRA----AVDDALERVGL-----ADLAGRQLGeLSGGQRQRALLAQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMqQAVRISDKTA 215
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDL-ELVRRADPCV 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-202 |
2.22e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKAL-KNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndlvkncrI----TGEVTLDKEDvyrdldi 78
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---------LwpygSGRIARPAGA------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 nvlrkkvGMVF--QKPNpFPM-SIYDNIAFgPRTHGIH---------NKVQLDEIVERsLKQAAIWDEVkdrlnksalgM 146
Cdd:COG4178 427 -------RVLFlpQRPY-LPLgTLREALLY-PATAEAFsdaelrealEAVGLGHLAER-LDEEADWDQV----------L 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTH 202
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-234 |
2.27e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTL---LKSLNRMNDLVKNCRITGEVTLDKEDvyrdldINVLRKKVGMVFQKP--- 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLarlLVGLESPSQGNVSWRGEPLAKLNRAQ------RKAFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 -NPfPMSIYDNIAfGPRTHgihnKVQLDEiVERS------LKQAAIWDEVKDRLNKSalgMSGGQQQRLCIARALAIEPD 165
Cdd:PRK10419 102 vNP-RKTVREIIR-EPLRH----LLSLDK-AERLarasemLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 166 VLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSM 234
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTF 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-233 |
2.30e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 13 YGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV-YRDLDINVLRKKVGMVFQK 91
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK-----GAVLWQGKPLdYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 92 PNP--FPMSIYDNIAFGPRTHGihnkVQLDEIVERSLKQAAIWDEVKDRlNKSALGMSGGQQQRLCIARALAIEPDVLLM 169
Cdd:PRK13638 86 PEQqiFYTDIDSDIAFSLRNLG----VPEAEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 170 DEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-203 |
4.79e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 90.57 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmNDLVKncriTGEVTLDKEDVYRDL------DINVLRKK-VGMVFQ 90
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPD----SGSILVRHDGGWVDLaqasprEILALRRRtIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 91 kpnpFPMSIydniafgPRthgihnkVQLDEIVERSL------KQAAIwDEVKD---RLN-KSAL------GMSGGQQQRL 154
Cdd:COG4778 101 ----FLRVI-------PR-------VSALDVVAEPLlergvdREEAR-ARAREllaRLNlPERLwdlppaTFSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYT-IVMVTHN 203
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHD 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-202 |
6.26e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVYRDLDInvlrkKV 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKI------------LAGELEPDSGEVSIPKGL-----RI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 86 GMVFQKPNPFP-MSIYDNI--AFGPRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNK--------------SALG--- 145
Cdd:COG0488 64 GYLPQEPPLDDdLTVLDTVldGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilSGLGfpe 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 146 ---------MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKkyTIVMVTH 202
Cdd:COG0488 144 edldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-177 |
1.02e-21 |
|
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: 93.73 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncrITGEVTLDKEDVyRDLDINVLRKKVGMVFQKPNPFPMS 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV-----TSGRILIDGQDI-RDVTQASLRAAIGIVPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIAFGpRTHGIHNKV-------QLDEIVErSLKQAaiWD-EVKDRlnksALGMSGGQQQRLCIARALAIEPDVLLMD 170
Cdd:COG5265 448 IAYNIAYG-RPDASEEEVeaaaraaQIHDFIE-SLPDG--YDtRVGER----GLKLSGGEKQRVAIARTLLKNPPILIFD 519
|
....*..
gi 517187183 171 EPTSALD 177
Cdd:COG5265 520 EATSALD 526
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-241 |
1.83e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.96 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKStlLKSLNRMNDLVKNCRITGE-VTLDKEDVYRd 75
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYPGRVMAEkLEFNGQDLQR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDINVLRKKVG----MVFQKP----NPFPMSIYdNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWDEvKDRLNKSALGMS 147
Cdd:PRK11022 78 ISEKERRNLVGaevaMIFQDPmtslNPCYTVGF-QIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|....*.
gi 517187183 226 NKTSQLFSMPQDERTE 241
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQ 251
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-202 |
5.24e-21 |
|
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: 85.58 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVkncRITGEVTLDKedvyrdldinvlRK 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELE---PDEGIVTWGS------------TV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQkpnpfpmsiydniafgprthgihnkvqldeiverslkqaaiwdevkdrlnksalgMSGGQQQRLCIARALAIE 163
Cdd:cd03221 64 KIGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLEN 88
|
170 180 190
....*....|....*....|....*....|....*....
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKkyTIVMVTH 202
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-204 |
6.35e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRI----TGEVTLDKEDVYR--DLDINVLRKKV 85
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLI---------CGIerpsAGKIWFSGHDITRlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 86 GMVFQKPNPF-PMSIYDNIAFGPRTHGihnkVQLDEIVERSlkqAAIWDEVK--DRLNKSALGMSGGQQQRLCIARALAI 162
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLIIAG----ASGDDIRRRV---SAALDKVGllDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTHNM 204
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDI 197
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-232 |
9.36e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.93 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCritGEVTLDKEDVYRdLDINVL 81
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLTE---GEIRLDGRPLSS-LSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPMSIYDNIAFG-----PRTHGIHNKVQLDEIVeRSLKqaaiwDEVKDRLNKSALGMSGGQQQRLCI 156
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGrdiseEQVWQALETVQLAELA-RSLP-----DGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 157 ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-225 |
1.12e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRI----TGEVTLDKEDVYRdLDI 78
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLL---------AGIyppdSGTVTVRGRVSSL-LGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NvlrkkVGMvfqkpNPfPMSIYDNIAFGPRTHGIHNKVQ---LDEIVERSlkqaaiwdEVKDRLNKSALGMSGGQQQRLC 155
Cdd:cd03220 92 G-----GGF-----NP-ELTGRENIYLNGRLLGLSRKEIdekIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY-TIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-240 |
1.44e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvknCRITGEVTLDKEDVYRDLDINVL--RKKVGMVFQKP--- 92
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNRRQLLpvRHRIQVVFQDPnss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 -NPfPMSIYDNIAFGPRTHGIH-NKVQLDEIVERSLKQAAIWDEVKDRLNKSalgMSGGQQQRLCIARALAIEPDVLLMD 170
Cdd:PRK15134 375 lNP-RLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETRHRYPAE---FSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 171 EPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERT 240
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-209 |
1.45e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGD----FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYRdLD 77
Cdd:PRK10584 5 NIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLHQ-MD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 IN---VLR-KKVGMVFQKpnpFpMSIydniafgPRTHGIHNkVQLDEIVE-----RSLKQAAIWDE---VKDRLNKSALG 145
Cdd:PRK10584 79 EEaraKLRaKHVGFVFQS---F-MLI-------PTLNALEN-VELPALLRgessrQSRNGAKALLEqlgLGKRLDHLPAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVR 209
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-239 |
1.54e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTllkSLNRMNDLVKncRITGEVTLDKEDvyrdldINV 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDED------ISL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 L------RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQR 153
Cdd:PRK10895 70 LplharaRRGIGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQS---LSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVT-HNMQQAVRISDKTAFFLLGEIVEYNKTSQLF 232
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
....*..
gi 517187183 233 SMPQDER 239
Cdd:PRK10895 226 QDEHVKR 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-241 |
1.64e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 87.19 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndlvkncRI---TGEVTLDKEDvYRDLDI-- 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAG--------RLapdHGTATYIMRS-GAELELyq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 -------NVLRKKVGMVFQKPNP---FPMSIYDNI-----AFGPRTHGihnkvqldeiverSLKQAAI-W-DEVK---DR 138
Cdd:TIGR02323 75 lseaerrRLMRTEWGFVHQNPRDglrMRVSAGANIgerlmAIGARHYG-------------NIRATAQdWlEEVEidpTR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 139 LNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAF 216
Cdd:TIGR02323 142 IDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLV 221
|
250 260
....*....|....*....|....*
gi 517187183 217 FLLGEIVEYNKTSQLFSMPQDERTE 241
Cdd:TIGR02323 222 MQQGRVVESGLTDQVLDDPQHPYTQ 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-232 |
1.68e-20 |
|
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: 90.46 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTllkSLNRMNDLVKNcrITGEVTLDKEDVYRDLDinVLRKKVGMVFQKPNPFP- 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPP--TSGTVLVGGKDIETNLD--AVRQSLGMCPQHNILFHh 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 MSIYDNIAFGPRTHG-IHNKVQLDeiVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSA 175
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGrSWEEAQLE--MEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 176 LDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIveYNKTSQLF 232
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL--YCSGTPLF 1146
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-213 |
1.73e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.62 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 13 YGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRI----TGEVTLDKEDVYRDLdiNVLRKKVGMV 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL---------SGLlqptSGEVRVAGLVPWKRR--KKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 89 FQKPNP--FPMSIYDNIAFGPRTHGI---HNKVQLDEIVERSlkqaaiwdEVKDRLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:cd03267 100 FGQKTQlwWDLPVIDSFYLLAAIYDLppaRFKKRLDELSELL--------DLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDK 213
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARR 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-232 |
2.27e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvkncrITGE------VTLDKEDVYRD-- 75
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--------ITGDksagshIELLGRTVQREgr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 --LDINVLRKKVGMVFQKPNPFP-MSIYDNIAFGP-------RTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNKsalg 145
Cdd:PRK09984 77 laRDIRKSRANTGYIFQQFNLVNrLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVST---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*....
gi 517187183 224 eYNKTSQLF 232
Cdd:PRK09984 233 -YDGSSQQF 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-222 |
2.61e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrMNDLVKNCriTGEVTLDKEDVyRDLDINVLRK 83
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA---INGTLTPT--AGTVLVAGDDV-EALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPN-PFPMSIYDNIAFGPRTH----GIHNKVQlDEIVERSLKQAAIwDEVKDRlnkSALGMSGGQQQRLCIAR 158
Cdd:PRK09536 78 RVASVPQDTSlSFEFDVRQVVEMGRTPHrsrfDTWTETD-RAAVERAMERTGV-AQFADR---PVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 159 ALAIEPDVLLMDEPTSALD---PIST-AKIEDLVIELKkkyTIVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDinhQVRTlELVRRLVDDGK---TAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-241 |
3.33e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.52 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndlvkncRIT---GEVTLD-KEDVYRDL-DIN- 79
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--------RLApdaGEVHYRmRDGQLRDLyALSe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 -----VLRKKVGMVFQKP-NPFPMSIY--DNI-----AFGPRTHGihnkvqldEIVErslkQAAIW-DEVK---DRLNKS 142
Cdd:PRK11701 81 aerrrLLRTEWGFVHQHPrDGLRMQVSagGNIgerlmAVGARHYG--------DIRA----TAGDWlERVEidaARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 143 ALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIED----LVIELkkKYTIVMVTHNMQQAVRISDKTAFFL 218
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDllrgLVREL--GLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|...
