|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-258 |
6.57e-178 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 489.16 E-value: 6.57e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDP 80
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPtMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:COG1117 88 VELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKI 240
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYL------GELVEFGPTEQI 240
|
250
....*....|....*...
gi 694049011 241 FSNPTQKATEDYISGRFG 258
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-257 |
2.68e-142 |
|
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: 398.98 E-value: 2.68e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPtMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKIFSNP 244
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYD------GELVEYGPTEQIFTNP 234
|
250
....*....|...
gi 694049011 245 TQKATEDYISGRF 257
Cdd:TIGR00972 235 KEKRTEDYISGRF 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-258 |
6.63e-132 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 373.35 E-value: 6.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTmSIRDNVVAGLKLQGGRGkkELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKG--DMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNLEAT---GKPGKLIEIDDTEKIF 241
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTeggGRYGYLVEFDRTEKIF 247
|
250
....*....|....*..
gi 694049011 242 SNPTQKATEDYISGRFG 258
Cdd:PRK14243 248 NSPQQQATRDYVSGRFG 264
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-240 |
3.28e-124 |
|
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: 352.25 E-value: 3.28e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPtMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDkpGGGLSGGQQQRLCIARAIA 164
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKI 240
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLL------NGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-258 |
1.75e-109 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 315.95 E-value: 1.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPtMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFnLEatgkpGKLIEIDDTEKIFSNP 244
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFF-LD-----GDLIEYNDTKQMFMNP 238
|
250
....*....|....
gi 694049011 245 TQKATEDYISGRFG 258
Cdd:PRK14239 239 KHKETEDYISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-258 |
2.36e-96 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 282.89 E-value: 2.36e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDP 80
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQG-GRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCI 159
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEK 239
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYL------GKLIEVGPTRK 234
|
250
....*....|....*....
gi 694049011 240 IFSNPTQKATEDYISGRFG 258
Cdd:PRK14267 235 VFENPEHELTEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
3.42e-85 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 254.45 E-value: 3.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGsgVDPVGV 83
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK--MDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQG-GRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRlVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFnleatgKPGKLIEIDDTEKIFS 242
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL------YKGQIVEWGPTREVFT 234
|
250
....*....|....
gi 694049011 243 NPTQKATEDYISGR 256
Cdd:PRK14247 235 NPRHELTEKYVTGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-258 |
5.92e-82 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 246.49 E-value: 5.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPtMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQ--ELKQDFTIVIVTHNMQQAARVSDQTGFFNLEATgKPGKLIEIDDTEKIFS 242
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEN-RIGQLVEFGLTKKIFN 245
|
250
....*....|....*.
gi 694049011 243 NPTQKATEDYISGRFG 258
Cdd:PRK14258 246 SPHDSRTREYVLSRLG 261
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-256 |
1.92e-66 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 206.82 E-value: 1.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGSVLLDGEDIYGsgVDPVGVRRTIGMVFQRPNPFP 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKiKVDGKVLYFGKDIFQ--IDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSA 178
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 179 LDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFnleatgKPGKLIEIDDTEKIFSNPTQKATEDYISGR 256
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFL------YNGELVEWGSSNEIFTSPKNELTEKYVIGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-258 |
5.03e-65 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 203.79 E-value: 5.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGvDPVGVRRTIGMVFQRPNPFPt 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSAL 179
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 180 DPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPTQKATEDYISGRFG 258
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFF------DGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
9.50e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 194.06 E-value: 9.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDK-PGgglsggqqqRLCIARAI 163
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL----ADKADAyPAqlsg-gqqqRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTEKIFS 242
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVF--MDG----GRIVEEGPPEEFFE 225
|
250
....*....|..
gi 694049011 243 NPTQKATEDYIS 254
Cdd:COG1126 226 NPQHERTRAFLS 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-221 |
6.07e-51 |
|
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: 164.28 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVvaGLKLQGGRGKkeldeiaerslkganlwnevkdrldkpggglsggqqqRLCIARAIA 164
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENI--ALGLSGGQQQ-------------------------------------RVALARALA 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFN 221
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-221 |
1.20e-50 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 165.00 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvR 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDV--TGVPPE--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRgKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVP-KAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFN 221
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMN 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-246 |
1.23e-50 |
|
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: 172.78 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGV 78
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-----SGSILFDGKDLTKlSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 DPVGVRRTIGMVFQrpNPF----PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRL-------DKpgg 147
Cdd:COG1123 336 SLRELRRRVQMVFQ--DPYsslnPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYphelsggQR--- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 148 glsggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNLeat 225
Cdd:COG1123 411 -------QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYD--- 480
|
250 260
....*....|....*....|.
gi 694049011 226 gkpGKLIEIDDTEKIFSNPTQ 246
Cdd:COG1123 481 ---GRIVEDGPTEEVFANPQH 498
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-220 |
1.05e-48 |
|
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: 160.00 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFF 220
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFM 208
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-244 |
6.40e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 160.64 E-value: 6.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVN-IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRR 85
Cdd:COG1125 4 FENVTkRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPT-----SGRILIDGEDI--RDLDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 86 TIGMVFQRPNPFPTMSIRDNV--VAGLKlqgGRGKKELDEIAERSLKGANLW-NEVKDRldKPGgglsggqqqRLC---- 158
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIatVPRLL---GWDKERIRARVDELLELVGLDpEEYRDR--YPH---------ELSggqq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 159 ----IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFnleatgKPGKLI 232
Cdd:COG1125 143 qrvgVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVM------REGRIV 216
|
250
....*....|..
gi 694049011 233 EIDDTEKIFSNP 244
Cdd:COG1125 217 QYDTPEEILANP 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
7.36e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 7.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGS 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 77 GVDpvgvrrtIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKpggglsggqqqR 156
Cdd:COG1116 79 GPD-------RGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGL----AGFEDAyphqlsggmrqR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFnleaTGKPGKLIEI 234
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVL----SARPGRIVEE 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-234 |
4.22e-47 |
|
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: 156.09 E-value: 4.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYG----KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygsgvdp 80
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGL----SGFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFnleaTGKPGKLIEI 234
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADRVVVL----SARPGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-253 |
6.47e-47 |
|
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: 156.31 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV 83
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT-----SGEIFIDGEDI--REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnEVKDRLDKPGGGLSGGQQQRLCIARAI 163
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFnleatgKPGKLIEIDDTEKIF 241
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIM------KNGEIVQVGTPDEIL 224
|
250
....*....|..
gi 694049011 242 SNPTQKATEDYI 253
Cdd:cd03295 225 RSPANDFVAEFV 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
2.95e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAK-RLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVd 79
Cdd:COG3842 1 MAMpALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-----SGRILLDGRDV--TGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVGvRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwNEVKDRldKPGgglsggqqqRL-- 157
Cdd:COG3842 73 PPE-KRNVGMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGL-EGLADR--YPH---------QLsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 158 ------CIARAIAVSPDVLLMDEPCSALDPisTLAiEDLIQELKQ-----DFTIVIVTHNMQQAARVSDQTGFFNLeatg 226
Cdd:COG3842 139 gqqqrvALARALAPEPRVLLLDEPLSALDA--KLR-EEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMND---- 211
|
250
....*....|....*...
gi 694049011 227 kpGKLIEIDDTEKIFSNP 244
Cdd:COG3842 212 --GRIEQVGTPEEIYERP 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
3.25e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.75 E-value: 3.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGsgvDPVGVR 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-----SGEVRVLGEDVAR---DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNV--VAGLKlqgGRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLrfFARLY---GLPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQTGFFN---LEATGKPGKLIE 233
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDkgrIVADGTPDELKA 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-244 |
1.12e-44 |
|
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: 152.51 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtPGARVEGSVLLDGEDIYG-SGVD 79
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDLLKlSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVGVR-RTIGMVFQrpNPF----PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRLDKpggglsggqq 154
Cdd:COG0444 80 LRKIRgREIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRyphelsggmr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 qRLCIARAIAVSPDVLLMDEPCSALDpISTLA-IEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNLeatgkpGKL 231
Cdd:COG0444 157 qRVMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYA------GRI 229
|
250
....*....|...
gi 694049011 232 IEIDDTEKIFSNP 244
Cdd:COG0444 230 VEEGPVEELFENP 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-236 |
1.56e-44 |
|
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: 149.96 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDIYG-SGVDPVGV 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRP---DSGEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAI 163
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARVSDQTGFF---NLEATGKPGKLIEIDD 236
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLydgKIVAEGTPEELRASDD 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-234 |
4.18e-43 |
|
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: 146.11 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDP 80
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRT-IGMVFQrpNPF----PTMSIRDNVVAGLKLQGGRGKKEldEIAERSLKGANLWNEVKDRLDKpggglsggqqq 155
Cdd:cd03257 77 RKIRRKeIQMVFQ--DPMsslnPRMTIGEQIAEPLRIHGKLSKKE--ARKEAVLLLLVGVGLPEEVLNRyphelsggqrq 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIE 233
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYA------GKIVE 226
|
.
gi 694049011 234 I 234
Cdd:cd03257 227 E 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-236 |
8.01e-43 |
|
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: 145.51 E-value: 8.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGV 83
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-----SGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRL--------DKpggglsggqqq 155
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMpselsggmRK----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFN---LEATGKPGK 230
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLAdgkIIAEGTPEE 228
|
....*.
gi 694049011 231 LIEIDD 236
Cdd:COG1127 229 LLASDD 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
3.29e-42 |
|
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: 143.73 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgVR 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-----SGSVLFDGEDITGLPPHEI-AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGG---------RGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQ 155
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLA----DLADRPAGELSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAARVSD 215
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLAD 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-212 |
3.88e-42 |
|
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: 143.01 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYG----KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDP 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGV--RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLC 158
Cdd:cd03255 76 LAAfrRRHIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAAR 212
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEY 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-217 |
8.52e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 8.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPtMSIRDNVVAGLKLqggRGKKELDEIAERSLKGANLWNEVkdrLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:COG4619 74 RQVAYVPQEPALWG-GTVRDNLPFPFQL---RERKFDRERALELLERLGLPPDI---LDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQT 217
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRV 201
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-254 |
1.45e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 145.22 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPV 81
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT-----SGSVLVDGVDLTAlSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKEldeIAERSlkgANLWNEV--KDRLD----------Kpgggl 149
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAE---IRKRV---AELLELVglSDKADaypsqlsggqK----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 150 sggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFfnLEAtgk 227
Cdd:COG1135 147 -----QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAV--LEN--- 216
|
250 260
....*....|....*....|....*..
gi 694049011 228 pGKLIEIDDTEKIFSNPTQKATEDYIS 254
Cdd:COG1135 217 -GRIVEQGPVLDVFANPQSELTRRFLP 242
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-244 |
1.74e-41 |
|
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: 141.95 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYG----KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPV 81
Cdd:cd03258 4 LKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-----SGSVLVDGTDLTLlSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLqGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTEK 239
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAV--MEK----GEVVEEGTVEE 227
|
....*
gi 694049011 240 IFSNP 244
Cdd:cd03258 228 VFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-248 |
1.05e-40 |
|
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: 146.59 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGARVEGSVLLDGEDIYGSGV 78
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 DPVGvrRTIGMVFQRP-NPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRL 157
Cdd:COG1123 79 ALRG--RRIGMVFQDPmTQLNPVTVGDQIAEALENLG-LSRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 158 CIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEID 235
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRV------VVMDDGRIVEDG 225
|
250
....*....|...
gi 694049011 236 DTEKIFSNPTQKA 248
Cdd:COG1123 226 PPEEILAAPQALA 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-249 |
1.05e-40 |
|
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: 140.32 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK----FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSgvDP 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRR--RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRP----NPFptMSIRDNVVAGLKLQGgrgKKELDEIAERSLKGANLWNEVKDR---------LDkpgg 147
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR--HTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSFLDRyphqlsggqRQ---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 148 glsggqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSDQTGFFnleat 225
Cdd:COG1124 146 --------RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAHLCDRVAVM----- 212
|
250 260
....*....|....*....|....
gi 694049011 226 gKPGKLIEIDDTEKIFSNPTQKAT 249
Cdd:COG1124 213 -QNGRIVEELTVADLLAGPKHPYT 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-255 |
1.10e-40 |
|
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: 140.86 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRR-TIGMVFQRPNP 96
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT-----SGKVLIDGQDIAAmSRKELRELRRkKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPC 176
Cdd:cd03294 114 LPHRTVLENVAFGLEVQG-VPRAEREERAAEALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 177 SALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFSNPTQKATEDYIS 254
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRI------AIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
.
gi 694049011 255 G 255
Cdd:cd03294 263 G 263
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-244 |
1.91e-40 |
|
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: 139.00 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVN-IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV 83
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-----SGEVLVDGKDI--TKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQrpNP-----FPTmsIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPggglsggqqqRLC 158
Cdd:COG1122 74 RRKVGLVFQ--NPddqlfAPT--VEEDVAFGPENLG-LPREEIRERVEEALELVGLE----HLADRPphelsggqkqRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF-TIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDT 237
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRVIVLD------DGRIVADGTP 218
|
....*..
gi 694049011 238 EKIFSNP 244
Cdd:COG1122 219 REVFSDY 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-215 |
2.61e-40 |
|
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: 139.40 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPV--- 81
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-----SGRILFDGRDI--TGLPPHria 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 --GVRRTigmvFQRPNPFPTMSIRDNVVAGLKLQGGRG--------------KKELDEIAERSLKGANLwnevKDRLDKP 145
Cdd:COG0411 78 rlGIART----FQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGL----ADRADEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 146 GGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSD 215
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLAD 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.41e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 136.71 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYG----KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGS 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 77 GVDPVGV--RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPggglsggqq 154
Cdd:COG1136 76 SERELARlrRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGL----GDRLDHRpsqlsggqq 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 qRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAAR 212
Cdd:COG1136 151 qRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-244 |
3.26e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.13 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRS---LnrmheVTPGarvEGSVLLDGEDIYgSGVdPV 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagL-----ETPD---SGRIVLNGRDLF-TNL-PP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRtIGMVFQRPNPFPTMSIRDNVVAGLKlQGGRGKKELDEIAERSLKGANLwNEVKDRldKPggglsggqqqRLCIAR 161
Cdd:COG1118 73 RERR-VGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQL-EGLADR--YPsqlsg-gqrqRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEK 239
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADRVVVMN------QGRIEQVGTPDE 220
|
....*
gi 694049011 240 IFSNP 244
Cdd:COG1118 221 VYDRP 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-221 |
1.21e-38 |
|
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: 132.52 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGsgvDPVGVR 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDIKK---EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNvvagLKLQGGrGKKeldeiaerslkganlwnevkdrldkpggglsggqqqRLCIARAIA 164
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVREN----LKLSGG-MKQ------------------------------------RLALAQALL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF-TIVIVTHNMQQAARVSDQTGFFN 221
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILN 169
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-216 |
1.64e-38 |
|
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: 134.79 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDL--ASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLK-LQG--GRGKKELDEIAERSLKGANLWnEVKDRLdkpggglsggqQQRL--- 157
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALGRYpHLGlfGRPSAEDREAVEEALERTGLE-HLADRP-----------VDELsgg 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 158 -----CIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:COG1120 142 erqrvLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADR 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
2.58e-38 |
|
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: 131.74 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-GKFHAV-SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFpTMSIRDNVvaglkLQGGrgkkeldeiaERslkganlwnevkdrldkpggglsggqqQRLCIARA 162
Cdd:cd03228 74 LRKNIAYVPQDPFLF-SGTIRENI-----LSGG----------QR---------------------------QRIAIARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARV 213
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA 161
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-244 |
2.68e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.04 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAkRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDP 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT-----SGEILIGGRDV--TDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VgvRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwNEVKDRldKPGgglsggqqqRLCIA 160
Cdd:COG3839 73 K--DRNIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGL-EDLLDR--KPKqlsg-gqrqRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTE 238
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTHDQVEAMTLADRIAVMND------GRIQQVGTPE 219
|
....*.
gi 694049011 239 KIFSNP 244
Cdd:COG3839 220 ELYDRP 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-255 |
2.96e-37 |
|
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: 134.59 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV----RRTIGMVFQRP 94
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPT-----AGQIFIDGENI--MKQSPVELrevrRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDE 174
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLG-WPEQERKEKALELLKLVGL----EEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 175 PCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFSNPTQKATEDY 252
Cdd:TIGR01186 156 AFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRI------VIMKAGEIVQVGTPDEILRNPANEYVEEF 229
|
...
gi 694049011 253 ISG 255
Cdd:TIGR01186 230 IGK 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-217 |
3.60e-37 |
|
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: 130.28 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFH--AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-----SGEVLVDGKDL--TKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQrpNP---FPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:cd03225 75 RKVGLVFQ--NPddqFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQT 217
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRV 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-231 |
9.94e-37 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 129.41 E-value: 9.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPG-ARVEGsvlldgediYGSGVDPVGVRRTIGMVFQ 92
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGrATVAG---------HDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 RPNPFPTMSIRDNVVAGLKLQGGRGKkELDEIAERSLKGANLWnEVKDRLDKpggGLSGGQQQRLCIARAIAVSPDVLLM 172
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGA-ERRERIDELLDFVGLL-EAADRLVK---TYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 173 DEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFN---LEATGKPGKL 231
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDhgrIIAEGTPEEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-216 |
1.19e-36 |
|
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: 126.98 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRT 86
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDI--AKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQrpnpfptmsirdnvvaglkLQGGrgkkeldeiaERSlkganlwnevkdrldkpggglsggqqqRLCIARAIAVS 166
Cdd:cd00267 75 IGYVPQ-------------------LSGG----------QRQ---------------------------RVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 167 PDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADR 149
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-215 |
2.80e-36 |
|
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: 127.94 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarVEGSVLLDGEDIygSGVDPVG-V 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MGLLPP---RSGSIRFDGRDI--TGLPPHErA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDN-VVAGLKLQGGRGKKELDEIAErslkganLWNEVKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENlLLGAYARRRAKRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSD 215
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIAD 200
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-253 |
9.58e-36 |
|
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: 126.97 E-value: 9.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvR 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKDI--TNLPPH--K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQL----EGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDpiSTLAiEDLIQELKQ-----DFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEK 239
Cdd:cd03300 147 NEPKVLLLDEPLGALD--LKLR-KDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMN------KGKIQQIGTPEE 217
|
250
....*....|....
gi 694049011 240 IFSNPTQKATEDYI 253
Cdd:cd03300 218 IYEEPANRFVADFI 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-233 |
2.36e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 126.36 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFFN---LEATGKPGKLIE 233
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDkgrIAEDGDPQVLIK 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
6.42e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 6.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarVEGSVLLDGEDiygsgvdP 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI--LGLLPP---TSGTVRLFGKP-------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPN---PFPtMSIRDNVVAGLKLQGG---RGKKELDEIAERSLKGANLWnevkDRLDKPggglsggqq 154
Cdd:COG1121 71 RRARRRIGYVPQRAEvdwDFP-ITVRDVVLMGRYGRRGlfrRPSRADREAVDEALERVGLE----DLADRPigelsggqq 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 qRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFFNleatgkpGKLIE 233
Cdd:COG1121 146 qRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLN-------RGLVA 218
|
....*....
gi 694049011 234 IDDTEKIFS 242
Cdd:COG1121 219 HGPPEEVLT 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-238 |
1.02e-34 |
|
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: 126.35 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGsgvDPVGVRRTIGMVFQ 92
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPTS---GTARVAGYDVVR---EPRKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 RPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLM 172
Cdd:TIGR01188 74 YASVDEDLTGRENLEMMGRLYG-LPKDEAEERAEELLELFELG----EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 173 DEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTE 238
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIID------HGRIIAEGTPE 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-254 |
1.67e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevTPGArveGSVLLDGEDI-YGSGVDPVGV 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLE--TPDS---GQLNIAGHQFdFSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 ---RRTIGMVFQRPNPFPTMSIRDNVV-AGLKLQgGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCI 159
Cdd:COG4161 78 rllRQKVGMVFQQYNLWPHLTVMENLIeAPCKVL-GLSKEQAREKAMKLLARLRL----TDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTE 238
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVY--MEK----GRIIEQGDAS 226
|
250
....*....|....*.
gi 694049011 239 kIFSNPTQKATEDYIS 254
Cdd:COG4161 227 -HFTQPQTEAFAHYLS 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-254 |
2.70e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.07 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 6 DLKDVN-IYYGK---FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDP 80
Cdd:PRK11153 3 ELKNISkVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT-----SGRVLVDGQDLTAlSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSRTVFDNVALPLELAG-TPKAEIKARVTELLELVGL----SDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTE 238
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAV--IDA----GRLVEQGTVS 226
|
250
....*....|....*.
gi 694049011 239 KIFSNPTQKATEDYIS 254
Cdd:PRK11153 227 EVFSHPKHPLTREFIQ 242
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-215 |
2.63e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 121.32 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVN-IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVG 82
Cdd:COG3638 3 LELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTAlRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTMSIRDNVVAGL-----KLQGGRGK--KELDEIAERSLKGANLwnevKDRLDKPggglsggqqq 155
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVLAGRlgrtsTWRSLLGLfpPEDRERALEALERVGL----ADKAYQRadqlsggqqq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSD 215
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-177 |
4.90e-33 |
|
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: 117.36 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgvRRTIGMVFQRPNPFPT 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDERKSL--RKEIGYVFQDPQLFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 100 MSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCS 177
Cdd:pfam00005 74 LTVRENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-221 |
5.68e-33 |
|
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: 119.28 E-value: 5.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvR 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIGGRDV--TDLPPK--D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGkkelDEIAERSLKGANLWnEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPK----DEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 165 VSPDVLLMDEPCSALDP---ISTLA-IEDLIQELKQdfTIVIVTHNMQQAARVSDQTGFFN 221
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrVQMRAeLKRLQQRLGT--TTIYVTHDQVEAMTMADRIAVMN 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-205 |
7.81e-33 |
|
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: 126.10 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFH--AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPV 81
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDL--RQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFPTmSIRDNvvaglkLQGGRGKKELDEIaERSLKGANLWNEVK---DRLD--------------K 144
Cdd:COG2274 546 SLRRQIGVVLQDVFLFSG-TIREN------ITLGDPDATDEEI-IEAARLAGLHDFIEalpMGYDtvvgeggsnlsggqR 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 145 pggglsggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:COG2274 618 ----------QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-244 |
8.84e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 122.14 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDpvgvR 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT-----EGQIFIDGEDVTHRSIQ----Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKkelDEIAERslkganlwneVKDRL---------DKPGGGLSGGQQQ 155
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLG-VPK---EERKQR----------VKEALelvdlagfeDRYVDQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTGFFNleatgkPGKLIE 233
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMN------KGKIMQ 217
|
250
....*....|.
gi 694049011 234 IDDTEKIFSNP 244
Cdd:PRK11432 218 IGSPQELYRQP 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-253 |
1.10e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 122.52 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG---VRRT-IGMVFQRP 94
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT-----AGEVLIDGEDI--TKLSKKElreLRRKkMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPggglsggqqqRLCIARAIAVSPDVLLMDE 174
Cdd:COG4175 115 ALLPHRTVLENVAFGLEIQG-VPKAERRERAREALELVGL----AGWEDSYpdelsggmqqRVGLARALATDPDILLMDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 175 PCSALDPistlaiedLI------------QELKQdfTIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFS 242
Cdd:COG4175 190 AFSALDP--------LIrremqdellelqAKLKK--TIVFITHDLDEALRLGDRI------AIMKDGRIVQIGTPEEILT 253
|
250
....*....|.