gi 517187183 219 LGEIVEYNKTSQLFSMPQDERTE 241
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYTQ 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
5.38e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDlvKNCRIT-GEVTLDKEDVyRDLDINV-L 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGH--PKYEVTeGEILFKGEDI-TDLPPEErA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPnpfpmsiydniafgPRTHGIHNKVQLDEIVErslkqaaiwdevkdrlnksalGMSGGQQQRLCIARALA 161
Cdd:cd03217 76 RLGIFLAFQYP--------------PEIPGVKNADFLRYVNE---------------------GFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELK-KKYTIVMVTHNMQQAVRISDKTAFFLL-GEIVE 224
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIKPDRVHVLYdGRIVK 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-213 |
6.42e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNdlvknCRITGEVTLDKEDVYRDldINVLRK 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-----SPDAGKITVLGVPVPAR--ARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKvQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIARALAI 162
Cdd:PRK13536 115 RIGVVPQFDNLDLeFTVRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALIN 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 163 EPDVLLMDEPTSALDPISTAKI-EDLVIELKKKYTIVMVTHNMQQAVRISDK 213
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-241 |
1.04e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 6 IKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYRD----LD 77
Cdd:PRK10261 15 VENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-----QAGGLVQCDKMLLRRRsrqvIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKK---------VGMVFQKP----NP-FPMSiyDNIAFGPRTH-GIHNKVQLDEiVERSLKQAAIwDEVKDRLNKS 142
Cdd:PRK10261 90 LSEQSAAqmrhvrgadMAMIFQEPmtslNPvFTVG--EQIAESIRLHqGASREEAMVE-AKRMLDQVRI-PEAQTILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 143 ALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYT--IVMVTHNMQQAVRISDKTAFFLLG 220
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
250 260
....*....|....*....|.
gi 517187183 221 EIVEYNKTSQLFSMPQDERTE 241
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTR 266
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-213 |
1.57e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.63 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndLVKNCRITGEVTLDKEDVYRDldINVLRK 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML-----LGLTHPDAGSISLCGEPVPSR--ARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP-MSIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIARALAI 162
Cdd:PRK13537 81 RVGVVPQFDNLDPdFTVRENLLVFGRYFGL-SAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 163 EPDVLLMDEPTSALDPISTAKI-EDLVIELKKKYTIVMVTHNMQQAVRISDK 213
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMwERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-249 |
4.21e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYRDlDINVLRKKVGMVFQKP---- 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHFG-DYSYRSQRIRMIFQDPstsl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 NP---------FPMSIYDNIAFGPRTHGIHnkvqldeiveRSLKQAAIwdeVKDRLNKSALGMSGGQQQRLCIARALAIE 163
Cdd:PRK15112 101 NPrqrisqildFPLRLNTDLEPEQREKQII----------ETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTE 241
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
....*...
gi 517187183 242 NYITGRFG 249
Cdd:PRK15112 248 RLIAGHFG 255
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-231 |
4.23e-19 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 82.83 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndLVKNcriTGEVTLDKEDVYR-DLdinvlr 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRPT---SGEIIFDGHPWTRkDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPNPFP-MSIYDNIafgpRTHGIHNKVQLDEIVErSLKQAAIWDEVKDRLNKSALGMsggqQQRLCIARALA 161
Cdd:TIGR03740 70 HKIGSLIESPPLYEnLTARENL----KVHTTLLGLPDSRIDE-VLNIVDLTNTGKKKAKQFSLGM----KQRLGIAIALL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIV---EYNKTSQL 231
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGyqgKINKSENL 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-225 |
6.99e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRIT----GEVTLdkedvyrdldinvlRKKV-- 85
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLI---------AGILeptsGRVEV--------------NGRVsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 86 ----GMVFQkPNpfpMSIYDNIAFGPRTHGIHNKV---QLDEIVERSlkqaaiwdEVKDRLN---KSalgMSGGQQQRLC 155
Cdd:COG1134 92 llelGAGFH-PE---LTGRENIYLNGRLLGLSRKEideKFDEIVEFA--------ELGDFIDqpvKT---YSSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY-TIVMVTHNMQQAVRISDKTAffLL--GEIVEY 225
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAI--WLekGRLVMD 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-203 |
7.51e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDlvKNCRIT-GEVTLDKEDVyrdLDINV--- 80
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGH--PKYEVTsGSILLDGEDI---LELSPder 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFP-MSIYDNIafgpRThgIHNKVQLDEI----VERSLKQAAiwDEVKdrLNKSAL------GMSGG 149
Cdd:COG0396 75 ARAGIFLAFQYPVEIPgVSVSNFL----RT--ALNARRGEELsareFLKLLKEKM--KELG--LDEDFLdryvneGFSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDpISTAKIedlVIE-----LKKKYTIVMVTHN 203
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLD-IDALRI---VAEgvnklRSPDRGILIITHY 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-210 |
9.77e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLlkslnrMNDLvkNCritgevtLDK--EDVYR--- 74
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL------MNIL--GC-------LDKptSGTYRvag 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 75 ----DLDINVL----RKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERsLKQAAIWDEVKDRLNKsalg 145
Cdd:PRK10535 70 qdvaTLDADALaqlrREHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQEL-LQRLGLEDRVEYQPSQ---- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQ---QAVRI 210
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQvaaQAERV 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-205 |
1.13e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.61 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 15 DFKALKNINLEIASNEITAFIGPSGCGKSTLL-KSLNRMNdlvkncRITGEV----TLDKEDVYRDLDINVlRKKVGMVF 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVhwsnKNESEPSFEATRSRN-RYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 90 QKPNPFPMSIYDNIAFGPRthgiHNKVQLDEIVERSLKQAAI-----WDEVKdrLNKSALGMSGGQQQRLCIARALAIEP 164
Cdd:cd03290 86 QKPWLLNATVEENITFGSP----FNKQRYKAVTDACSLQPDIdllpfGDQTE--IGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517187183 165 DVLLMDEPTSALD-PISTAKIEDLVIELKK--KYTIVMVTHNMQ 205
Cdd:cd03290 160 NIVFLDDPFSALDiHLSDHLMQEGILKFLQddKRTLVLVTHKLQ 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-202 |
1.34e-18 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 84.32 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRdLDINVLRKKVGMVFQKPNPFPMS 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTS-----GSVRLDGADLKQ-WDRETFGKHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIA-FGprthgihNKVQLDEIVERSlkQAAIWDEVKDRLNK---SALG-----MSGGQQQRLCIARALAIEPDVLLM 169
Cdd:TIGR01842 408 VAENIArFG-------ENADPEKIIEAA--KLAGVHELILRLPDgydTVIGpggatLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190
....*....|....*....|....*....|....
gi 517187183 170 DEPTSALDPISTAKIEDLVIELKK-KYTIVMVTH 202
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-212 |
1.86e-18 |
|
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: 80.17 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYygdfKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLDINVLRKK 84
Cdd:cd03215 6 EVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS-----GEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVfqkpnP--------FP-MSIYDNIAFGprthgihnkVQLdeiverslkqaaiwdevkdrlnksalgmSGGQQQRLC 155
Cdd:cd03215 77 IAYV-----PedrkreglVLdLSVAENIALS---------SLL----------------------------SGGNQQKVV 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISD 212
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCD 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-199 |
1.86e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.31 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYG---DFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLD 77
Cdd:PTZ00265 380 IKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE-----GDIIINDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKKVGMVFQKPNPFPMSIYDNIAF------------------GPRTHGIHNK------------------------ 115
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedGNDSQENKNKrnscrakcagdlndmsnttdsnel 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 116 ---------VQLDEIVERSLK------QAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPIS 180
Cdd:PTZ00265 535 iemrknyqtIKDSEVVDVSKKvlihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260
....*....|....*....|..
gi 517187183 181 TAKIEDLVIELK---KKYTIVM 199
Cdd:PTZ00265 615 EYLVQKTINNLKgneNRITIII 636
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
2.00e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 83.85 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmndlvkncritGEVTLDKEDVYRDLDINV 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQDLIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRkkvgmvFQK--PNPFPMSIYDNIAFG--------PRTHGIHNKVQLDEiVERSLKQAAIWDEVKDRLN--------KS 142
Cdd:PRK11147 69 AR------LQQdpPRNVEGTVYDFVAEGieeqaeylKRYHDISHLVETDP-SEKNLNELAKLQEQLDHHNlwqlenriNE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 143 ALG------------MSGGQQQRLCIARALAIEPDVLLMDEPTSALDpISTakIEDLVIELKK-KYTIVMVTH------N 203
Cdd:PRK11147 142 VLAqlgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirN 218
|
....*....