gi 694049011 243 NPtqkATeDYI 253
Cdd:COG4175 254 NP---AN-DYV 260
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-231 |
1.25e-32 |
|
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: 118.76 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK--FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygsGVDPVG 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-----SGTAYINGYSI---RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTMSIRDNVV--AGLKlqgGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRfyARLK---GLPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFN---LEATGKPGKL 231
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSdgkLRCIGSPQEL 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-244 |
1.79e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRRTIGMVFQrpNP 96
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-----SGEILFDGQDITGlSGRELRPLRRRMQMVFQ--DP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 F----PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRldkpggglsggqqqRLCIARAIAVSPDVLLM 172
Cdd:COG4608 105 YaslnPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRyphefs---ggqrqRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 173 DEPCSALDpISTLA-IEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKIFSNP 244
Cdd:COG4608 182 DEPVSALD-VSIQAqVLNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMYL------GKIVEIAPRDELYARP 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-245 |
4.30e-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: 119.91 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 36 IGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGg 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDV--TNVPPH--LRHINMVFQSYALFPHMTVEENVAFGLKMRK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 116 RGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPistlAIEDLIQ-EL 194
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQL----EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDK----KLRDQMQlEL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 195 KQ-----DFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPT 245
Cdd:TIGR01187 144 KTiqeqlGITFVFVTHDQEEAMTMSDRIAIMR------KGKIAQIGTPEEIYEEPA 193
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-253 |
6.11e-32 |
|
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: 117.40 E-value: 6.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI-YGSGVDPVG 82
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDItKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTMSIRDNVVAG-------LKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKpgggLSGGQQQ 155
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENVLHGrlgykptWRSLLGRFSEEDKERALSALERVGLADKAYQRADQ----LSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDqtgffnleatgkpgKLIE 233
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYAD--------------RIVG 218
|
250 260
....*....|....*....|
gi 694049011 234 IDDTEKIFSNPTQKATEDYI 253
Cdd:TIGR02315 219 LKAGEIVFDGAPSELDDEVL 238
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-254 |
1.27e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGarvEGSVLLDGEDiYGSGVDPVGV--- 83
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSG---TLNIAGNHFD-FSKTPSDKAIrel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVV-AGLKLQgGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIeAPCRVL-GLSKDQALARAEKLLERLRL----KPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTEKiF 241
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVY--MEN----GHIVEQGDASC-F 228
|
250
....*....|...
gi 694049011 242 SNPTQKATEDYIS 254
Cdd:PRK11124 229 TQPQTEAFKNYLS 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-251 |
2.11e-31 |
|
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: 116.13 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI-YGSGVDPVGVRRTIGMVF 91
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDInKLKGKALRQLRRQIGMIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNPFPTMSIRDNVVAGL-----KLQGGRG--KKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03256 85 QQFNLIERLSVLENVLSGRlgrrsTWRSLFGlfPKEEKQRALAALERVGL----LDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDqtgffnleatgkpgKLIEIDDTEKIFS 242
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYAD--------------RIVGLKDGRIVFD 226
|
....*....
gi 694049011 243 NPTQKATED 251
Cdd:cd03256 227 GPPAELTDE 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-245 |
2.38e-31 |
|
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: 115.90 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvRRTIGMVFQR 93
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-----SGTILFGGEDA--TDVPVQ--ERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSlkgANLWNEVK-DRL-DKPGGGLSGGQQQRLCIARAIAVSPDVLL 171
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKV---HELLKLVQlDWLaDRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 172 MDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPT 245
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMN------KGRIEQVGTPDEVYDHPA 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-205 |
8.05e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.88 E-value: 8.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAV-SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:COG1132 339 EIEFENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-----SGRILIDGVDI--RDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFpTMSIRDNvvagLKLqgGRGKKELDEIaERSLKGANLWNEVK---DRLD--------------Kp 145
Cdd:COG1132 412 LRRQIGVVPQDTFLF-SGTIREN----IRY--GRPDATDEEV-EEAAKAAQAHEFIEalpDGYDtvvgergvnlsggqR- 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 146 ggglsggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:COG1132 483 ---------QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-215 |
9.10e-31 |
|
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: 114.31 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG-V 83
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-----SGSIRFDGEDI--TGLPPHRiA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRG--KKELDEIAErslkganLWNEVKDRLDKPGGGLSggqqqrLCIAR 161
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAevRADLERVYE-------LFPRLKERRRQRAGTLSggeqqmLAIGR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSD 215
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIAD 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-219 |
8.74e-30 |
|
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: 111.31 E-value: 8.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 15 GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGsgvDPVGVRRTIGMVFQRP 94
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPDA---GFATVDGFDVVK---EPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPFPTMSIRDNVV--AGLK-LQGGRGKKELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLL 171
Cdd:cd03266 88 GLYDRLTARENLEyfAGLYgLKGDELTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 172 MDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQTGF 219
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-244 |
9.79e-30 |
|
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: 111.66 E-value: 9.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHaVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGArveGSVLLDGEDIygSGVDPVgvR 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPDS---GKILLNGKDI--TNLPPE--K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGK---KELDEIAErSLKGANLWNEVKDRLDkpggglsGGQQQRLCIAR 161
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKeieRKVLEIAE-MLGIDHLLNRKPETLS-------GGEQQRVAIAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 162 AIAVSPDVLLMDEPCSALDPistLAIEDLIQELKQ-----DFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDD 236
Cdd:cd03299 143 ALVVNPKILLLDEPFSALDV---RTKEKLREELKKirkefGVTVLHVTHDFEEAWALADKVAIML------NGKLIQVGK 213
|
....*...
gi 694049011 237 TEKIFSNP 244
Cdd:cd03299 214 PEEVFKKP 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
1.55e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKF----HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLrslNRMHE-VTPGArveGSVLLDGEDIYGSGV 78
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGfLAPSS---GEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 DpvgvrRtiGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLC 158
Cdd:COG4525 77 D-----R--GVVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQA 210
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-244 |
1.85e-29 |
|
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: 113.66 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRS---LNRmhevTPGARVE--GSVLLDGEdiygSGVD-PVGvRRTIGMVFQRPN 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER----PDSGRIRlgGEVLQDSA----RGIFlPPH-RRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 96 PFPTMSIRDNVVAGLK-LQGGRGKKELDEIAE------------RSLKGAnlwnevkDRldkpggglsggqqQRLCIARA 162
Cdd:COG4148 88 LFPHLSVRGNLLYGRKrAPRAERRISFDEVVEllgighlldrrpATLSGG-------ER-------------QRVAIGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTEKI 240
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADHVVL--LEQ----GRVVASGPLAEV 221
|
....
gi 694049011 241 FSNP 244
Cdd:COG4148 222 LSRP 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-254 |
5.26e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.84 E-value: 5.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSGVDPV-GVRRTIGMVFQRPNPFPTMS 101
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrQLRQHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDP 181
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 182 ISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPTQKATEDYIS 254
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMD------QGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-253 |
7.82e-29 |
|
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: 111.67 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGArvegsVLLDGEDIygSGVDP 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGT-----IYQGGRDI--TRLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VgvRRTIGMVFQRPNPFPTMSIRDNVVAGLKlqgGRGKKElDEIAERslkgANLWNEVKDRLD---KPGGGLSGGQQQRL 157
Cdd:TIGR03265 74 Q--KRDYGIVFQSYALFPNLTVADNIAYGLK---NRGMGR-AEVAER----VAELLDLVGLPGserKYPGQLSGGQQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 158 CIARAIAVSPDVLLMDEPCSALDpisTLAIEDLIQELKQ-----DFTIVIVTHNMQQAARVSDQTGFFN---LEATGKPg 229
Cdd:TIGR03265 144 ALARALATSPGLLLLDEPLSALD---ARVREHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNhgvIEQVGTP- 219
|
250 260
....*....|....*....|....
gi 694049011 230 klieiddtEKIFSNPTQKATEDYI 253
Cdd:TIGR03265 220 --------QEIYRHPATPFVADFV 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-216 |
8.27e-29 |
|
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: 107.52 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 6 DLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRR 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 86 TIGMVFQrpnpfptmsirdnvvaGLKLQGgrgkkeLDEIAERSlkganlWNEVKD--RldkpggglsggqqQRLCIARAI 163
Cdd:cd03214 74 KIAYVPQ----------------ALELLG------LAHLADRP------FNELSGgeR-------------QRVLLARAL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQ 216
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADR 167
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-245 |
1.85e-28 |
|
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: 109.08 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGK-----FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGS-GVDP 80
Cdd:TIGR04521 3 LKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPTS---GTVTIDGRDITAKkKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQrpnpFPTM-----SIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWNEVKD-----------Rldk 144
Cdd:TIGR04521 78 KDLRKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLG-LSEEEAEERVKEALELVGLDEEYLErspfelsggqmR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 145 pggglsggqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFNl 222
Cdd:TIGR04521 150 -----------RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMH- 217
|
250 260
....*....|....*....|...
gi 694049011 223 eatgkPGKLIEIDDTEKIFSNPT 245
Cdd:TIGR04521 218 -----KGKIVLDGTPREVFSDVD 235
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-213 |
4.18e-28 |
|
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: 112.16 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV 83
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTmSIRDNvvaglkLQGGRGKKELDEIaERSLKGANLWNEVK---DRLDKPGGGLSG----GQQQR 156
Cdd:COG4988 410 RRQIAWVPQNPYLFAG-TIREN------LRLGRPDASDEEL-EAALEAAGLDEFVAalpDGLDTPLGEGGRglsgGQAQR 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH---NMQQAARV 213
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI 541
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-217 |
4.38e-28 |
|
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: 106.46 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarVEGSVLLDGEDiygsgvdPVGVRRT 86
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--LGLLKP---TSGSIRVFGKP-------LEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQRPN---PFPtMSIRDNVVAGLKLQGG---RGKKELDEIAERSLKGANLwNEVKDRldkPGGGLSGGQQQRLCIA 160
Cdd:cd03235 70 IGYVPQRRSidrDFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGL-SELADR---QIGELSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQT 217
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRV 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-213 |
1.42e-27 |
|
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: 110.63 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPV 81
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDL--RDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFPTmSIRDNvvagLKLqggrGKKEL-DEIAERSLKGANL--W-NEVKDRLD-------------- 143
Cdd:COG4987 406 DLRRRIAVVPQRPHLFDT-TLREN----LRL----ARPDAtDEELWAALERVGLgdWlAALPDGLDtwlgeggrrlsgge 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 144 -KpggglsggqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARV 213
Cdd:COG4987 477 rR-----------RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM 536
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-253 |
1.94e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.22 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDvtLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVDpvgvR 84
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLLNLIAGF--LPPDS---GRILWNGQDLTALPPA----E 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVV----AGLKL---QggrgKKELDEIAER-SLKGanlwneVKDRL-------DKpgggl 149
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIGlglrPGLKLtaeQ----RAQVEQALERvGLAG------LLDRLpgqlsggQR----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 150 sggqqQRLCIARAIAVSPDVLLMDEPCSALDPIstLAIE--DLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFNleat 225
Cdd:COG3840 136 -----QRVALARCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVA---- 204
|
250 260
....*....|....*....|....*...
gi 694049011 226 gkPGKLIEIDDTEKIFSNPTQKATEDYI 253
Cdd:COG3840 205 --DGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-205 |
5.38e-27 |
|
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: 103.81 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPrSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarVEGSVLLDGEDIygsGVDPVGVR 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRIL--ATLTPP---SSGTIRIDGQDV---LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNV--VAGLKlqgGRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLdyIAWLK---GIPSKEVKARVDEVLELVNLG----DRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-253 |
7.54e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvR 84
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-----AGQIMLDGVDL--SHVPPY--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKlqggRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQqRLCIARAIA 164
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLK----QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQ-RVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPI----STLAIEDLIQELkqDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKI 240
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMN------RGKFVQIGEPEEI 237
|
250
....*....|...
gi 694049011 241 FSNPTQKATEDYI 253
Cdd:PRK11607 238 YEHPTTRYSAEFI 250
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-213 |
1.05e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.21 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV-- 83
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT-----SGQVLVNGQDL--SRLKRREIpy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 -RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:COG2884 77 lRRRIGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNM----QQAARV 213
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLelvdRMPKRV 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-255 |
1.39e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 3 KRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIY----GSGV 78
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS-----EGSIVVNGQTINlvrdKDGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 DPVG-------VRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDrldKPGGGLSG 151
Cdd:PRK10619 79 LKVAdknqlrlLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG---KYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 152 GQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFFNleatgkPGK 230
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLH------QGK 229
|
250 260
....*....|....*....|....*
gi 694049011 231 LIEIDDTEKIFSNPTQKATEDYISG 255
Cdd:PRK10619 230 IEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-244 |
2.25e-26 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 103.34 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrMHEvTPGArveGSVLLDGEDIY----GSG--- 77
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN-LLE-TPDS---GEIRVGGEEIRlkpdRDGelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 -VDPVGVRRT---IGMVFQRPNPFPTMSIRDNVVAG-LKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGG 152
Cdd:COG4598 84 pADRRQLQRIrtrLGMVFQSFNLWSHMTVLENVIEApVHVLG-RPKAEAIERAEALLAKVGLA----DKRDAYPAHLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 153 QQQRLCIARAIAVSPDVLLMDEPCSALDPistlaieDLIQE-LK--QDF-----TIVIVTHNMQQAARVSDQTGFFN--- 221
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmRDLaeegrTMLVVTHEMGFARDVSSHVVFLHqgr 231
|
250 260
....*....|....*....|...