gi 517187183 204 MqqAVRISD 212
Cdd:PRK11147 219 M--ATRIVD 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-225 |
3.56e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVyrDLDINVlrk 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL------------LAGELEPDSGTV--KLGETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFP--MSIYDNIA-FGPrthgihnkvQLDEIVERSL------KQAAIWDEVKDrlnksalgMSGGQQQRL 154
Cdd:COG0488 379 KIGYFDQHQEELDpdKTVLDELRdGAP---------GGTEQEVRGYlgrflfSGDDAFKPVGV--------LSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIElkkkY--TIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD----FpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
6.60e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.54 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYY-----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDL-D 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTS-----GEVNVRVGDEWVDMtK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVL-----RKKVGMVFQKPNPFP-MSIYDNIafgprTHGIhnKVQL-DEIVER----SLKQAAIWDE-VKDRLNKSALG 145
Cdd:TIGR03269 355 PGPDgrgraKRYIGILHQEYDLYPhRTVLDNL-----TEAI--GLELpDELARMkaviTLKMVGFDEEkAEEILDKYPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|
gi 517187183 224 EYNKTSQLFS 233
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-211 |
2.57e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVtldkedVYRDLDINVL---------RKKVGMVF 89
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT-----PTSGDV------IFNGQPMSKLssaakaelrNQKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 90 QKPNPFP-MSIYDNIAFgPRTHGihnKVQLDEIVERSLKQ-AAIWDEVKDRLNKSALgmSGGQQQRLCIARALAIEPDVL 167
Cdd:PRK11629 94 QFHHLLPdFTALENVAM-PLLIG---KKKPAEINSRALEMlAAVGLEHRANHRPSEL--SGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517187183 168 LMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQQAVRIS 211
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-223 |
3.15e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLV-----KNCRITGEVTLDKEDVYRdLDINVLRKKVGMVFQKPN 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTgggapRGARVTGDVTLNGEPLAA-IDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 94 P-FPMSIYDNIAFGPRTHG-------IHNKvqldEIVERSLKQAAIwdEVKDRLNKSALgmSGGQQQRLCIARALA---- 161
Cdd:PRK13547 94 PaFAFSAREIVLLGRYPHArragaltHRDG----EIAWQALALAGA--TALVGRDVTTL--SGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 162 -----IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTI--VMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-213 |
1.52e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.42 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLlksLNRMNDLVkncRITGEVTLDKEDVyRDLDINVLRKKVGMVFQK-PNPFPM 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLL---PGQGEILLNGRPL-SDWSAAELARHRAYLSQQqSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFGPRTHGIHNKVQ--LDEIVERsLKqaaiwdeVKDRLNKSALGMSGGQQQRLCIARAL-----AIEPD--VLL 168
Cdd:COG4138 85 PVFQYLALHQPAGASSEAVEqlLAQLAEA-LG-------LEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517187183 169 MDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADR 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-213 |
1.64e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 21 NINLEIASNEITAFIGPSGCGKSTLLkslNRMNDLVKNCRitGEVTLDKE---DVYRDLDINVLRKKVGMVFQKPNPFP- 96
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLI---NAISGLTRPQK--GRIVLNGRvlfDAEKGICLPPEKRRIGYVFQDARLFPh 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 MSIYDNIAFGPRTHgihNKVQLDEIVE----RSLkqaaiwdevkdrLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:PRK11144 91 YKVRGNLRYGMAKS---MVAQFDKIVAllgiEPL------------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 173 TSALD--------PIstakIEDLVIELkkKYTIVMVTHNMQQAVRISDK 213
Cdd:PRK11144 156 LASLDlprkrellPY----LERLAREI--NIPILYVSHSLDEILRLADR 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-211 |
5.24e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriT-------GEVTLDKEDV-YRD 75
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKML------------TgllpaseGEAWLFGQPVdAGD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 LDInvlRKKVGMVFQKpnpFpmSIY------DNIA-----FGPRTHGIHNKVqlDEIVER-SLKQAAiwDEVKDRLnksA 143
Cdd:NF033858 335 IAT---RRRVGYMSQA---F--SLYgeltvrQNLElharlFHLPAAEIAARV--AEMLERfDLADVA--DALPDSL---P 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 144 LGMsggqQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL--KKKYTIVMVTHNMQQAV---RIS 211
Cdd:NF033858 400 LGI----RQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAErcdRIS 468
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-213 |
6.15e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDvYRDLDINVLRK 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK-----GTITINNIN-YNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 -KVGMVFQKPNPF-PMSIYDNIAFG----PRTHGIhNKVQLDEIVERSlkqAAIWDEV--KDRLNKSALGMSGGQQQRLC 155
Cdd:PRK09700 80 lGIGIIYQELSVIdELTVLENLYIGrhltKKVCGV-NIIDWREMRVRA---AMMLLRVglKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYT-IVMVTHNMQQAVRISDK 213
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDR 214
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-244 |
7.20e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYY----GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvKNCRITGevtldkeDVYRDL 76
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--DNWRVTA-------DRMRFD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVL-------RKKVG----MVFQKP----NP-----------FPMSIYDniafGPRTHGIH-NKVQLDEIVERslkqA 129
Cdd:PRK15093 72 DIDLLrlsprerRKLVGhnvsMIFQEPqsclDPservgrqlmqnIPGWTYK----GRWWQRFGwRKRRAIELLHR----V 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 130 AIWDEvKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQA 207
Cdd:PRK15093 144 GIKDH-KDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQML 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 517187183 208 VRISDKTAFFLLGEIVEYNKTSQLFSMPQDERTENYI 244
Cdd:PRK15093 223 SQWADKINVLYCGQTVETAPSKELVTTPHHPYTQALI 259
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-202 |
1.18e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 16 FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRmndLVKNCRITGEVTLDKEDVYRDLdinvlrkkvgmvfqkpnpf 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGREA------------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 pmSIYDNIafgPRTHGIHNKVQLDEIVerSLKQAAIWDEVKDRLnksalgmSGGQQQRLCIARALAIEPDVLLMDEPTSA 175
Cdd:COG2401 101 --SLIDAI---GRKGDFKDAVELLNAV--GLSDAVLWLRRFKEL-------STGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|..
gi 517187183 176 LDPiSTAKI-----EDLVIELKKkyTIVMVTH 202
Cdd:COG2401 167 LDR-QTAKRvarnlQKLARRAGI--TLVVATH 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-177 |
1.80e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYrDLDINVLRKKVGMVFQKPNPFPM 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE-----GDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFG-PrthgihNKVQldEIVERSLKQAAIWD-----------EVKDRlnksALGMSGGQQQRLCIARALAIEPD 165
Cdd:PRK10789 404 TVANNIALGrP------DATQ--QEIEHVARLASVHDdilrlpqgydtEVGER----GVMLSGGQKQRISIARALLLNAE 471
|
170
....*....|..
gi 517187183 166 VLLMDEPTSALD 177
Cdd:PRK10789 472 ILILDDALSAVD 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-233 |
1.80e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRdLDINVLRKKVGMVFQKPNPFPMS 98
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK-----GRIMIDDCDVAK-FGLTDLRRVLSIIPQSPVLFSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIafGPRTHgiHNKVQLDEIVERSlkqaaiwdEVKDRLNKSALGM-----------SGGQQQRLCIARALAIEPDVL 167
Cdd:PLN03232 1326 VRFNI--DPFSE--HNDADLWEALERA--------HIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517187183 168 LMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-213 |
4.12e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRI------TGEVTLDKEDVYRDLD 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL---------SGVyphgtwDGEIYWSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKKVGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERS---LKQAAIwDEVKDRLNKSALGmsGGQQQR 153
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPeLSVAENIFLGNEITLPGGRMAYNAMYLRAknlLRELQL-DADNVTRPVGDYG--GGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCDT 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-212 |
4.93e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLdlyyGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSL---NRmndlvkncRITGEVTLDKEDV----YRDld 77
Cdd:COG1129 258 EVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgaDP--------ADSGEIRLDGKPVrirsPRD-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 inVLRKKVGMV---------FQkpnpfPMSIYDNIAFGP----RTHGIHNKVQLDEIVERSLKQAAIwdevK-DRLNKSA 143
Cdd:COG1129 324 --AIRAGIAYVpedrkgeglVL-----DLSIRENITLASldrlSRGGLLDRRRERALAEEYIKRLRI----KtPSPEQPV 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 144 LGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDpIStAK--IEDLVIELKKK-YTIVMVTHNMQQAVRISD 212
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VG-AKaeIYRLIRELAAEgKAVIVISSELPELLGLSD 462
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-202 |
7.13e-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: 69.88 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKAL-KNINLEIASNEITAFIGPSGCGKSTLLKSLNrmndlvkncritGEVTLDKEDVYRDLDINVLr 82
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALA------------GLWPWGSGRIGMPEGEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 kkvgMVFQKPnpfpmsiYdnIAFGprthgihnkvqldeiverSLKQAAI--WDEVkdrlnksalgMSGGQQQRLCIARAL 160
Cdd:cd03223 68 ----FLPQRP-------Y--LPLG------------------TLREQLIypWDDV----------LSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517187183 161 AIEPDVLLMDEPTSALDPISTAKIEDLVieLKKKYTIVMVTH 202
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLL--KELGITVISVGH 146
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-235 |
8.07e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNL----DLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCRITGevtldkeDVYRDL 76
Cdd:COG4170 1 MPLLDIRNLtieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTA-------DRFRWN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVLR-----------KKVGMVFQKPNPF--PMS-----IYDNIAFGP-RTHGIHNKVQLDEIVERSLKQAAIWDEvKD 137
Cdd:COG4170 72 GIDLLKlsprerrkiigREIAMIFQEPSSCldPSAkigdqLIEAIPSWTfKGKWWQRFKWRKKRAIELLHRVGIKDH-KD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 138 RLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKK--KYTIVMVTHNMQQAVRISDKTA 215
Cdd:COG4170 151 IMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTIT 230
|
250 260
....*....|....*....|
gi 517187183 216 FFLLGEIVEYNKTSQLFSMP 235
Cdd:COG4170 231 VLYCGQTVESGPTEQILKSP 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-205 |
9.03e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriT-------GEVTLDKEDVYRDLdiNVLRKKVGMVF 89
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML------------TgilvptsGEVRVLGYVPFKRR--KEFARRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 90 -QK-------PnpfPM-------SIYDnIafgPRTHGIHNkvqLDEIVERsLkqaaiwdEVKDRLNKSALGMSGGQQQRL 154
Cdd:COG4586 102 gQRsqlwwdlP---AIdsfrllkAIYR-I---PDAEYKKR---LDELVEL-L-------DLGELLDTPVRQLSLGQRMRC 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKY--TIVMVTHNMQ 205
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-237 |
1.95e-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: 72.67 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYG---DFkALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDIN 79
Cdd:TIGR00957 1284 RVEFRNYCLRYRedlDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAE-----GEIIIDGLNI-AKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMVFQKPNPFPMSIYDNI-AFGPRThgihnkvqlDEIVERSLKQAAIWDEVK---DRLN----KSALGMSGGQQ 151
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLdPFSQYS---------DEEVWWALELAHLKTFVSalpDKLDhecaEGGENLSVGQR 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQavrISDKTAFFLL--GEIVEYNKTS 229
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTRVIVLdkGEVAEFGAPS 1504
|
250
....*....|....*
gi 517187183 230 QL-------FSMPQD 237
Cdd:TIGR00957 1505 NLlqqrgifYSMAKD 1519
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-213 |
2.01e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvknCRI------TGEVTLDKEDVY---- 73
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL---------SGVyphgtyEGEIIFEGEELQasni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 RDLDinvlRKKVGMVFQK----PNpfpMSIYDNIAFG--PRTHGIHNKVQLDEIVERSLKQAAIwdEVKDRLNKSALGms 147
Cdd:PRK13549 77 RDTE----RAGIAIIHQElalvKE---LSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKL--DINPATPVGNLG-- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 148 GGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISDT 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-239 |
2.92e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLDINVlrkkVGMVFQKPN---P 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLAS-----GKISILGQPTRQALQKNL----VAYVPQSEEvdwS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FPMSIYDNIAFGPRTH-GI--HNKVQLDEIVERSLKQAAIWDEVKDRLNKsalgMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:PRK15056 93 FPVLVEDVVMMGRYGHmGWlrRAKKRDRQIVTAALARVDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 172 PTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAfFLLGEIVEYNKTSQLFSMPQDER 239
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLEL 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-203 |
3.77e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDvYRDLD---- 77
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA-----GTIKLDGGD-IDDPDvaea 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 INVLRKKVGMvfqKPNpfpMSIYDNIAFGPRTHGihnkvQLDEIVERSLkqAAIwdEVKDRLNKSALGMSGGQQQRLCIA 157
Cdd:PRK13539 75 CHYLGHRNAM---KPA---LTVAENLEFWAAFLG-----GEELDIAAAL--EAV--GLAPLAHLPFGYLSAGQKRRVALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517187183 158 RALAIEPDVLLMDEPTSALDPISTAKIEDLVIE-LKKKYTIVMVTHN 203
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-233 |
7.89e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVyRDLDINVLRKKVGMVFQKPNPFPMS 98
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER-----GRILIDGCDI-SKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNI-AFGPrthgiHNKVQLDEIVERSlkqaaiwdEVKDRLNKSALGM-----------SGGQQQRLCIARALAIEPDV 166
Cdd:PLN03130 1329 VRFNLdPFNE-----HNDADLWESLERA--------HLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 167 LLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRiSDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-224 |
3.14e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLD-KEDVYRDLdINVLRKKVGMVFQKPNPF 95
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDgQEMRFAST-TAALAAGVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 P-MSIYDNIAFG--PRTHGIHNKVQLDEIVERSLKqaaiwdEVKDRLNKSA-LG-MSGGQQQRLCIARALAIEPDVLLMD 170
Cdd:PRK11288 92 PeMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLE------HLGVDIDPDTpLKyLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 171 EPTSALdpiSTAKIEDL--VI-ELKKKYTIVM-VTHNMQQAVRISDKTAFFLLGEIVE 224
Cdd:PRK11288 166 EPTSSL---SAREIEQLfrVIrELRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-244 |
3.51e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLYygDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYRDLDINVLRKK 84
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVFQ--KPNPF--PMSIYDNIAFGPR--------THGIHNKVQLDEIVERSLKQAAIwdeVKDRLNKSALGMSGGQQQ 152
Cdd:PRK09700 340 MAYITEsrRDNGFfpNFSIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENQRELLAL---KCHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIveynktSQL 231
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL------TQI 490
|
250
....*....|...
gi 517187183 232 FSmPQDERTENYI 244
Cdd:PRK09700 491 LT-NRDDMSEEEI 502
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-204 |
3.90e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndLVKNCRITGEVTLdkedvyrdldin 79
Cdd:TIGR00957 635 NSITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVHM------------ 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 vlRKKVGMVFQKPNPFPMSIYDNIAFGPrthgihnkvQLDEIVERSLKQA-AIWDEVK-----DR--LNKSALGMSGGQQ 151
Cdd:TIGR00957 698 --KGSVAYVPQQAWIQNDSLRENILFGK---------ALNEKYYQQVLEAcALLPDLEilpsgDRteIGEKGVNLSGGQK 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIE----LKKKyTIVMVTHNM 204
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvLKNK-TRILVTHGI 822
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-212 |
4.93e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTLDK-EDVYRDLDINVLR 82
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVL------------TGIYTRDAgSILYLGKEVTFNG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KK------VGMVFQKPNPFP-MSIYDNIAFGPRTHGIHNKVQLDEIVERSlkqaaiwDEVKDRLN-----KSALG-MSGG 149
Cdd:PRK10762 73 PKssqeagIGIIHQELNLIPqLTIAENIFLGREFVNRFGRIDWKKMYAEA-------DKLLARLNlrfssDKLVGeLSIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELK-KKYTIVMVTHNMQQAVRISD 212
Cdd:PRK10762 146 EQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICD 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-184 |
6.20e-13 |
|
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: 65.34 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSL-NRMNDLVkncrITGEVTLDKedvyRDLDINvLRKKVGMVFQKPnpfpm 97
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGV----ITGEILING----RPLDKN-FQRSTGYVEQQD----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 siydniafgprthgIHNKVQldeiverslkqaaiwdEVKDRLNKSAL--GMSGGQQQRLCIARALAIEPDVLLMDEPTSA 175
Cdd:cd03232 89 --------------VHSPNL----------------TVREALRFSALlrGLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
....*....
gi 517187183 176 LDPISTAKI 184
Cdd:cd03232 139 LDSQAAYNI 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-194 |
6.48e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDV-------YRDLDINVL---RKKVGM 87
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS-----GSIRLDGEDItglspreRRRLGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 88 VfqkPNpfpMSIYDNIAFG-PRTHGIHNKVQLD---------EIVER-SLKQAAIWDEVKdrlnksalGMSGGQQQRLCI 156
Cdd:COG3845 348 V---PD---MSVAENLILGrYRRPPFSRGGFLDrkairafaeELIEEfDVRTPGPDTPAR--------SLSGGNQQKVIL 413
|
170 180 190
....*....|....*....|....*....|....*...
gi 517187183 157 ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK 194
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA 451
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-233 |
9.41e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 66.09 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDF--KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRdLDINV 80
Cdd:cd03288 19 EIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD-----GKIVIDGIDISK-LPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIafGPRTHGIHNKV-QLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARA 159
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNL--DPECKCTDDRLwEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 160 LAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMqQAVRISDKTAFFLLGEIVEYNKTSQLFS 233
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRV-STILDADLVLVLSRGILVECDTPENLLA 243
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-210 |
4.42e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEV-TLDKEDVyrdldinVLRKKVGMVFQKPNPFPM 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISA------------MLGELpPRSDASV-------VIRGTVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFG-PRTHGIHNKVQLDEIVERSLKQAAIWD--EVKDRlnksALGMSGGQQQRLCIARALAIEPDVLLMDEPTS 174
Cdd:PLN03130 694 TVRDNILFGsPFDPERYERAIDVTALQHDLDLLPGGDltEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517187183 175 ALDPISTAKIEDLVI--ELKKKyTIVMVT---HNMQQAVRI 210
Cdd:PLN03130 770 ALDAHVGRQVFDKCIkdELRGK-TRVLVTnqlHFLSQVDRI 809
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-201 |
4.74e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCRITGEVTLDKEDVYRDLdinvLRKKVGMVFQKPNPFPM- 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPIDAKE----MRAISAYVQQDDLFIPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFGPRthgihnkVQLDEIVERSLKQAAIwDEVKDRLN--KSA----------LGMSGGQQQRLCIARALAIEPD 165
Cdd:TIGR00955 115 TVREHLMFQAH-------LRMPRRVTKKEKRERV-DEVLQALGlrKCAntrigvpgrvKGLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 517187183 166 VLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVT 201
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-188 |
4.75e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKslnrmndLVKNCRI--TGEVT-LDKedvyrDLDINV 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS-------LIAGARKiqQGRVEvLGG-----DMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVG-----MvfqkP-----NPFP-MSIYDNIAFGPRTHGiHNKVQLDEIVERsLKQAAIWDEVKDRLnksALGMSGG 149
Cdd:NF033858 70 HRRAVCpriayM----PqglgkNLYPtLSVFENLDFFGRLFG-QDAAERRRRIDE-LLRATGLAPFADRP---AGKLSGG 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 517187183 150 QQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLV 188
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELI 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-213 |
4.92e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKaLKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTLDKEDVYRDLDIN---- 79
Cdd:PRK13409 341 VEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLL------------AGVLKPDEGEVDPELKISykpq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 -VLRKKVGMVFQkpnpFPMSIYDNIAFGPRTHGIHNKVQLDEIVERSLKqaaiwdevkdrlnksalGMSGGQQQRLCIAR 158
Cdd:PRK13409 408 yIKPDYDGTVED----LLRSITDDLGSSYYKSEIIKPLQLERLLDKNVK-----------------DLSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 159 ALAIEPDVLLMDEPTSALD---PISTAKIEDLVIELKKKYTIVmVTHNMQQAVRISDK 213
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDveqRLAVAKAIRRIAEEREATALV-VDHDIYMIDYISDR 523
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-231 |
5.27e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDvyrdLDIN---- 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKI------------IAGIVPPDSGT----LEIGgnpc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 -----VLRKKVG--MVFQKPNPFP-MSIYDNIAFG-PRTHGIHNKVQ--LDEI-VERSLKQAAIWDEVKDrlnksalgms 147
Cdd:PRK15439 76 arltpAKAHQLGiyLVPQEPLLFPnLSVKENILFGlPKRQASMQKMKqlLAALgCQLDLDSSAGSLEVAD---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 148 ggqQQRLCIARALAIEPDVLLMDEPTSALDPIST----AKIEDLvieLKKKYTIVMVTHNMQQAVRISDKTAFFLLGEIV 223
Cdd:PRK15439 146 ---RQIVEILRGLMRDSRILILDEPTASLTPAETerlfSRIREL---LAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
....*...
gi 517187183 224 EYNKTSQL 231
Cdd:PRK15439 220 LSGKTADL 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-241 |
5.36e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.11 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVYRDldinvlrKKVGMVFQKPNPFPMS 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLML------------ILGELEPSEGKIKHS-------GRISFSSQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIAFGprthgihnkVQLDEIVERSLKQAAIWDE------VKDR--LNKSALGMSGGQQQRLCIARALAIEPDVLLMD 170
Cdd:cd03291 114 IKENIIFG---------VSYDEYRYKSVVKACQLEEditkfpEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 171 EPTSALDPISTAKI-EDLVIELKKKYTIVMVTHNMQQaVRISDKTAFFLLGEIVEYNKTSQLfsmpQDERTE 241
Cdd:cd03291 185 SPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSEL----QSLRPD 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-205 |
6.65e-12 |
|
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: 63.72 E-value: 6.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvknCRITGEVTLDKEDvYRDLDINV 80
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS-WNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIafgpRTHGIHNKVQLDEIVER-SLKqaAIWDEVKDRLNKSALG----MSGGQQQRLC 155
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNL----DPYGKWSDEEIWKVAEEvGLK--SVIEQFPGQLDFVLVDggcvLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517187183 156 IARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQ 205
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-202 |
7.02e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCrITGEVTLDKedvyRDLDINVLrKKVGMVFQKPNPFP-M 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNAL--AGRIQGNN-FTGTILANN----RKPTKQIL-KRTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFG-----PRTHGIHNKVQLDEIVERSLKQAAIWDEVKDrlNKSALGMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:PLN03211 156 TVRETLVFCsllrlPKSLTKQEKILVAESVISELGLTKCENTIIG--NSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|.