gi 694049011 222 LEATGKPgklieiddtEKIFSNP 244
Cdd:COG4598 232 IEEQGPP---------AEVFGNP 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-217 |
3.13e-26 |
|
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: 101.60 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 29 PRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGSVLLDGEdiygSGVDPVGVRRTIGMVFQRPNPFPTMSIRDNVV 107
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTiVLNGTVLFDSR----KKINLPPQQRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 108 AGLKlqggRGKKELDEIAERSLKGANLWNEVKDRldkPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAI 187
Cdd:cd03297 98 FGLK----RKRNREDRISVDELLDLLGLDHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|..
gi 694049011 188 EDLIQELKQDFTI--VIVTHNMQQAARVSDQT 217
Cdd:cd03297 171 LPELKQIKKNLNIpvIFVTHDLSEAEYLADRI 202
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-205 |
4.46e-26 |
|
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: 101.85 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTmS 101
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNVVAGLKlqggrgkKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQ-------RLCIARAIAVSPDVLLMDE 174
Cdd:cd03249 93 IAENIRYGKP-------DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQlsggqkqRIAIARALLRNPKILLLDE 165
|
170 180 190
....*....|....*....|....*....|.
gi 694049011 175 PCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-233 |
4.46e-26 |
|
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: 101.14 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygsgVDPVGVR 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-----SGEITFDGKSY----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRgKKELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIR-KKRIDEVLDVV--------GLKDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIE 233
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIIN------KGKLIE 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-255 |
9.22e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.34 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRRT-IGMVFQRPNP 96
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-----RGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDNVVAGLKLqGGRGKKELDEIAERSLKGANLWNEVKDRLDKpgggLSGGQQQRLCIARAIAVSPDVLLMDEPC 176
Cdd:PRK10070 118 MPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 177 SALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFSNPTQKATEDYIS 254
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRI------AIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
.
gi 694049011 255 G 255
Cdd:PRK10070 267 G 267
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-214 |
1.34e-25 |
|
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: 100.02 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 12 IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRRTIGMV 90
Cdd:TIGR02673 10 AYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPS-----RGQVRIAGEDVNRlRGRQLPLLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 91 FQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVL 170
Cdd:TIGR02673 85 FQDFRLLPDRTVYENVALPLEVRG-KKEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 171 LMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVS 214
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVA 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
2.77e-25 |
|
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: 99.52 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG-V 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-----SGSIRLDGEDI--TKLPPHErA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAErslkganLWNEVKDRLDKPGGGLSGGQQQRLCIARAI 163
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARVSDQ 216
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADR 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-249 |
3.34e-25 |
|
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: 103.61 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-----------GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevtpgaRVEGSVLLDGEDI 73
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 74 YG-SGVDPVGVRRTIGMVFQrpNPF----PTMSIRDNVVAGLKLQG-GRGKKELDEIAERSLKGANLWNEVKDRldkpgg 147
Cdd:COG4172 350 DGlSRRALRPLRRRMQVVFQ--DPFgslsPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRyphefs 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 148 glsggqqqRLCIARAIAVSPDVLLMDEPCSALDpISTLA-IEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTgffnleA 224
Cdd:COG4172 428 ---ggqrqRIAIARALILEPKLLVLDEPTSALD-VSVQAqILDLLRDLqrEHGLAYLFISHDLAVVRALAHRV------M 497
|
250 260
....*....|....*....|....*
gi 694049011 225 TGKPGKLIEIDDTEKIFSNPTQKAT 249
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDAPQHPYT 522
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-216 |
1.14e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygsgvdPVGVR 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-----SGEVLWDGEPL------DPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIG-MvfqrpnP-----FPTMSIRDNVV--AGLK-LQGGRGKKELDEIAERslkganLwnEVKDRLDKPGGGLSGGQQQ 155
Cdd:COG4152 71 RRIGyL------PeerglYPKMKVGEQLVylARLKgLSKAEAKRRADEWLER------L--GLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIV-THNMQQAARVSDQ 216
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDR 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-215 |
2.09e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvR 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI--THVPAE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQggrgKKELDEIAER---SLKGANLwNEVKDRldKPGGGLSGGQQqRLCIAR 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQ----KTPAAEITPRvmeALRMVQL-EEFAQR--KPHQLSGGQQQ-RVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEdliQELKQ-----DFTIVIVTHNMQQAARVSD 215
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQ---NELKAlqrklGITFVFVTHDQEEALTMSD 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-205 |
5.52e-24 |
|
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: 100.05 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 2 AKRLDLKDVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDP 80
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPL--ADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPTmSIRDNVvaglklqgGRGKKELDEIA-ERSLKGANLWNEVKDR-------LDKPGGGLSGG 152
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAG-TIAENI--------RLARPDASDAEiREALERAGLDEFVAALpqgldtpIGEGGAGLSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 153 QQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-205 |
9.42e-24 |
|
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: 95.37 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGIDI--RDISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTmSIRDNvvagLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQ----RLC 158
Cdd:cd03254 75 LRSMIGVVLQDTFLFSG-TIMEN----IRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQgerqLLA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.57e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGK-FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGSVLlDGEDIYGsgv 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRvKVMGREV-NAENEKW--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 dpvgVRRTIGMVFQRPNP--FpTMSIRDNVVAGlKLQGGRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQR 156
Cdd:PRK13647 77 ----VRSKVGLVFQDPDDqvF-SSTVWDDVAFG-PVNMGLDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQ 207
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-215 |
7.17e-23 |
|
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: 95.56 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGarvEGSVLLDGEDIYGS--GVDPVGVRRTIGMVFQRPNPFPT 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL--TRPD---EGEIVLNGRTLFDSrkGIFLPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevkdrLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSAL 179
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSERRISFERVIELLGIGHL-------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 694049011 180 DPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSD 215
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLAD 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-247 |
9.10e-23 |
|
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: 96.68 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK----FHAVSDVTLAVPPRSVTAFIGPSGCGKS----TVLRSLNRmhevtPGARVEGSVLLDGEDIygS 76
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD-----PAAHPSGSILFDGQDL--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 77 GVDPV---GVR-RTIGMVFQRP----NPFptMSIRDNVVAGLKLQGGRGKKEldeIAERSLKganLWNEV-----KDRLD 143
Cdd:COG4172 80 GLSERelrRIRgNRIAMIFQEPmtslNPL--HTIGKQIAEVLRLHRGLSGAA---ARARALE---LLERVgipdpERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 144 ----------KpggglsggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAA 211
Cdd:COG4172 152 ayphqlsggqR----------QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 694049011 212 RVSDQTgffnleATGKPGKLIEIDDTEKIFSNP----TQK 247
Cdd:COG4172 222 RFADRV------AVMRQGEIVEQGPTAELFAAPqhpyTRK 255
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-207 |
1.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK-FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDIYGSGVDPVGV 83
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRP-NPFPTMSIRDNVVAGLkLQGGRGKKELDEIAERSLKGANlwneVKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:PRK13636 81 RESVGMVFQDPdNQLFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTG----IEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNM 207
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDI 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-241 |
1.89e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 2 AKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDI--YGSGvd 79
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIqhYASK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 pvGVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQG---GRGKKELDEIAERSLKGANLWNEVKDRLDkpggGLSGGQQQR 156
Cdd:PRK10253 78 --EVARRIGLLAQNATTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAAR-----VSDQTGffNLEATGKPG 229
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRyashlIALREG--KIVAQGAPK 229
|
250
....*....|..
gi 694049011 230 KLIEIDDTEKIF 241
Cdd:PRK10253 230 EIVTAELIERIY 241
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-221 |
3.01e-22 |
|
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: 91.19 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEdiygsGVDPvGVR 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFDGK-----PLDI-AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVV-----AGLKLQGGRgkKELDEIAERsLKGANLWNEVKDRLDKpggglsgGQQQRLCI 159
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVylaqlKGLKKEEAR--RRIDEWLER-LELSEYANKRVEELSK-------GNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQTGFFN 221
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLN 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-241 |
3.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGV--DPVGVRRTIGMVFQRPNP 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-----QGSVRVDDTLITSTSKnkDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 --FPTMSIRDnvVAGLKLQGGRGKKELDEIAERSLkgaNLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDE 174
Cdd:PRK13649 97 qlFEETVLKD--VAFGPQNFGVSQEEAEALAREKL---ALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 175 PCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTgfFNLEAtgkpGKLIEIDDTEKIF 241
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFV--YVLEK----GKLVLSGKPKDIF 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-205 |
3.61e-22 |
|
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: 91.52 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK--FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDV--RDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTmSIRDNVVAGlklqggRGKKELDEIaERSLKGANLwNEVKDRLDKPGGGLSGGQQQ------- 155
Cdd:cd03251 74 LRRQIGLVSQDVFLFND-TVAENIAYG------RPGATREEV-EEAARAANA-HEFIMELPEGYDTVIGERGVklsggqr 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 156 -RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:cd03251 145 qRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-213 |
4.43e-22 |
|
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: 89.58 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPT 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-----SGRVRLDGADI--SQWDPNELGDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 mSIRDNVVAGLKLQggrgkkeldeiaerslkganlwnevkdrldkpggglsggqqqRLCIARAIAVSPDVLLMDEPCSAL 179
Cdd:cd03246 91 -SIAENILSGGQRQ------------------------------------------RLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 694049011 180 DPISTLAIEDLIQELK-QDFTIVIVTHNM---QQAARV 213
Cdd:cd03246 128 DVEGERALNQAIAALKaAGATRIVIAHRPetlASADRI 165
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-207 |
8.69e-22 |
|
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: 90.37 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQ 92
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI--REVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 RPNPFPTmSIRDNVVAGlKLQGGrgkkelDEIAERSLKGANLWNEVKDRLDKPGGGL-------SGGQQQRLCIARAIAV 165
Cdd:cd03253 83 DTVLFND-TIGYNIRYG-RPDAT------DEEVIEAAKAAQIHDKIMRFPDGYDTIVgerglklSGGEKQRVAIARAILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694049011 166 SPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNM 207
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-242 |
1.06e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKR-LDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGsg 77
Cdd:PRK13635 1 MKEEiIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 vdpvgVRRTIGMVFQRP-NPFPTMSIRDNVVAGLKLQGgrgkKELDEIAER---SLKGANLwnevKDRLDKPGGGLSGGQ 153
Cdd:PRK13635 79 -----VRRQVGMVFQNPdNQFVGATVQDDVAFGLENIG----VPREEMVERvdqALRQVGM----EDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 154 QQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK--QDFTIVIVTHNMQQAARvSDQTGFFNleatgkPGKL 231
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMN------KGEI 218
|
250
....*....|.