gi 517187183 173 TSALDPISTAKIEDLVIELKKK-YTIVMVTH 202
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKgKTIVTSMH 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-213 |
7.07e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 22 INLEIASNEITAFIGPSGCGKSTLLKSL---NRmndlvkncRITGEVTLDKEDVyrdlDIN----------VL----RKK 84
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTR--------RTAGQVYLDGKPI----DIRsprdairagiMLcpedRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 85 VGMVfqkpnpfPM-SIYDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIWD-EVKDRLNKSALG-MSGGQQQRLCIARALA 161
Cdd:PRK11288 340 EGII-------PVhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSlNIKTPSREQLIMnLSGGNQQKAILGRWLS 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDK 213
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADR 465
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-231 |
9.68e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyRDLDINVLRKKVGMVFQK-PNPFPM 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPL-ESWSSKAFARKVAYLPQQlPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFGPRT-HG------IHNKVQLDE-IVERSLKQAAiwdevkDRLNKSalgMSGGQQQRLCIARALAIEPDVLLM 169
Cdd:PRK10575 101 TVRELVAIGRYPwHGalgrfgAADREKVEEaISLVGLKPLA------HRLVDS---LSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517187183 170 DEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQL 231
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-181 |
1.08e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 16 FKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmNDLVKNCRITGEVTLDKEDVyrdldinvlrKKVGMVFQKPnpf 95
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIPY----------KEFAEKYPGE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 pmSIYDNiafgprTHGIHNKVQLdeiVERSLKQAAiwdevKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSA 175
Cdd:cd03233 85 --IIYVS------EEDVHFPTLT---VRETLDFAL-----RCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
....*.
gi 517187183 176 LDPIST 181
Cdd:cd03233 149 LDSSTA 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-239 |
1.47e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKN---CRITGEVTLDKedvyrdldinvlrkkvgmvfQKPNPF 95
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPSegkIKHSGRISFSP--------------------QTSWIM 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 PMSIYDNIAFGprthgihnkVQLDEIVERSLKQAAIWDE------VKDR--LNKSALGMSGGQQQRLCIARALAIEPDVL 167
Cdd:TIGR01271 500 PGTIKDNIIFG---------LSYDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 168 LMDEPTSALDPISTAKI-EDLVIELKKKYTIVMVTHNMQQAVRiSDKtaFFLLGEIVEYNKTSqlFSMPQDER 239
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADK--ILLLHEGVCYFYGT--FSELQAKR 638
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-204 |
2.84e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrmndlvkncrITGEVTLDKEDVYRDLDInv 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRV------------VLGLVAPDEGVIKRNGKL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 lrkKVGMVFQKpnpfpmsiydniafgprthgIHNKVQLDEIVERSL------KQAAIWDEVKdRLNKSAL------GMSG 148
Cdd:PRK09544 68 ---RIGYVPQK--------------------LYLDTTLPLTVNRFLrlrpgtKKEDILPALK-RVQAGHLidapmqKLSG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 149 GQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK--YTIVMVTHNM 204
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDL 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-213 |
3.61e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvKNcriTGEVTLDKEDVYRDLDINVLRKKVGMVFQKPNPF- 95
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ--KD---SGSILFQGKEIDFKSSKEALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 PMSIYDNIAFG--PrTHGI---HNKVQLDEIverslkqaAIWDE----VKDRLNKSALGMSggQQQRLCIARALAIEPDV 166
Cdd:PRK10982 87 QRSVMDNMWLGryP-TKGMfvdQDKMYRDTK--------AIFDEldidIDPRAKVATLSVS--QMQMIEIAKAFSYNAKI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517187183 167 LLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDE 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-214 |
1.03e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmnDLVKNCRITGEVTLDKEdVYRDLDINvLRKKVGMVF--QKPNP 94
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLS---GVYPHGSYEGEILFDGE-VCRFKDIR-DSEALGIVIihQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FP-MSIYDNIAFG--PRTHGIHNkvqldeiverslkqaaiWDEVKDR----LNK-----------SALGMsgGQQQRLCI 156
Cdd:NF040905 90 IPyLSIAENIFLGneRAKRGVID-----------------WNETNRRarelLAKvgldespdtlvTDIGV--GKQQLVEI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 157 ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKT 214
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSI 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-217 |
1.05e-10 |
|
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: 60.11 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 12 YYGDFKaLKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTLDKEDVYRDLDinvlrkKVGMVFQK 91
Cdd:cd03237 9 TLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEGDIEIELD------TVSYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 92 PNP-FPMSIYDNIAFGPRTHGIH--------NKVQLDEIVERslkqaaiwdEVKDrlnksalgMSGGQQQRLCIARALAI 162
Cdd:cd03237 70 IKAdYEGTVRDLLSSITKDFYTHpyfkteiaKPLQIEQILDR---------EVPE--------LSGGELQRVAIAACLSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 163 EPDVLLMDEPTSALDP---ISTAKIEDLVIELKKKyTIVMVTHNMQQAVRISDKTAFF 217
Cdd:cd03237 133 DADIYLLDEPSAYLDVeqrLMASKVIRRFAENNEK-TAFVVEHDIIMIDYLADRLIVF 189
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-202 |
1.10e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNcriTGEVTLDK--------EDVY 73
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKWSEnanigyyaQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 RDLDINvlrkkvgmvfqkpnpfpMSIYDNIAfGPRTHGiHNKVQLDEIVERSLKQAaiwdevkDRLNKSALGMSGGQQQR 153
Cdd:PRK15064 393 YDFEND-----------------LTLFDWMS-QWRQEG-DDEQAVRGTLGRLLFSQ-------DDIKKSVKVLSGGEKGR 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517187183 154 LCIARALAIEPDVLLMDEPTSALDPIStakIEDLVIELKK-KYTIVMVTH 202
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKyEGTLIFVSH 493
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-232 |
1.28e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTldkedvYRDLDINVLRKKVGMVFQKPNPFPMS 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM------------LGELS------HAETSSVVIRGSVAYVPQVSWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIAFGPRTHgihnkvqlDEIVERSLKQAAIWDEV-----KDR--LNKSALGMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:PLN03232 695 VRENILFGSDFE--------SERYWRAIDVTALQHDLdllpgRDLteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 172 PTSALDPISTAKIEDLVI--ELKKKyTIVMVThNMQQAVRISDKTAFFLLGEI------VEYNKTSQLF 232
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMkdELKGK-TRVLVT-NQLHFLPLMDRIILVSEGMIkeegtfAELSKSGSLF 833
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-213 |
1.40e-10 |
|
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: 60.57 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 13 YGDFKalkninLEIAS-----NEITAFIGPSGCGKSTLLKSLnrmndlvkncriTGEVTLDKEDVYRDLDIN-------- 79
Cdd:COG1245 351 YGGFS------LEVEGgeireGEVLGIVGPNGIGKTTFAKIL------------AGVLKPDEGEVDEDLKISykpqyisp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 --------VLRKKVGmvfqkpNPFPMSIYdniafgprTHGIHNKVQLDEIVERSLKqaaiwdevkdrlnksalGMSGGQQ 151
Cdd:COG1245 413 dydgtveeFLRSANT------DDFGSSYY--------KTEIIKPLGLEKLLDKNVK-----------------DLSGGEL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALD---PISTAKIEDLVIELKKKYTIVmVTHNMQQAVRISDK 213
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRRFAENRGKTAMV-VDHDIYLIDYISDR 525
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-202 |
2.06e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.52 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLD-----I 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS-----GEVRWNGTPLAEQRDephenI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 79 NVLRKKVGMvfqKPNpfpMSIYDNIAFGPRTHGIHnkvqlDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIAR 158
Cdd:TIGR01189 76 LYLGHLPGL---KPE---LSALENLHFWAAIHGGA-----QRTIEDALAAVGL----TGFEDLPAAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIE-LKKKYTIVMVTH 202
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-202 |
2.36e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLvkncRIT-GEVTLDKEDVYRDLDINVLR 82
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY----EVTgGTVEFKGKDLLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKP-------NPFPMSIYDNIAFGPRTHGIHNKVQLDEIVErslKQAAIWDEVKDRLNKSA-LGMSGGQQQRL 154
Cdd:PRK09580 78 EGIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLME---EKIALLKMPEDLLTRSVnVGFSGGEKKRN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKK-KYTIVMVTH 202
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTH 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-213 |
3.70e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 22 INLEIASNEITAFIGPSGCGKSTLLKslnRMNDLVKNcriTGEVTLDKEDVyRDLDINVL-RKKVGMVFQKPNPFPMSIY 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLA---RMAGLLPG---SGSIQFAGQPL-EAWSAAELaRHRAYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 101 DNIAF--GPRTHGIHNKVQLDEIVERsLKqaaiwdeVKDRLNKSALGMSGGQQQRLCIARA-LAIEPDV------LLMDE 171
Cdd:PRK03695 88 QYLTLhqPDKTRTEAVASALNEVAEA-LG-------LDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517187183 172 PTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDK 213
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADR 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-213 |
4.25e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNCritGEVTLDKEDVYRD-----LD-----INVLRKKVGMV 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVL--YGALPRTS---GYVTLDGHEVVTRspqdgLAngivyISEDRKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 89 FQkpnpfpMSIYDNIAFGPRTHGIHNKVQLDEIVErslkQAAIWD-----EVKDRLNKSALG-MSGGQQQRLCIARALAI 162
Cdd:PRK10762 343 LG------MSVKENMSLTALRYFSRAGGSLKHADE----QQAVSDfirlfNIKTPSMEQAIGlLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517187183 163 EPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDR 464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-202 |
1.01e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYrdldinvlrkkvgmVFQKPNPFPMS 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISE-----GRVWAERSIAY--------------VPQQAWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 99 IYDNIAF--GPRTHGIHNKVQLDEIvERSLKQAAIWDEVKdrLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSAL 176
Cdd:PTZ00243 737 VRGNILFfdEEDAARLADAVRVSQL-EADLAQLGGGLETE--IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190
....*....|....*....|....*....|..
gi 517187183 177 DpistAKIEDLVIE------LKKKyTIVMVTH 202
Cdd:PTZ00243 814 D----AHVGERVVEecflgaLAGK-TRVLATH 840
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-230 |
1.09e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 135 VKDRLNKSALG-MSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISD 212
Cdd:PRK10982 380 VKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITD 459
|
90 100
....*....|....*....|.
gi 517187183 213 KTAFF---LLGEIVEYNKTSQ 230
Cdd:PRK10982 460 RILVMsngLVAGIVDTKTTTQ 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-202 |
2.62e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 35 IGPSGCGKSTLLK--SLNRMNDLVKNCRI---TGEVTLDKEDVYR---DLDIN---VLRKKVGMVFQKPN-PFPMSI--- 99
Cdd:PLN03073 209 VGRNGTGKTTFLRymAMHAIDGIPKNCQIlhvEQEVVGDDTTALQcvlNTDIErtqLLEEEAQLVAQQRElEFETETgkg 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 100 -------YDNIAFGPRTHGIHNKVQLDEIVERSLKQAAIW------DEVKDRLNKSalgMSGGQQQRLCIARALAIEPDV 166
Cdd:PLN03073 289 kgankdgVDKDAVSQRLEEIYKRLELIDAYTAEARAASILaglsftPEMQVKATKT---FSGGWRMRIALARALFIEPDL 365
|
170 180 190
....*....|....*....|....*....|....*.
gi 517187183 167 LLMDEPTSALDPISTAKIEDLVIELKKkyTIVMVTH 202
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSH 399
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-179 |
3.48e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkSL-------NRMNDLV--KNCRITGEVTLDkedv 72
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLitgdhpqGYSNDLTlfGRRRGSGETIWD---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 73 yrdldinvLRKKVGMVfqkpnpfpmsiydniafgprthgiHNKVQLDEIVERSLKQA---------AIWDEVKDRLNKSA 143
Cdd:PRK10938 334 --------IKKHIGYV------------------------SSSLHLDYRVSTSVRNVilsgffdsiGIYQAVSDRQQKLA 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517187183 144 ------LGMSG------------GQQQRLCIARALAIEPDVLLMDEPTSALDPI 179
Cdd:PRK10938 382 qqwldiLGIDKrtadapfhslswGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-205 |
4.65e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYY--GDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlvknCRITGEVTLDKEDvYRDLDINV 80
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDGVS-WNSVTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIYDNIafGPrthgiHNKVQLDEI--VERSLKQAAIWDEVKDRLN----KSALGMSGGQQQRL 154
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNL--DP-----YEQWSDEEIwkVAEEVGLKSVIEQFPDKLDfvlvDGGYVLSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQ 205
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-202 |
6.18e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLK--------SLNRMNDLVKNCRITgevTLDKEDvyrd 75
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKviaghpayKILEGDILFKGESIL---DLEPEE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 76 ldinvlRKKVG--MVFQKPNPFP-MSIYD--NIAFGPRtHGIHNKVQLD-----EIVERSLKQAAIWDEVKDR-LNKsal 144
Cdd:CHL00131 81 ------RAHLGifLAFQYPIEIPgVSNADflRLAYNSK-RKFQGLPELDpleflEIINEKLKLVGMDPSFLSRnVNE--- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 145 GMSGGQQQRLCIARALAIEPDVLLMDEPTSALDpISTAKIEDLVIE--LKKKYTIVMVTH 202
Cdd:CHL00131 151 GFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKIIAEGINklMTSENSIILITH 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-204 |
6.73e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 31 ITAFIGPSGCGKSTLLKSLNrmNDLVKN-CRITGEVTLDkedvyrdldiNVLRKKVGMVFQkpNPFPMsIYDNiafgpRT 109
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILS--GELIPNlGDYEEEPSWD----------EVLKRFRGTELQ--NYFKK-LYNG-----EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 110 HGIHnKVQLDEIVERSLK-----------QAAIWDEVKDRLNKSAL------GMSGGQQQRLCIARALAIEPDVLLMDEP 172
Cdd:PRK13409 161 KVVH-KPQYVDLIPKVFKgkvrellkkvdERGKLDEVVERLGLENIldrdisELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 517187183 173 TSALDPISTAKIEDLVIELKKKYTIVMVTHNM 204
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
7.14e-09 |
|
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: 54.04 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVTLDKEDVYRDLDInVLRK 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP-----PLAGRVLLNGGPLDFQRDS-IARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKPNPFPMSIYDNIAFGPRTHGihnkvqlDEIVERSLKQAAIwDEVKDRLNKSalgMSGGQQQRLCIARALAIE 163
Cdd:cd03231 75 LLYLGHAPGIKTTLSVLENLRFWHADHS-------DEQVEEALARVGL-NGFEDRPVAQ---LSAGQQRRVALARLLLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517187183 164 PDVLLMDEPTSALDPISTAKIEDLVI-ELKKKYTIVMVTH 202
Cdd:cd03231 144 RPLWILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTH 183
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-202 |
1.25e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMndlVKNCriTGEVTLDKEDV--YrdlDINVLRKKVGMVFQKPNPFP 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM---VEVC--GGEIRVNGREIgaY---GLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 MSIYDNiafgprthgihnkvqLDEIVERSlkQAAIW----------------DEVKDRLNKSALGMSGGQQQRLCIARAL 160
Cdd:PTZ00243 1398 GTVRQN---------------VDPFLEAS--SAEVWaalelvglrervasesEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517187183 161 AIE-PDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTH 202
Cdd:PTZ00243 1461 LKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAH 1503
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-231 |
1.40e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCG--KSTLLKSLNRMNDLVKNCRITGEVTldkedvyrdlDIN 79
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCA----------NRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 80 VLRKKVGMvfQKP----NPFPMSIYDNIAFGPRTHGIHNK---VQLDEIVER-SLKQAAiwdevkdrlNKSALGMSGGQQ 151
Cdd:NF000106 82 ALRRTIG*--HRPvr*gRRESFSGRENLYMIGR*LDLSRKdarARADELLERfSLTEAA---------GRAAAKYSGGMR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 152 QRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNMQQAVRISDKTAFFLLGEIVEYNKTSQ 230
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
.
gi 517187183 231 L 231
Cdd:NF000106 231 L 231
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-239 |
1.62e-08 |
|
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: 54.24 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNldlyygdFKALKNINLEIASNeITAFIGPSGCGKSTLLKSLNRMNDLvkncriTGEVTLDKEDVYRDLDINVLR 82
Cdd:COG3593 5 KIKIKN-------FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP------SSSRKFDEEDFYLGDDPDLPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 83 KKVGMVFQKPnpfPMSIYDNIAFGPRTHGIHNKVQ-LDEIVERSLKQAAiwDEVKDRLNKSALG---------------- 145
Cdd:COG3593 71 IEIELTFGSL---LSRLLRLLLKEEDKEELEEALEeLNEELKEALKALN--ELLSEYLKELLDGldlelelsldeledll 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 146 -----------------MSGGQQQRLCIARALAI-------EPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMV 200
Cdd:COG3593 146 kslslriedgkelpldrLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIIT 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 517187183 201 THNMqQAVRISDKTAFFLLGEIVEYNKTSQLFSMPQDER 239
Cdd:COG3593 226 THSP-HLLSEVPLENIRRLRRDSGGTTSTKLIDLDDEDL 263
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
17-202 |
1.99e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSlnrMNDLVKNcrITGEVTLDKedvyrdlDInvlrkKVGMVFQKPNPFP 96
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKD--FNGEARPQP-------GI-----KVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 -MSIYDNIAfgprtHGIHNKVQ-LDEIVERSLK------------------QAAI-----WD-EVKDRLNKSAL------ 144
Cdd:TIGR03719 82 tKTVRENVE-----EGVAEIKDaLDRFNEISAKyaepdadfdklaaeqaelQEIIdaadaWDlDSQLEIAMDALrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517187183 145 ----GMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKkyTIVMVTH 202
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-225 |
5.24e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 15 DFKALKNINLEIASNEITAFIGPSGCGKSTLlkslnrmndlvkNCRITGEVTLDKEDVYRDLDINVLRKKVGMVFQkpnp 94
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTL------------SNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 fpMSIYDNIAFGPRTHGIHNK---VQLDEIVERSLKQAAIWDEVKDrlnksalgMSGGQQQRLCIARALAIEPDVLLMDE 171
Cdd:PRK13546 100 --LTGIENIEFKMLCMGFKRKeikAMTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 172 PTSALDPISTAKIEDLVIELKK-KYTIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-178 |
6.83e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNLDLYYGDFK-ALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDlDINVL 81
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-----GEILLDGKPVTAE-QPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQKPNPFPmsiydniafgpRTHGIHNKVQLDEIVERSLKQAAIWDEVKDRLNK-SALGMSGGQQQRLCIARAL 160
Cdd:PRK10522 396 RKLFSAVFTDFHLFD-----------QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLAL 464
|
170
....*....|....*...