gi 694049011 232 IEIDDTEKIFS 242
Cdd:PRK13635 219 LEEGTPEEIFK 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-211 |
1.37e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtPGARVEGSVLLDGEDIYGSGVDpvgvR 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASGEVLLNGRRLTALPAE----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKlqGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEAGL----AGFADRDPATLSGGQRARVALLRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAA 211
Cdd:COG4136 150 AEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAP 198
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-210 |
1.51e-21 |
|
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: 88.63 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGArvegsVLLDGEDIYGSGVDPVGVRRTIGMVFQ 92
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGA-----VLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 RPNP--FPTmSIRDNVVAGLKLQGGRGkkelDEIAERslkganlwneVKDRL---------DKPGGGLSGGQQQRLCIAR 161
Cdd:TIGR01166 76 DPDDqlFAA-DVDQDVAFGPLNLGLSE----AEVERR----------VREALtavgasglrERPTHCLSGGEKKRVAIAG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQA 210
Cdd:TIGR01166 141 AVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-207 |
4.24e-21 |
|
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: 88.42 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPV 81
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-----SGSVLLDGTDI--RQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFpTMSIRDN------------VVAGLKLQG-----GRGKKELD-EIAERslkGANLwnevkdrld 143
Cdd:cd03245 75 DLRRNIGYVPQDVTLF-YGTLRDNitlgapladderILRAAELAGvtdfvNKHPNGLDlQIGER---GRGL--------- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 144 kpggglsgGQQQR--LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNM 207
Cdd:cd03245 142 --------SGGQRqaVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-205 |
4.52e-21 |
|
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: 87.92 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarVEGSVLLDGEDIygsGVDPVGV 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPP---SAGEVLWNGEPI---RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKkelDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAI 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRAD---REAIDEALEAVGL----AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQE-LKQDFTIVIVTH 205
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-243 |
5.04e-21 |
|
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: 88.22 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVdpvgvr 84
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPT-----SGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIaersLKGANLWNEVKdrldKPGGGLSGGQQQRLCIARAIA 164
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLG-LPDSRIDEV----LNIVDLTNTGK----KKAKQFSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFFNLEATGKPGKLIEIDDTEKIFSN 243
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSENLEKLFVE 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-243 |
5.95e-21 |
|
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: 89.03 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGSVLLDGEDIYGsgvdpv 81
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKvTVDGLDTLDEENLWE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 gVRRTIGMVFQRP-NPFPTMSIRDNVVAGLKlqgGRG--KKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLC 158
Cdd:TIGR04520 75 -IRKKVGMVFQNPdNQFVGATVEDDVAFGLE---NLGvpREEMRKRVDEALKLVGME----DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARvSDQTGFFNleatgkPGKLIEIDD 236
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMN------KGKIVAEGT 219
|
....*..
gi 694049011 237 TEKIFSN 243
Cdd:TIGR04520 220 PREIFSQ 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-216 |
7.36e-21 |
|
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: 85.94 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKEV--SFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RT-IGMVFQrpnpfptMSIrdnvvaglklqggrgkkeldeiAERslkganlwnevkdrldkpggglsggqqQRLCIARAI 163
Cdd:cd03216 74 RAgIAMVYQ-------LSV----------------------GER---------------------------QMVEIARAL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQ 216
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEIADR 151
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-205 |
8.52e-21 |
|
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: 86.84 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSL-NRmhevTPGARVEGSVLLDGEDIYgsgvdPVGVRRTIGMVFQRPNPFP 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGR----RTGLGVSGEVLINGRPLD-----KRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGLKLQGGRGkkeldeiAERslkganlwnevkdrldkpggglsggqqQRLCIARAIAVSPDVLLMDEPCSA 178
Cdd:cd03213 96 TLTVRETLMFAAKLRGLSG-------GER---------------------------KRVSIALELVSNPSLLFLDEPTSG 141
|
170 180
....*....|....*....|....*...
gi 694049011 179 LDPISTLAIEDLIQELKQD-FTIVIVTH 205
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-235 |
1.39e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.14 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgvrrtigMVFQRPNPFPTMS 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT-----SGGVILEGKQITEPGPDRM-------VVFQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNVVAGLK-LQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALD 180
Cdd:TIGR01184 71 VRENIALAVDrVLPDLSKSERRAIVEEHIALVGL----TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 181 PISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSDQTGFFNLEATGKPGKLIEID 235
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEhrVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVP 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-245 |
1.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.32 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGARVEGSVLLDGEDIYGSGVdpVGVRRTIGMVFQRP-NPF 97
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKTV--WDIREKVGIVFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGLKlqgGRG--KKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PRK13640 98 VGATVGDDVAFGLE---NRAvpRPEMIKIVRDVLADVGM----LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 176 CSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAArVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPT 245
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLD------DGKLLAQGSPVEIFSKVE 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-217 |
1.52e-20 |
|
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: 86.54 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtpgaRVEGSVLLDGEDIygsgvdPVGVR-RTIGMVF 91
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPI------KAKERrKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPN-PFPTMSIRDNVVAGLKLQGGRGkkeldEIAERSLKGANLWnEVKDRL-------DKpggglsggqqQRLCIARAI 163
Cdd:cd03226 78 QDVDyQLFTDSVREELLLGLKELDAGN-----EQAETVLKDLDLY-ALKERHplslsggQK----------QRLAIAAAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQT 217
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-240 |
1.87e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.80 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVRRTIGMVFQRP--NP 96
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-----SGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTmSIRDNVVAGLKlqgGRGKKElDEIAERSLKGANLWN-EVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PRK13637 97 FEE-TIEKDIAFGPI---NLGLSE-EEIENRVKRAMNIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 176 CSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTGFFN---LEATGKPGKLI-EIDDTEKI 240
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNkgkCELQGTPREVFkEVETLESI 242
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-216 |
1.94e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVgvRRT 86
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGDLFIGEKRM--NDVPPA--ERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQRPNPFPTMSIRDNVVAGLKLqGGRGKKELD---EIAERSLKGANLwnevkdrLDKPGGGLSGGQQQRLCIARAI 163
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKL-AGAKKEEINqrvNQVAEVLQLAHL-------LDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQ 216
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADK 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
1.97e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.43 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGediygsgvdpvgVR 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------------AR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVvaGLKLQGGRGKKELDEIAERSLKG-ANLWNEVKDRLDKpggglsggqqQRLCIARAI 163
Cdd:PRK11247 81 EDTRLMFQDARLLPWKKVIDNV--GLGLKGQWRDAALQALAAVGLADrANEWPAALSGGQK----------QRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSD 215
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAVAMAD 202
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-213 |
2.66e-20 |
|
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: 85.74 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRR 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFD-----SGQVYLNGQETPPlNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 86 -TIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWNevkdRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:TIGR03608 76 eKLGYLFQNFALIENETVEENLDLGLKYKK-LSKKEKREKKKEALEKVGLNL----KLKQKIYELSGGEQQRVALARAIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNM---QQAARV 213
Cdd:TIGR03608 151 KPPPLILADEPTGSLDPKNRDEVLDLLLELnDEGKTIIIVTHDPevaKQADRV 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-219 |
3.43e-20 |
|
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: 85.62 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGkfHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevTPGArveGSVLLDGEDIygSGVDPVgvR 84
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFE--TPQS---GRVLINGVDV--TAAPPA--D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNV----VAGLKLQGgRGKKELDEIAERsLKGANLWNEVKDRLDkpggglsGGQQQRLCIA 160
Cdd:cd03298 70 RPVSMLFQENNLFAHLTVEQNVglglSPGLKLTA-EDRQAIEVALAR-VGLAGLEKRLPGELS-------GGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSDQTGF 219
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-249 |
4.10e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKS-TVLRSLnrmhEVTPG--ARVEGSVLLDGEDiygsgVDPVGVR-RTIGMVFQRP- 94
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GILPAgvRQTAGRVLLDGKP-----VAPCALRgRKIATIMQNPr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 ---NPFPTMsiRDNVVAGLKlqgGRGKKELDEIAERSLKGANLwNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLL 171
Cdd:PRK10418 90 safNPLHTM--HTHARETCL---ALGKPADDATLTAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 172 MDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFSNPTQKAT 249
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDV------AVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-212 |
4.95e-20 |
|
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: 85.56 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 15 GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPV-GVR-RTIGMVFQ 92
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT-----SGTVRLAGQDLFALDEDARaRLRaRHVGFVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 RpnpF---PTMSIRDNVVAGLKLqggRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDV 169
Cdd:COG4181 98 S---FqllPTLTALENVMLPLEL---AGRRDARARARALLERVGL----GHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 170 LLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAAR 212
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-212 |
5.36e-20 |
|
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: 85.60 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFpTMS 101
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPI--SQYEHKYLHSKVSLVGQEPVLF-ARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNVVAGLklqggrGKKELDEIAERSLKG------ANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:cd03248 104 LQDNIAYGL------QSCSFECVKEAAQKAhahsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 694049011 176 CSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAAR 212
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-216 |
5.72e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLdGEDIYGSGVDPVG---VRRTIGMVFQrpn 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT-----SGTVTI-GERVITAGKKNKKlkpLRKKVGIVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 96 pFPTMSIRDNVVagLK------LQGGRGKKELDEIAERSLKGANLWNEVkdrLDKPGGGLSGGQQQRLCIARAIAVSPDV 169
Cdd:PRK13634 93 -FPEHQLFEETV--EKdicfgpMNFGVSEEDAKQKAREMIELVGLPEEL---LARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 170 LLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQ 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-244 |
1.23e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGVRRTIGMVFQRPNP-- 96
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT-----SGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDDql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 -FPTmsIRDNVVAGlKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PRK13639 92 fAPT--VEEDVAFG-PLNLGLSKEEVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 176 CSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNP 244
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMS------DGKIIKEGTPKEVFSDI 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-242 |
1.31e-19 |
|
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: 85.24 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGsgVDPVG---VRRTIGMVFQ-RPNPF 97
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA-----QGTVSFRGQDLYQ--LDRKQrraFRRDVQLVFQdSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 -PTMSIRDNVVAGLklqggRGKKELDEiAERSLKGANLWNEVK---DRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:TIGR02769 102 nPRMTVRQIIGEPL-----RHLTSLDE-SEQKARIAELLDMVGlrsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFS 242
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRV------AVMDKGQIVEECDVAQLLS 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-206 |
1.33e-19 |
|
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: 84.00 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVG- 82
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-----SGTIRVNGQDVSDLRGRAIPy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKkeldEIAERSLKGANLWNeVKDRLDKPGGGLSGGQQQRLCIARA 162
Cdd:cd03292 76 LRRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPR----EIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHN 206
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-227 |
1.47e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgVR 84
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-----SGRIVFDGKDITDWQTAKI-MR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGlklqGGRGKKEldEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAMG----GFFAERD--QFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSD-----QTGFFNLEATGK 227
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADrgyvlENGHVVLEDTGD 222
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-242 |
1.52e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFpTMS 101
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT-----GGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNVVAGLKlqggrgKKELDEI-AERSLKGA-----NLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:TIGR00958 571 VRENIAYGLT------DTPDEEImAAAKAANAhdfimEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 176 CSALDpistLAIEDLIQELK--QDFTIVIVTHNMQQAARvSDQTGFFNLEATGKPGKLIEIDDTEKIFS 242
Cdd:TIGR00958 645 TSALD----AECEQLLQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-249 |
1.65e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.60 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI---YGSGVDPVgvRRTIGMVFQrp 94
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFNGQRIdtlSPGKLQAL--RRDIQFIFQ-- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPFPTMSIRDNV---------VAGLkLQGGRGKKELDEIAER-SLKGANLWnevkdrldKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK10261 409 DPYASLDPRQTVgdsimeplrVHGL-LPGKAAAARVAWLLERvGLLPEHAW--------RYPHEFSGGQRQRICIARALA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKIFS 242
Cdd:PRK10261 480 LNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYL------GQIVEIGPRRAVFE 553
|
....*..
gi 694049011 243 NPTQKAT 249
Cdd:PRK10261 554 NPQHPYT 560
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-228 |
1.85e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDiygsgVDPVGVR 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-----SGHIRFHGTD-----VSRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 -RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAErslKGANLWNEVK-DRL-DKPGGGLSGGQQQRLCIAR 161
Cdd:PRK10851 73 dRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKA---KVTQLLEMVQlAHLaDRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLA----IEDLIQELKqdFTIVIVTHNMQQAARVSDQTGFF---NLEATGKP 228
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKElrrwLRQLHEELK--FTSVFVTHDQEEAMEVADRVVVMsqgNIEQAGTP 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
14-257 |
2.74e-19 |
|
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: 83.86 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVDpVGVRRTIGMVFQR 93
Cdd:TIGR04406 11 YKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGL--VRPDA---GKILIDGQDITHLPMH-ERARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:TIGR04406 85 ASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPtqKATEDY 252
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIIS------DGKVLAEGTPAEIVANE--KVRRVY 232
|
....*
gi 694049011 253 ISGRF 257
Cdd:TIGR04406 233 LGEQF 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-215 |
3.47e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevTPGarvEGSVLLDGEDiygsgVDPVGVR 84
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY--QPD---SGEILLDGEP-----VRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RT----IGMVFQRPNPFPTMSIRDNVVAGlKLQGGRG---KKELDEIAERSLK--GANLwnevkdRLDKPGGglsggqqq 155
Cdd:COG1129 75 DAqaagIAIIHQELNLVPNLSVAENIFLG-REPRRGGlidWRAMRRRARELLArlGLDI------DPDTPVG-------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 156 RLC--------IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSD 215
Cdd:COG1129 140 DLSvaqqqlveIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIAD 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-205 |
5.57e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 9 DVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTI 87
Cdd:PRK13657 339 DVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ-----SGRILIDGTDI--RTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 88 GMVFQRPNPFpTMSIRDNvvaglkLQGGRGKKELDEIAErSLKGANLWNEVKDRLDKPGGGLSGGQQQ-------RLCIA 160
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDN------IRVGRPDATDEEMRA-AAERAQAHDFIERKPDGYDTVVGERGRQlsggerqRLAIA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
8-246 |
5.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 8 KDVNIYYGK-----FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPV- 81
Cdd:PRK13646 6 DNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-----TGTVTVDDITITHKTKDKYi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 -GVRRTIGMVFQRPNpfpTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:PRK13646 81 rPVRKRIGMVFQFPE---SQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFnleatgKPGKLIEIDDTE 238
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVM------KEGSIVSQTSPK 231
|
....*...
gi 694049011 239 KIFSNPTQ 246
Cdd:PRK13646 232 ELFKDKKK 239
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-216 |
1.09e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDIYGSGvdPVGVR 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTP---QSGTVFLGDKPISMLS--SRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAG----LKLQgGRGKKELDEIAERSLKGAnlwnEVKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYGrspwLSLW-GRLSAEDNARVNQAMEQT----RINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQ 216
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDH 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-205 |
1.37e-18 |
|
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: 82.05 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEgsVLldGEDiYGsGVDPVGVR 84
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR--LF--GER-RG-GEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMV---FQRPNPfPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWnEVKDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:COG1119 78 KRIGLVspaLQLRFP-RDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELL-GLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTH 205
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTH 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-205 |
1.39e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKrLDLKDV-NIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVD 79
Cdd:PRK11650 1 MAG-LKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERIT-----SGEIWIGGRVV--NELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVgvRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKkelDEIAERSLKGANLWnEVKDRLDKPGGGLSGGQQQRLCI 159
Cdd:PRK11650 73 PA--DRDIAMVFQNYALYPHMSVRENMAYGLKIRG-MPK---AEIEERVAEAARIL-ELEPLLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDpistlA---------IEDLIQELKQdfTIVIVTH 205
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD-----AklrvqmrleIQRLHRRLKT--TSLYVTH 193
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-208 |
1.48e-18 |
|
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: 84.53 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNI-YYG-KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPV 81
Cdd:TIGR03375 463 EIEFRNVSFaYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT-----EGSVLLDGVDI--RQIDPA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFpTMSIRDNVVAGlklQGGRGKKELDEIAERSlkGA-NLWNEVKDRLDKPGGGlsggqqqR---- 156
Cdd:TIGR03375 536 DLRRNIGYVPQDPRLF-YGTLRDNIALG---APYADDEEILRAAELA--GVtEFVRRHPDGLDMQIGE-------Rgrsl 602
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 157 -------LCIARAIAVSPDVLLMDEPCSALDPISTlaiEDLIQELKQ---DFTIVIVTHNMQ 208
Cdd:TIGR03375 603 sggqrqaVALARALLRDPPILLLDEPTSAMDNRSE---ERFKDRLKRwlaGKTLVLVTHRTS 661
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-233 |
1.60e-18 |
|
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: 80.43 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYG--KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRmhEVTPGarvEGSVLLDGEDIYGSGVDpvg 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLEKA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTmSIRDNVvaGLKLQGGrgkkeldeiaERSlkganlwnevkdrldkpggglsggqqqRLCIARA 162
Cdd:cd03247 73 LSSLISVLNQRPYLFDT-TLRNNL--GRRFSGG----------ERQ---------------------------RLALARI 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 163 IAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVsDQTGFFnleatgKPGKLIE 233
Cdd:cd03247 113 LLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFL------ENGKIIM 176
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
7-219 |
1.67e-18 |
|
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: 81.06 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDIYGSGvdpvGVRRT 86
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSHTGLA----PYQRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQRPNPFPTMSIRDNVVAGLK--LQGGRGKKELDEIAERSLKGANLwnevkdrLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:TIGR01277 72 VSMLFQENNLFAHLTVRQNIGLGLHpgLKLNAEQQEKVVDAAQQVGIADY-------LDRLPEQLSGGQRQRVALARCLV 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGF 219
Cdd:TIGR01277 145 RPNPILLLDEPFSALDPLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAV 201
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-211 |
1.68e-18 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 81.30 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 16 KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrMHEVTPgarvEGSVLLDGEDIYG-SGVDPVGVRRT-IGMVFQR 93
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVTNlSYSQKIILRRElIGYIFQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVVAGLKLQGgRGKKELdeiAERSLKGANLWNeVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:NF038007 92 FNLIPHLSIFDNVALPLKYRG-VAKKER---IERVNQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLAD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694049011 174 EPCSALDPISTLAIedlIQELK----QDFTIVIVTHNMQQAA 211
Cdd:NF038007 167 EPTGNLDSKNARAV---LQQLKyinqKGTTIIMVTHSDEAST 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-210 |
1.79e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVDPvgvr 84
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF--VPYQH---GSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 rtiGMVFQRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWNEVKDRLDKpgggLSGGQQQRLCIARAIA 164
Cdd:PRK11248 73 ---GVVFQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQA 210
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-215 |
2.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDIYGSgVDPVgvRRTIGMVFQRPNP-- 96
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE-IKPV--RKKVGVVFQFPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDnvVAGLKLQGGRGKKELDEIAERSLKGANLwneVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPC 176
Cdd:PRK13643 98 FEETVLKD--VAFGPQNFGIPKEKAEKIAAEKLEMVGL---ADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 694049011 177 SALDPISTLAIEDLIQELKQDF-TIVIVTHNMQQAARVSD 215
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYAD 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-244 |
4.02e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SG-- 77
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT-----GGTILLRGQHIEGlPGhq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 VDPVGVRRTigmvFQRPNPFPTMSIRDN------------VVAGL-KLQGGRGkkeldeiAER-SLKGANLWNEVKDRLD 143
Cdd:PRK11300 77 IARMGVVRT----FQHVRLFREMTVIENllvaqhqqlktgLFSGLlKTPAFRR-------AESeALDRAATWLERVGLLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 144 ---KPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTG 218
Cdd:PRK11300 146 hanRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIY 225
|
250 260
....*....|....*....|....*....
gi 694049011 219 FFNLE---ATGKPgklieiddtEKIFSNP 244
Cdd:PRK11300 226 VVNQGtplANGTP---------EEIRNNP 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-233 |
6.16e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVDpvgVR 84
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDA---GSISLCGEPVPSRARH---AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNvvagLKLQG---GRGKKELDEIAERSLKGANLWNevkdRLDKPGGGLSGGQQQRLCIAR 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVREN----LLVFGryfGLSAAAARALVPPLLEFAKLEN----KADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 162 AIAVSPDVLLMDEPCSALDPIST-LAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFNLE---ATGKPGKLIE 233
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARhLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrkiAEGAPHALIE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-206 |
6.36e-18 |
|
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: 79.89 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGsgvDPVGVRRTIGMVF-- 91
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-----SGKILLDGQDITK---LPMHKRARLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLL 171
Cdd:cd03218 82 QEASIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI----THLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 694049011 172 MDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHN 206
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHN 192
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
6.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.93 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGK---FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSG 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 VdpVGVRRTIGMVFQRP-NPFPTMSIRDNVVAGLKLQGgrgkKELDEIAERSLKGANLWNeVKDRLDKPGGGLSGGQQQR 156
Cdd:PRK13650 76 V--WDIRHKIGMVFQNPdNQFVGATVEDDVAFGLENKG----IPHEEMKERVNEALELVG-MQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAArVSDQ 216
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDR 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-241 |
6.62e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrmheVTPGARVEGSVLLDGEDIygsGVDPVG--VRRTIGMVFQRPNPF 97
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV-----VGIVPRDAGNIIIDDEDI---SLLPLHarARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRLDKpggGLSGGQQQRLCIARAIAVSPDVLLMDEPCS 177
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 178 ALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQTGFF---NLEATGKPGKLIEIDDTEKIF 241
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVsqgHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-208 |
9.97e-18 |
|
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: 78.99 E-value: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFpTMS 101
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDI--STIPLEDLRSSLTIIPQDPTLF-SGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDNvvagLKLQGGRGKKELDEIAERSLKGANLwNEVKDRLdkpggglsggqqqrLCIARAIAVSPDVLLMDEPCSALDP 181
Cdd:cd03369 98 IRSN----LDPFDEYSDEEIYGALRVSEGGLNL-SQGQRQL--------------LCLARALLKRPRVLVLDEATASIDY 158
|
170 180
....*....|....*....|....*..
gi 694049011 182 ISTLAIEDLIQELKQDFTIVIVTHNMQ 208
Cdd:cd03369 159 ATDALIQKTIREEFTNSTILTIAHRLR 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-206 |
1.03e-17 |
|
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: 82.02 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYY-GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPV--SSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTmSIRDNvvaglkLQGGRGKKELDEIAE--RSLKGANLWNEVKDRLDKPGGGLSGG----QQQR 156
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT-TVREN------LRLARPDATDEELWAalERVGLADWLRALPDGLDTVLGEGGARlsggERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLA-IEDLIQELkQDFTIVIVTHN 206
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADElLEDLLAAL-SGRTVVLITHH 529
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-211 |
1.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGK---FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtpgaRVEGSVLLDGEDIYGSG 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKesdVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 VdpVGVRRTIGMVFQRP-NPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQR 156
Cdd:PRK13642 76 V--WNLRRKIGMVFQNPdNQFVGATVEDDVAFGMENQG-IPREEMIKRVDEALLAVNML----DFKTREPARLSGGQKQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 157 LCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAA 211
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAA 205
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-215 |
1.56e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.42 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmHEVTPGArveGSVLLDGEDIYG-SGVDPVGV 83
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPDH---GEILFDGENIPAmSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFPTMSIRDNVVAGLklqggRGKKELDEIAERS----------LKGA-NLW-NEVKDRLDKpggglsg 151
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPL-----REHTQLPAPLLHStvmmkleavgLRGAaKLMpSELSGGMAR------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 152 gqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSD 215
Cdd:PRK11831 151 ----RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIAD 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-217 |
2.10e-17 |
|
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: 78.63 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 16 KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEdiyGSGVD-----PVGV----RRT 86
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD-----SGSILVRHD---GGWVDlaqasPREIlalrRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQRPNPFPTMSIRDnVVAGLKLQGGRGKKELDEIAERSLKGANLwnevKDRL-----------DKpggglsggqqQ 155
Cdd:COG4778 95 IGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNL----PERLwdlppatfsggEQ----------Q 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFT-IVIVTHNMQQAARVSDQT 217
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVADRV 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-180 |
3.51e-17 |
|
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: 80.77 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 21 SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGArveGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTm 100
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLL--LGFETPES---GSVFYDGQDL--AGLDVQAVRRQLGVVLQNGRLMSG- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 101 SIRDNVVAGLKLQggrgkkeLDEiAERSLKGANLWNEVKDR-------LDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:TIGR03797 542 SIFENIAGGAPLT-------LDE-AWEAARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQRLLIARALVRKPRILLFD 613
|
....*..
gi 694049011 174 EPCSALD 180
Cdd:TIGR03797 614 EATSALD 620
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-245 |
4.72e-17 |
|
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: 80.23 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGaRVEGSVLLDGEDIYGSGVD 79
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG-EVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVG-VRRTIGMVFQRPNPFPTMSIRDNVVAGLKLqggrgkkEL-DEIAER----SLKGANLWNE-VKDRLDKPGGGLSGG 152
Cdd:TIGR03269 359 GRGrAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-------ELpDELARMkaviTLKMVGFDEEkAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 153 QQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLI----QELKQDFtiVIVTHNMQQAARVSDQTGFFnleatgKP 228
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTF--IIVSHDMDFVLDVCDRAALM------RD 503
|
250
....*....|....*..