gi 517187183 161 AIEPDVLLMDEPTSALDP 178
Cdd:PRK10522 465 AEERDILLLDEWAADQDP 482
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-201 |
7.17e-08 |
|
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: 52.83 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 2 NKIEIKNLDLYY--GDfKALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncRITGEV------TLDKEDvy 73
Cdd:TIGR00954 450 NGIKFENIPLVTpnGD-VLIESLSFEVPSGNNLLICGPNGCGKSSLF-------------RILGELwpvyggRLTKPA-- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 74 rdldinvlRKKVGMVFQKPNP----------FPMSIYDNIAFGPRTH---GIHNKVQLDEIVERSLKqaaiWDEVKDRLN 140
Cdd:TIGR00954 514 --------KGKLFYVPQRPYMtlgtlrdqiiYPDSSEDMKRRGLSDKdleQILDNVQLTHILEREGG----WSAVQDWMD 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 141 KsalgMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPistaKIEDLVIELKKKYTIVMVT 201
Cdd:TIGR00954 582 V----LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFS 634
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-222 |
1.06e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 20 KNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVkncriTGEVTLDKEDVyRDLDInVLRKKVGMVF-----QKPNP 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR-----GGRIMLNGKEI-NALST-AQRLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 F---PMS------IYDNIAFGPRTHgihnkvQLDEIVERSLKQAAIwdevK-DRLNKSALGMSGGQQQRLCIARALAIEP 164
Cdd:PRK15439 353 YldaPLAwnvcalTHNRRGFWIKPA------RENAVLERYRRALNI----KfNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 165 DVLLMDEPTSALDPISTAKIEDLVIELKKKYT-IVMVTHNMQQAVRISDKTAFFLLGEI 222
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
1-202 |
1.41e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 51.12 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNldlyygdFKALKNINLEIAsnEITAFIGPSGCGKSTLLKSL----------------------NRMNDLVKN 58
Cdd:COG4938 1 IKSISIKN-------FGPFKEAELELK--PLTLLIGPNGSGKSTLIQALllllqsnfiylpaersgparlyPSLVRELSD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 59 CRITGEVTLDKEDVYRDLDINVLRKKvgmvfqkpnpfpmSIYDNIA-----FGPRTHGIHNKVQLDEIVERSLkqaaiWD 133
Cdd:COG4938 72 LGSRGEYTADFLAELENLEILDDKSK-------------ELLEQVEewlekIFPGKVEVDASSDLVRLVFRPS-----GN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 134 EVKDRLnksaLGMSGGQQQRLCI---ARALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTH 202
Cdd:COG4938 134 GKRIPL----SNVGSGVSELLPIllaLLSAAKPGSLLIIEEPEAHLHPKAQSALAELLAELaNSGVQVIIETH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-200 |
1.67e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNrmNDLVKncrITGEVTLDKEDVYRdLDINV 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA--GELPL---LSGERQSQFSHITR-LSFEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 81 LRKKVGMVFQKPNPFPMSIyDNIAFGpRTHG--IHNKVQLDEIVERSLKQAAIwdevKDRLNKSALGMSGGQQQRLCIAR 158
Cdd:PRK10938 75 LQKLVSDEWQRNNTDMLSP-GEDDTG-RTTAeiIQDEVKDPARCEQLAQQFGI----TALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517187183 159 ALAIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMV 200
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLhQSGITLVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-200 |
4.95e-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: 50.17 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 30 EITAFIGPSGCGKSTLLKSLNrmNDLVKN-CRITGEVTLDKedvyrdldinVLRKKVGMV----FQKpnpfpmsIYDNia 104
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILS--GELKPNlGDYDEEPSWDE----------VLKRFRGTElqdyFKK-------LANG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 105 fgpRTHGIHnKVQLDEIVERSLK-----------QAAIWDEVKDRLN-KSALG-----MSGGQQQRLCIARALAIEPDVL 167
Cdd:COG1245 159 ---EIKVAH-KPQYVDLIPKVFKgtvrellekvdERGKLDELAEKLGlENILDrdiseLSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 517187183 168 LMDEPTSALD---PISTAKiedLVIELKKKYTIVMV 200
Cdd:COG1245 235 FFDEPSSYLDiyqRLNVAR---LIRELAEEGKYVLV 267
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-225 |
5.24e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLlkslnrmNDLVKNCRITGEVTLDKEDVYRDLDINVlrkkvGMVFQkpnpfpM 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTL-------SNLIAGVTMPNKGTVDIKGSAALIAISS-----GLNGQ------L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIYDNIAFGPRTHGIhNKVQLDEIVERSLKQAaiwdEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALD 177
Cdd:PRK13545 101 TGIENIELKGLMMGL-TKEKIKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517187183 178 PISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDKTAFFLLGEIVEY 225
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEY 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
145-213 |
9.68e-07 |
|
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: 49.05 E-value: 9.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 145 GMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDR 472
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-212 |
1.01e-06 |
|
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: 47.70 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 18 ALKNINLEIASNEITAFIGPSGCGKSTLLkslnrmndlvkncritgevtldkedvyrdLDINVLRKKVGMVFQKPNPFPM 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------------------NEGLYASGKARLISFLPKFSRN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 98 SIydnIAFGprthgihnkvQLDEIVERSLKQAaiwdevkdRLNKSALGMSGGQQQRLCIARALA--IEPDVLLMDEPTSA 175
Cdd:cd03238 61 KL---IFID----------QLQFLIDVGLGYL--------TLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517187183 176 LDPISTAKIEDLVIEL-KKKYTIVMVTHN---MQQAVRISD 212
Cdd:cd03238 120 LHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-204 |
1.02e-06 |
|
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: 48.38 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLL-----KSLNRMNDLVKNC-----RITGEVTLDKE------------------ 70
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdRIEGLEHIDKVividqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 71 -----DVYRD---------------LDINVLRKKVGMVFQkpnpfpMSIYDNIAFGPRTHGIHNKVQLdeiversLKQAA 130
Cdd:cd03271 91 ytgvfDEIRElfcevckgkrynretLEVRYKGKSIADVLD------MTVEEALEFFENIPKIARKLQT-------LCDVG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 131 IwDEVKdrLNKSALGMSGGQQQRLCIARAL---AIEPDVLLMDEPTSALDPISTAKIEDLVIEL-KKKYTIVMVTHNM 204
Cdd:cd03271 158 L-GYIK--LGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNL 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-177 |
1.47e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLkslnRMndlvkncrITGEVTLDK------EDVyrdld 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLF----RM--------ITGQEQPDSgtieigETV----- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 invlrkKVGMVFQK-----PNPfpmSIYDNIAFGprthgihnkvqLDEIVERSLkqaaiwdEVKDRLNKSALGMSGGQQQ 152
Cdd:TIGR03719 386 ------KLAYVDQSrdaldPNK---TVWEEISGG-----------LDIIKLGKR-------EIPSRAYVGRFNFKGSDQQ 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 517187183 153 ------------RLCIARALAIEPDVLLMDEPTSALD 177
Cdd:TIGR03719 439 kkvgqlsggernRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-204 |
1.49e-06 |
|
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: 48.13 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 30 EITAFIGPSGCGKSTLLKSLNrmNDLVKN-CRITGEVTLDK--------------EDVyRDLDINVLRKkVGMVFQKPNP 94
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILA--GKLKPNlGKFDDPPDWDEildefrgselqnyfTKL-LEGDVKVIVK-PQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 95 FPMSIYDNIAfgpRTHGIHnkvQLDEIVERSlkqaaiwdEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTS 174
Cdd:cd03236 103 VKGKVGELLK---KKDERG---KLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|..
gi 517187183 175 ALDPISTAKIEDLVIELKK--KYTIVmVTHNM 204
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEddNYVLV-VEHDL 199
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-57 |
4.16e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.85 E-value: 4.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 517187183 3 KIEIKNldlyygdFKALKNINLEIASneITAFIGPSGCGKSTLLKSLNRMNDLVK 57
Cdd:COG4637 4 RIRIKN-------FKSLRDLELPLGP--LTVLIGANGSGKSNLLDALRFLSDAAR 49
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
147-202 |
4.22e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 4.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVielkKKY--TIVMVTH 202
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
82-213 |
4.24e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 82 RKKVGMVFQkpnpfpMSIYDNIafgprTHGIHNKVQLDEIVERSLKQAAIWDEVKdRLN-KSALGM------SGGQQQRL 154
Cdd:PRK13549 347 RKRDGIVPV------MGVGKNI-----TLAALDRFTGGSRIDDAAELKTILESIQ-RLKvKTASPElaiarlSGGNQQKA 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 155 CIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQAVRISDK 213
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGLSDR 474
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-202 |
6.04e-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: 45.68 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 31 ITAFIGPSGCGKSTLL---------------KSLNRMNDLVKNCRITGEVTLDKEDVyRDLDINVLRKkvgmvfqkpnpf 95
Cdd:cd03240 24 LTLIVGQNGAGKTTIIealkyaltgelppnsKGGAHDPKLIREGEVRAQVKLAFENA-NGKKYTITRS------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 96 pMSIYDNIAFgprthgIHNKvQLDEIVERSLKQaaiwdevkdrlnksalgMSGGQQQ------RLCIARALAIEPDVLLM 169
Cdd:cd03240 91 -LAILENVIF------CHQG-ESNWPLLDMRGR-----------------CSGGEKVlasliiRLALAETFGSNCGILAL 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 517187183 170 DEPTSALDPIS-TAKIEDLVIELKKKYT--IVMVTH 202
Cdd:cd03240 146 DEPTTNLDEENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-203 |
7.38e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 28 SNEITAFIGPSGCGKSTLLKSLNRmndlvkncritgevtldkedvyrdldiNVLRKKVGMVFQKPNPFPmsiydniafgp 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR---------------------------ELGPPGGGVIYIDGEDIL----------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 108 rthgihnkvqldeiverslkQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKI--- 184
Cdd:smart00382 43 --------------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLlll 102
|
170 180
....*....|....*....|...
gi 517187183 185 ----EDLVIELKKKYTIVMVTHN 203
Cdd:smart00382 103 eelrLLLLLKSEKNLTVILTTND 125
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-212 |
8.20e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLL------KSLNRMNDLVKNCRITGEVTLDKEDVYRdldINVLRKKVGmVFQKp 92
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaEGQRRYVESLSAYARQFLGQMDKPDVDS---IEGLSPAIA-IDQK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 93 npfpmsiydNIAFGPR-----THGIHNKVQL----DEIVERsLKQAaiwDEVKD---RLNKSALGMSGGQQQRLCIARAL 160
Cdd:cd03270 86 ---------TTSRNPRstvgtVTEIYDYLRLlfarVGIRER-LGFL---VDVGLgylTLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517187183 161 AIEPDVLL--MDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHN---MQQAVRISD 212
Cdd:cd03270 153 GSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDedtIRAADHVID 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-205 |
1.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KI--EIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLnrMNDLVKNcriTGEVTLDKE------DVYR 74
Cdd:PRK11147 317 KIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQAD---SGRIHCGTKlevayfDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 75 -DLDinvlrkkvgmvfqkPNPFPMsiyDNIAFGPRTHGIHNKvqldeivER---SLKQAAIWDEVKDRLNKSALgmSGGQ 150
Cdd:PRK11147 392 aELD--------------PEKTVM---DNLAEGKQEVMVNGR-------PRhvlGYLQDFLFHPKRAMTPVKAL--SGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517187183 151 QQRLCIARALAIEPDVLLMDEPTSALDpistakIE--DLVIELKKKY--TIVMVTHNMQ 205
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLD------VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-82 |
2.23e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 44.90 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIKNldlyygdFKALKNINLEIaSNEITAFIGPSGCGKSTLLKSLNRM--NDLVKNCRITGEVTLDKEDVYRDLDI 78
Cdd:pfam13175 3 IKSIIIKN-------FRCLKDTEIDL-DEDLTVLIGKNNSGKSSILEALDIFlnNKEKFFEDDFLVLYLKDVIKIDKEDL 74
|
....