gi 694049011 229 GKLIEIDDTEKIFSNPT 245
Cdd:TIGR03269 504 GKIVKIGDPEEIVEELT 520
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-244 |
5.53e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.85 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSgvDPVGV---RRTIGMVFQrp 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT-----GGELYYQGQDLLKA--DPEAQkllRQKIQIVFQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPF----PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLdkPGGGLSGGQQqRLCIARAIAVSPDVL 170
Cdd:PRK11308 100 NPYgslnPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY--PHMFSGGQRQ-RIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 171 LMDEPCSALDpISTLA-IEDLIQELKQDFTI--VIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKIFSNP 244
Cdd:PRK11308 177 VADEPVSALD-VSVQAqVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYL------GRCVEKGTKEQIFNNP 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-217 |
5.79e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 24 TLAVPPRSVTAFIGPSGCGKSTVLrslNRMHEVTPGARveGSVLLDGEDIYGSGVDpvgvRRTIGMVFQRPNPFPTMSIR 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL---NLIAGFLTPAS--GSLTLNGQDHTTTPPS----RRPVSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 104 DNVV----AGLKLQGGRgKKELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSAL 179
Cdd:PRK10771 90 QNIGlglnPGLKLNAAQ-REKLHAIARQM--------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 694049011 180 DPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQT 217
Cdd:PRK10771 161 DPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARIAPRS 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-216 |
1.01e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.73 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIygSGVDPVGVR 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTPTA---GTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGR--GKKELDEIA-ERSLKGAnlwnEVKDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:PRK09536 77 RRVASVPQDTSLSFEFDVRQVVEMGRTPHRSRfdTWTETDRAAvERAMERT----GVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 162 AIAVSPDVLLMDEPCSALD---PISTLAiedLIQELKQD-FTIVIVTHNMQQAARVSDQ 216
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDinhQVRTLE---LVRRLVDDgKTAVAAIHDLDLAARYCDE 208
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-206 |
1.36e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.61 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGarvEGSVLLDGEDIYGsgvDPVGVR--RTIGMVF 91
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI--VGLVKPD---SGRIFLDGEDITH---LPMHKRarLGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwNEVKD-----------RldkpggglsggqqqRLCIA 160
Cdd:COG1137 85 QEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGI-THLRKskayslsggerR--------------RVEIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHN 206
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKErGIGVLITDHN 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-205 |
2.52e-16 |
|
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: 77.83 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDpvGVRRTIGMVFQRPNPFP 98
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-----SGQILLDGHDLADYTLA--SLRRQVALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TmSIRDNVVAGlklqggRGKKELDEIAERSLKGANLwNEVKDRLDKPGGGLSGGQQQ--------RLCIARAIAVSPDVL 170
Cdd:TIGR02203 420 D-TIANNIAYG------RTEQADRAEIERALAAAYA-QDFVDKLPLGLDTPIGENGVllsggqrqRLAIARALLKDAPIL 491
|
170 180 190
....*....|....*....|....*....|....*
gi 694049011 171 LMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-207 |
2.79e-16 |
|
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: 75.60 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRpNPFP 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDL--ALADPAWLRRQVGVVLQE-NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGlklQGGRGKKELDEIAerSLKGANLW-NEVKDRLD----KPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:cd03252 89 NRSIRDNIALA---DPGMSMERVIEAA--KLAGAHDFiSELPEGYDtivgEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190
....*....|....*....|....*....|....
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDFTIVIVTHNM 207
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRL 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-215 |
2.82e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 76.38 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 12 IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVDPVgvRRTIGMVF 91
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPTS---GSVLIRGEPITKENIREV--RKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNP--FPTMSIRDNVVAGLKLQggrgkkeLDE--IAERSLKGANLWNeVKDRLDKPGGGLSGGQQQRLCIARAIAVSP 167
Cdd:PRK13652 85 QNPDDqiFSPTVEQDIAFGPINLG-------LDEetVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 694049011 168 DVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSD 215
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMAD 206
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-233 |
4.59e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGSGVdpvGVR 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM--TSPDA---GKITVLGVPVPARAR---LAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDN-VVAGLKLqgGRGKKELDEIAERSLKGANLWNEVkdrlDKPGGGLSGGQQQRLCIARAI 163
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENlLVFGRYF--GMSTREIEAVIPSLLEFARLESKA----DARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 164 AVSPDVLLMDEPCSALDPISTLAI-EDLIQELKQDFTIVIVTHNMQQAARVSDQTGFfnLE-----ATGKPGKLIE 233
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCV--LEagrkiAEGRPHALID 261
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-207 |
5.54e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRRTIGMVFQ-RPNPF 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-----QGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQdSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 -PTMSIRDNVVAGLklqggRGKKELDEiAERSLKGANLWNEVKDR---LDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:PRK10419 103 nPRKTVREIIREPL-----RHLLSLDK-AERLARASEMLRAVDLDdsvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNM 207
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDL 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-243 |
8.30e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGK-----FHAVSDVTLAVPPRSVTAFIGPSGCGKSTvlrslnrMHEVTPGARVEGSvlldGEDIYGSGVDPV 81
Cdd:PRK13645 9 LDNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKST-------MIQLTNGLIISET----GQTIVGDYAIPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GV---------RRTIGMVFQRPN-PFPTMSIRDNVVAGlKLQGGRGKKELDEIAERSLKGANLwneVKDRLDKPGGGLSG 151
Cdd:PRK13645 78 NLkkikevkrlRKEIGLVFQFPEyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 152 GQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFT--IVIVTHNMQQAARVSDQTGFFNleatgkPG 229
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMH------EG 227
|
250
....*....|....
gi 694049011 230 KLIEIDDTEKIFSN 243
Cdd:PRK13645 228 KVISIGSPFEIFSN 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-245 |
2.18e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.38 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGARVEGSVLLDGEDIYGSGVDP 80
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRT--IGMVFQRP----NPFptMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRLDKPGGGLSGGQQ 154
Cdd:PRK09473 91 LNKLRAeqISMIFQDPmtslNPY--MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 QRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQTgfFNLEAtgkpGKLI 232
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKV--LVMYA----GRTM 241
|
250
....*....|...
gi 694049011 233 EIDDTEKIFSNPT 245
Cdd:PRK09473 242 EYGNARDVFYQPS 254
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-205 |
2.20e-15 |
|
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: 75.24 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTmS 101
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-----SGRILIDGQDI--RDVTQASLRAAIGIVPQDTVLFND-T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 102 IRDN------------VVA-------------------------GLKLQGGrgkkeldeiaERSlkganlwnevkdrldk 144
Cdd:COG5265 448 IAYNiaygrpdaseeeVEAaaraaqihdfieslpdgydtrvgerGLKLSGG----------EKQ---------------- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 145 pggglsggqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:COG5265 502 -----------RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-244 |
2.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYG--SGVDPVGVRRTIGMVFQrpnpFPT 99
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPSS---GTITIAGYHITPetGNKNLKKLRKKVSLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVagLK------LQGGRGKKELDEIAERSLKGANLWNEVkdrLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:PRK13641 96 AQLFENTV--LKdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 174 EPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTgfFNLEAtgkpGKLIEIDDTEKIFSNP 244
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDV--LVLEH----GKLIKHASPKEIFSDK 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-211 |
2.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYY-----GKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPgarVEGSVLLDGEDIY 74
Cdd:PRK13633 1 MNEMIKCKNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 75 GSGvDPVGVRRTIGMVFQRPNPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLWnEVKDRldkPGGGLSGGQQ 154
Cdd:PRK13633 76 DEE-NLWDIRNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMY-EYRRH---APHLLSGGQK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 155 QRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAA 211
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAV 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-210 |
3.86e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.81 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK-----FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSgvd 79
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-----SGSILIDGKDVTKL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVGVR-RTIGMVFQrpNPF----PTMSIRDN-VVAGLK-----LQGGRGKKELDEIAERsLKGANLWNEvkDRLDKPGGG 148
Cdd:COG1101 74 PEYKRaKYIGRVFQ--DPMmgtaPSMTIEENlALAYRRgkrrgLRRGLTKKRRELFREL-LATLGLGLE--NRLDTKVGL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 149 lsggqqqrL------CIARAIAV--SPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQA 210
Cdd:COG1101 149 --------LsggqrqALSLLMATltKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQA 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
4.29e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:PRK13648 8 IVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-----SGEIFYNNQAI--TDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRP-NPFPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWnevkDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:PRK13648 81 LRKHIGIVFQNPdNQFVGSIVKYDVAFGLENHA-VPYDEMHRRVSEALKQVDML----ERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARvSDQTGFFNLEATGKPGKLIEIDDTEK 239
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-216 |
4.46e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.16 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVR-RTIGMVFQRPNPFPT 99
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT-----SGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLkLQGGRGKKELDEIAERSLKGANLWNEVKDRldkpGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSAL 179
Cdd:PRK11629 102 FTALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHR----PSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 694049011 180 DPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQ 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-205 |
5.19e-15 |
|
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: 71.76 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFp 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDI--SKIGLHDLRSRISIIPQDPVLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVvaglklqGGRGKKELDEIaERSLKGANLWNEVKDRLDKPGGGLSGGQQQ-----R--LCIARAIAVSPDVLL 171
Cdd:cd03244 91 SGTIRSNL-------DPFGEYSDEEL-WQALERVGLKEFVESLPGGLDTVVEEGGENlsvgqRqlLCLARALLRKSKILV 162
|
170 180 190
....*....|....*....|....*....|....
gi 694049011 172 MDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-240 |
5.20e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 3 KRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPG-ARVEGSV--LLDgediYGSGVD 79
Cdd:COG1134 25 KELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrVEVNGRVsaLLE----LGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 pvgvrrtigmvfqrpnpfPTMSIRDNVvaglKLQG---GRGKKE----LDEIAERSlkganlwnEVKDRLDKPGGGLSGG 152
Cdd:COG1134 101 ------------------PELTGRENI----YLNGrllGLSRKEidekFDEIVEFA--------ELGDFIDQPVKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 153 QQQRLCIARAIAVSPDVLLMDEpcsaldpisTLAI---------EDLIQELKQDF-TIVIVTHNMQQAARVSDQtgFFNL 222
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDE---------VLAVgdaafqkkcLARIRELRESGrTVIFVSHSMGAVRRLCDR--AIWL 219
|
250
....*....|....*...
gi 694049011 223 EAtgkpGKLIEIDDTEKI 240
Cdd:COG1134 220 EK----GRLVMDGDPEEV 233
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-206 |
1.05e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLNGQPI--ADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTmSIRDNVVAGL------KLQGGRGKKELDEIAErSLKGANLW----------NEVKdrldkpg 146
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNLLLAApnasdeALIEVLQQVGLEKLLE-DDKGLNAWlgeggrqlsgGEQR------- 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 147 gglsggqqqRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHN 206
Cdd:PRK11160 483 ---------RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHR 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
1.06e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGE--DIYGSGv 78
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-----SGEILIDGKpvRIRSPR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 dpVGVRRTIGMVFQRPNPFPTMSIRDNVVAGL-KLQGGRG-----KKELDEIAER-SLKgANLWNEVKD-------RLDk 144
Cdd:COG3845 76 --DAIALGIGMVHQHFMLVPNLTVAENIVLGLePTKGGRLdrkaaRARIRELSERyGLD-VDPDAKVEDlsvgeqqRVE- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 145 pggglsggqqqrlcIARAIAVSPDVLLMDEPCSALDPistLAIEDLIQELK----QDFTIVIVTHNMQQAARVSD 215
Cdd:COG3845 152 --------------ILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIAD 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-212 |
1.73e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG---VR-RTIGMVFQRPNPFP 98
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-----SGEVSLVGQPL--HQMDEEArakLRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGLKLQGGRGKKELDEIAERsLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSA 178
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKAL-LEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 694049011 179 LDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAAR 212
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-235 |
2.18e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.25 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYgsgvdPVGvrrtIGMVFQr 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-----SGTVTVRGRVSS-----LLG----LGGGFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 pnpfPTMSIRDNVVAGLKLQGGRGK---KELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVL 170
Cdd:cd03220 97 ----PELTGRENIYLNGRLLGLSRKeidEKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694049011 171 LMDEPCSALDPISTLAIEDLIQELKQDFTIVI-VTHNMQQAARVSDQtgFFNLEAtgkpGKLIEID 235
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDR--ALVLEK----GKIRFDG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-243 |
2.36e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.79 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgvRRTIGMVFQRP-NPF 97
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-----SGEIKIDGITISKENLKEI--RKKIGIIFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGL---KLQGGRGKKELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDE 174
Cdd:PRK13632 97 IGATVEDDIAFGLenkKVPPKKMKDIIDDLAKKV--------GMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 175 PCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARvSDQTGFFNleatgkPGKLIEIDDTEKIFSN 243
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAIL-ADKVIVFS------EGKLIAQGKPKEILNN 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-250 |
3.38e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.68 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGS--VLLDGEDI 73
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyRVAGQdvATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 74 ygsgvdpVGVRRT-IGMVFQRPNPFPTMSIRDNVVAGlKLQGGRGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGG 152
Cdd:PRK10535 81 -------AQLRREhFGFIFQRYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGL----EDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 153 QQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSdqtgffnleatgkpgKL 231
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAE---------------RV 213
|
250
....*....|....*....