gi 517187183 79 NVLR 82
Cdd:pfam13175 75 NIFE 78
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-218 |
2.60e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDLVKncritGEVTLDKEDVYRDLdiNVLRK 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK-----GEILFERQSIKKDL--CTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 84 KVGMVFQKP--NPFpMSIYDNIAFGprTHGIHNKVQLDEIVeRSLKQAAIWDEVKDRLnksalgmSGGQQQRLCIARALA 161
Cdd:PRK13540 75 QLCFVGHRSgiNPY-LTLRENCLYD--IHFSPGAVGITELC-RLFSLEHLIDYPCGLL-------SSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517187183 162 IEPDVLLMDEPTSALDPISTAKIEDLVIELKKKYTIVMVTHNMQQAVRISDKTAFFL 218
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
147-222 |
2.91e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.00 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 147 SGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTAKIEDLVIE-LKKKYTIVMVTHNMQQA------VRISDKTAFFLL 219
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECealctrLAIMVKGAFQCL 2151
|
...
gi 517187183 220 GEI 222
Cdd:TIGR01257 2152 GTI 2154
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-244 |
4.15e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 139 LNKSALGMSGGQQQRLCIARALAIEPD--VLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNMQQ---AVRISD 212
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIID 549
|
90 100 110
....*....|....*....|....*....|....
gi 517187183 213 --KTAFFLLGEIVeYNKTSQLFSMPQDERTENYI 244
Cdd:PRK00635 550 igPGAGIFGGEVL-FNGSPREFLAKSDSLTAKYL 582
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-209 |
4.32e-05 |
|
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: 42.73 E-value: 4.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 144 LGMSGGQQQRLCIARALAIE---PDVL-LMDEPTSALDPISTAKIEDLVIELKKKYTIVMV-THNMQQAVR 209
Cdd:cd03227 76 LQLSGGEKELSALALILALAslkPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIViTHLPELAEL 146
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1-45 |
4.83e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 4.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIK-----NLdlyygdfkalKNINLEIASNEITAFIGPSGCGKSTL 45
Cdd:COG0178 3 MDKIRIRgarehNL----------KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-191 |
6.04e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLLKSL-NRMNdlvkncriTGEVTLDKEDV-YRDLDINVLRKkVGMVFQKPNPFP 96
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVT--------TGVITGGDRLVnGRPLDSSFQRS-IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 97 MS-IYDNIAFG-----PRTHGIHNKVQ-LDEIVE----RSLKQAAIwdevkdrlNKSALGMSGGQQQRLCIARALAIEPD 165
Cdd:TIGR00956 850 TStVRESLRFSaylrqPKSVSKSEKMEyVEEVIKllemESYADAVV--------GVPGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 517187183 166 VLL-MDEPTSALDPISTAKIEDLVIEL 191
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-177 |
7.71e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 4 IEIKNLDLYYGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKslnrMndlvkncrITGEVTLDK------EDVyrdld 77
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK----M--------ITGQEQPDSgtikigETV----- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 78 invlrkKVGMVFQ-----KPNPfpmSIYDNIAFGprthgihnkvqLDEIVersLKQAaiwdEVKDRLNKSALGMSGGQQQ 152
Cdd:PRK11819 388 ------KLAYVDQsrdalDPNK---TVWEEISGG-----------LDIIK---VGNR----EIPSRAYVGRFNFKGGDQQ 440
|
170 180 190
....*....|....*....|....*....|....*..
gi 517187183 153 ------------RLCIARALAIEPDVLLMDEPTSALD 177
Cdd:PRK11819 441 kkvgvlsggernRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
132-217 |
9.37e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 132 WDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDP---ISTAKIEDLVIELKKKyTIVMVTHNMQQAV 208
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEGKK-TALVVEHDLAVLD 136
|
....*....
gi 517187183 209 RISDKTAFF 217
Cdd:cd03222 137 YLSDRIHVF 145
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
136-203 |
1.95e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517187183 136 KDRLNKSALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALDpistakiEDLVIELK---KKY--TIVMVTHN 203
Cdd:PRK10636 140 NEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEkwlKSYqgTLILISHD 205
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
112-203 |
2.50e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 112 IHNKVQLDEIVERSLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAI---EPDVLLMDEPTSALDPISTAKIEDLV 188
Cdd:pfam13304 203 GEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELL 282
|
90
....*....|....*.
gi 517187183 189 IELKKKYT-IVMVTHN 203
Cdd:pfam13304 283 KELSRNGAqLILTTHS 298
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
145-182 |
2.55e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 2.55e-04
10 20 30
....*....|....*....|....*....|....*...
gi 517187183 145 GMSGGQQQRLCIARALAIEPDVLLMDEPTSALDPISTA 182
Cdd:PLN03140 1019 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1-45 |
2.74e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 517187183 1 MNKIEIK-----NLdlyygdfkalKNINLEIASNEITAFIGPSGCGKSTL 45
Cdd:PRK00349 3 MDKIIIRgarehNL----------KNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-45 |
6.06e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.06e-04
10 20
....*....|....*....|....*..
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTL 45
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-204 |
6.45e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 6.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 138 RLNKSALGMSGGQQQRLCIARAL---AIEPDVLLMDEPTSALDPISTAKIEDLVIELKKK-YTIVMVTHNM 204
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKgNTVVVIEHNL 892
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
31-144 |
7.10e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 31 ITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITgeVTLDKEDVYRDLDINVLRkkvgmvfqkpnpfpmsiydniAFGPRTH 110
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVF--VDLPSGTSPKDLLRALLR---------------------ALGLPLS 63
|
90 100 110
....*....|....*....|....*....|....*....
gi 517187183 111 GIHNKVQLDEIVERSLKQAA-----IWDEVkDRLNKSAL 144
Cdd:pfam13401 64 GRLSKEELLAALQQLLLALAvavvlIIDEA-QHLSLEAL 101
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-249 |
8.25e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 3 KIEIKNldlyygdFKALKN---INLEIASNE---ITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTLDK------- 69
Cdd:COG1106 4 SFSIEN-------FRSFKDeltLSMVASGLRllrVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPflldses 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 70 -------------EDVYRDLDINVLRKKVGM--------VFQKPNPFPMSIYD----NIAFGPRTHGIHNKVQLDEIVER 124
Cdd:COG1106 77 knepsefeilfllDGVRYEYGFELDKERIISewlyflstAAQLNVPLLSPLYDwfdnNISLDTSSDGLTLLLKEDESLKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 125 SLKQA-AIWD------EVKDRLNKSALG------------------MSGGQQQRLCIARALAI---EPDVLLMDEPTSAL 176
Cdd:COG1106 157 ELLELlKIADpgiediEVEEEEIEDLVErklifkhkggnvplplseESDGTKRLLALAGALLDalaKGGVLLIDEIEASL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 177 DPISTAKIEDLVIELKKKYT--IVMVTHN---MQQAVRISDKTAFFLL-----GEIVEYNKTSqlFSMPQDER-TENYIT 245
Cdd:COG1106 237 HPSLLRKLLKLFLDLANKNNaqLIFTTHStelLDAFLELLRRDQIWFVekdkdGASELYSLED--FKVRKDENlEKGYLQ 314
|
....
gi 517187183 246 GRFG 249
Cdd:COG1106 315 GRYG 318
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-177 |
1.12e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 5 EIKNLDLY---YGDFKALKNINLEIASNEITAFIGPSGCGKSTLLKSL-----NRmndlvkncRITGEVTLDKEDVyrdl 76
Cdd:NF040905 259 EVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsyGR--------NISGTVFKDGKEV---- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 77 DINVL--------------RKKVGMVFqkpnpfPMSIYDNIAFgPRTHGIHNKVQLDEIVERslkqaAIWDEVKDRLN-K 141
Cdd:NF040905 327 DVSTVsdaidaglayvtedRKGYGLNL------IDDIKRNITL-ANLGKVSRRGVIDENEEI-----KVAEEYRKKMNiK 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517187183 142 S------ALGMSGGQQQRLCIARALAIEPDVLLMDEPTSALD 177
Cdd:NF040905 395 TpsvfqkVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-65 |
1.31e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*...
gi 517187183 28 SNEITAFIGPSGCGKSTLLKSLnrMNDLVkncRITGEV 65
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNAL--LPELV---LATGEI 116
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-189 |
1.50e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 17 KALKNINLEIASNEITAFIGPSGCGKSTLLKSLNRMNDlvkncRITGEVtldkedVYRDLDINVLRK--------KVGMV 88
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQ-----PSSGNI------YYKNCNINNIAKpyctyighNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517187183 89 FQkpnpfpMSIYDNIAFGPRthgIHNKVQLdeiversLKQAAIWDEVKDRLNKSALGMSGGQQQRLCIARALAIEPDVLL 168
Cdd:PRK13541 83 LE------MTVFENLKFWSE---IYNSAET-------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180
....*....|....*....|.
gi 517187183 169 MDEPTSALDPISTAKIEDLVI 189
Cdd:PRK13541 147 LDEVETNLSKENRDLLNNLIV 167
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-49 |
2.38e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 2.38e-03
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
31-67 |
3.25e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 38.57 E-value: 3.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 517187183 31 ITAFIGPSGCGKSTLLKSLNRMNDLVKNCRITGEVTL 67
Cdd:COG5192 71 IVAVVGPPGTGKSTLIRSLVRRFTKQTIDEIRGPITV 107
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-69 |
3.81e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 3.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLL---------KSLNRMNDLVKNC-RITGEVTLDK 69
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLInetlykalaRKLNGAKKVPGKHkEIEGLEHLDK 685
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
153-202 |
4.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 4.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 517187183 153 RLCIARALAIEPDVLLMDEPTSALDpISTAK-IEDLVIElkKKYTIVMVTH 202
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INTIRwLEDVLNE--RNSTMIIISH 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-69 |
5.57e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 5.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLL---------KSLNRMNDLVKNC-RITGEVTLDK 69
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVndilypalaRKLNGAKEKPGPHdSIEGLEHIDK 681
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-46 |
6.03e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.03e-03
10 20
....*....|....*....|....*...
gi 517187183 19 LKNINLEIASNEITAFIGPSGCGKSTLL 46
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-46 |
9.25e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.25e-03
|
| |