gi 694049011 232 IEIDDTEKIFSNPTQKATE 250
Cdd:PRK10535 214 IEIRDGEIVRNPPAQEKVN 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-216 |
3.47e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmHEVTPGArveGSVLLDGEDIygSGVDPVGVR 84
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPDS---GEVRLNGRPL--ADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPN---PFptmSIRDnVVA-GLkLQGGRGKKELDEIAERSLKGANLWnEVKDRL-------DKpggglsggq 153
Cdd:PRK13548 76 RRRAVLPQHSSlsfPF---TVEE-VVAmGR-APHGLSRAEDDALVAAALAQVDLA-HLAGRDypqlsggEQ--------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 154 qQRLCIARAIA------VSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:PRK13548 141 -QRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADR 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-244 |
7.89e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTMSI 102
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPL--ESWSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNVVAG-------LKLQGGRGKKELDE-IAERSLKgaNLWNEVKDRLDkpggglsGGQQQRLCIARAIAVSPDVLLMDE 174
Cdd:PRK10575 103 RELVAIGrypwhgaLGRFGAADREKVEEaISLVGLK--PLAHRLVDSLS-------GGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 175 PCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSD-----QTGffNLEATGKPGKLIEIDDTEKIFSNP 244
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINMAARYCDylvalRGG--EMIAQGTPAELMRGETLEQIYGIP 248
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-212 |
9.64e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 67.64 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLrslnrmhEVTPGAR--VEGSVLLDGEDIYG-----SGVD---PVGV 83
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLL-------KVLAGVLrpTSGTVRRAGGARVAyvpqrSEVPdslPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGM-VFQRPNPFPTMSIRDNVVAGLKLQggR-GKKELDEIAERSLKGANLwnevkdrldkpggglsggqqQRLCIAR 161
Cdd:NF040873 75 RDLVAMgRWARRGLWRRLTRDDRAAVDDALE--RvGLADLAGRQLGELSGGQR--------------------QRALLAQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAAR 212
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRR 184
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-206 |
1.03e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT-----SGTLLFEGEDI--STLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTmSIRDNVVAGLKLqggRGKKELDEIAERSLKGANLWNEVkdrLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQI---RNQQPDPAIFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVI--VTHN 206
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-208 |
1.19e-13 |
|
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: 67.49 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 21 SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTpgaRVEGSVLLDGediygsgvdpvgvrrTIGMVFQrpNPF-PT 99
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSVSVPG---------------SIAYVSQ--EPWiQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKELD-----------------EIAErslKGANLWNEVKdrldkpggglsggqqQRLCIARA 162
Cdd:cd03250 80 GTIRENILFGKPFDEERYEKVIKacalepdleilpdgdltEIGE---KGINLSGGQK---------------QRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694049011 163 IAVSPDVLLMDEPCSALDP-ISTLAIEDLIQ-ELKQDFTIVIVTHNMQ 208
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQ 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-216 |
1.36e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.19 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 6 DLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDiygsgvdpvgVRR 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLD----------VAT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 86 TIGMVFQRpnpfpTMSI--RDNVVAgLKL-------------QGGRGKKELDEIAERSLKGANLwNEVKDR-LD------ 143
Cdd:COG4604 68 TPSRELAK-----RLAIlrQENHIN-SRLtvrelvafgrfpySKGRLTAEDREIIDEAIAYLDL-EDLADRyLDelsggq 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 144 KpggglsggqqQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSDQ 216
Cdd:COG4604 141 R----------QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADH 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-243 |
2.12e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 17 FHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRM-------------HEVTPGARVEGSVLLDGEDIYGSGVDPV-- 81
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIQKTRFKKIkk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 --GVRRTIGMVFQrpnpFPTM-----SIRDNVVAGlKLQGGRGKKELDEIAERSLKGANLWNEVkdrLDKPGGGLSGGQQ 154
Cdd:PRK13651 100 ikEIRRRVGVVFQ----FAEYqlfeqTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESY---LQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 QRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFFnleatgKPGKLIE 233
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFF------KDGKIIK 245
|
250
....*....|
gi 694049011 234 IDDTEKIFSN 243
Cdd:PRK13651 246 DGDTYDILSD 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-245 |
2.81e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 16 KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGA-RVEGSVLLDGEDIYGSGVDPVG--------VRRT 86
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiQVGDIYIGDKKNNHELITNPYSkkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 87 IGMVFQRP--NPFPTMSIRDNVVAGLKLqgGRGKKELDEIAERSLKGANLwneVKDRLDKPGGGLSGGQQQRLCIARAIA 164
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVAL--GVKKSEAKKLAKFYLNKMGL---DDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSN 243
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMD------KGKILKTGTPYEIFTD 266
|
..
gi 694049011 244 PT 245
Cdd:PRK13631 267 QH 268
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-206 |
4.30e-13 |
|
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: 66.01 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSL--NRMHEVTpgarvEGSVLLDGEDIYGSGVDpVG 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVT-----EGEILFKGEDITDLPPE-ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPNPFPTMSIRD---NVVAGlkLQGGRGKKeldeiaerslkganlwNEvkdrldkpggglsggqqqrlcI 159
Cdd:cd03217 75 ARLGIFLAFQYPPEIPGVKNADflrYVNEG--FSGGEKKR----------------NE---------------------I 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHN 206
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHY 163
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-205 |
4.81e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.12 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY-GKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI--YGSGvdp 80
Cdd:PRK11176 342 IEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDLrdYTLA--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 vGVRRTIGMVFQRPNPFPTmSIRDNVVAGLKLQGGRgkkelDEIaERSLKGA---NLWNEVKDRLD----KPGGGLSGGQ 153
Cdd:PRK11176 414 -SLRNQVALVSQNVHLFND-TIANNIAYARTEQYSR-----EQI-EEAARMAyamDFINKMDNGLDtvigENGVLLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 694049011 154 QQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-250 |
5.59e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLLDGEDI-YGSGVDPVGVR-RTIGMVFQRP--- 94
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLlHASEQTLRGVRgNKIAMIFQEPmvs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 -NPFPTmsIRDNVVAGLKLQGGRGKKE--------LDEIAERSLKGanlwnevkdRLDKPGGGLSGGQQQRLCIARAIAV 165
Cdd:PRK15134 105 lNPLHT--LEKQLYEVLSLHRGMRREAargeilncLDRVGIRQAAK---------RLTDYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 166 SPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARVSDQTgffnleATGKPGKLIEIDDTEKIFSN 243
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRV------AVMQNGRCVEQNRAATLFSA 247
|
....*..
gi 694049011 244 PTQKATE 250
Cdd:PRK15134 248 PTHPYTQ 254
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-228 |
9.69e-13 |
|
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: 67.73 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYgSGVDpvGVRRTIGMVFQRPNPFP 98
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-----SGTVLVGGKDIE-TNLD--AVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLWNevkdRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSA 178
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKG-RSWEEAQLEMEAMLEDTGLHH----KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 179 LDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVSDQTGFFN---LEATGKP 228
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISqgrLYCSGTP 1144
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-213 |
1.13e-12 |
|
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: 67.46 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYG-KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVGV 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-----SGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 RRTIGMVFQRPNPFpTMSIRDNVVAGLKlqGGRGKKELD---EIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIA 160
Cdd:TIGR01193 547 RQFINYLPQEPYIF-SGSILENLLLGAK--ENVSQDEIWaacEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELkQDFTIVIVTHNMQQAARV 213
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQS 675
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-250 |
1.16e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYY----GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGARVEGSVLL---DGEDIYGSG 77
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 VDPVGVRRT----IGMVFQRP--NPFPTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRLDKPGGGLSG 151
Cdd:PRK10261 93 QSAAQMRHVrgadMAMIFQEPmtSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 152 GQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFT--IVIVTHNMQQAARVSDQTGFFNleatgkPG 229
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMY------QG 245
|
250 260
....*....|....*....|.
gi 694049011 230 KLIEIDDTEKIFSNPTQKATE 250
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYTR 266
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-215 |
1.52e-12 |
|
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: 65.05 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPG-ARVEGSVLLDGEDIYgsgvdpvgvRRTIGMVF-QRPNP 96
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGeVRVAGLVPWKRRKKF---------LRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRD--NVVAGL-KLQGGRGKKELDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:cd03267 107 WWDLPVIDsfYLLAAIyDLPPARFKKRLDELSELL--------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQQAARVSD 215
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALAR 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-231 |
1.92e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGarvEGSVLLDGEDIYGSGVDPVGVRRTIGMVFQRPNP--FPTm 100
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQqiFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 101 SIRDNVVAGLKlqgGRGKKElDEIAERSLKGANLWNEVKDRlDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALD 180
Cdd:PRK13638 94 DIDSDIAFSLR---NLGVPE-AEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 181 PISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQTGFF---NLEATGKPGKL 231
Cdd:PRK13638 169 PAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLrqgQILTHGAPGEV 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-254 |
2.24e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYG-SGVDPVGVRRTIGMVFQRP--- 94
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDPlas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 -NPfpTMSIRDNVVAGLKLQGGRGKKEldEIAERslkganlwneVKDRLDK----PGGGL------SGGQQQRLCIARAI 163
Cdd:PRK15079 111 lNP--RMTIGEIIAEPLRTYHPKLSRQ--EVKDR----------VKAMMLKvgllPNLINryphefSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 164 AVSPDVLLMDEPCSALDpISTLA-IEDLIQELKQD--FTIVIVTHNMQQAARVSDQTGFFNLeatgkpGKLIEIDDTEKI 240
Cdd:PRK15079 177 ILEPKLIICDEPVSALD-VSIQAqVVNLLQQLQREmgLSLIFIAHDLAVVKHISDRVLVMYL------GHAVELGTYDEV 249
|
250
....*....|....
gi 694049011 241 FSNPTQKATEDYIS 254
Cdd:PRK15079 250 YHNPLHPYTKALMS 263
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-205 |
3.81e-12 |
|
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: 65.74 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDG---EDIygsgvdPVGV-RRTIGMVFQRPN 95
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW-----SGEILFDGiprEEI------PREVlANSVAMVDQDIF 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 96 PFPTmSIRDNVV--------AGLkLQGGRGKKELDEIAERSLK--------GANLwnevkdrldkpggglSGGQQQRLCI 159
Cdd:TIGR03796 564 LFEG-TVRDNLTlwdptipdADL-VRACKDAAIHDVITSRPGGydaelaegGANL---------------SGGQRQRLEI 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQelKQDFTIVIVTH 205
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAH 670
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-207 |
5.19e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRmhEVTPGArveGSVLLDGEDiyGSGVDPVGV- 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDA---GEVHYRMRD--GQLRDLYALs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 84 ---RRTI-----GMVFQRPnpfpTMSIRDNVVAG------LKLQGGRGKKELDEIAERSLKganlwnEVK---DRLDKPG 146
Cdd:PRK11701 80 eaeRRRLlrtewGFVHQHP----RDGLRMQVSAGgnigerLMAVGARHYGDIRATAGDWLE------RVEidaARIDDLP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 147 GGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDpISTLA-IEDLIQELKQDF--TIVIVTHNM 207
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGLVRELglAVVIVTHDL 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-205 |
5.34e-12 |
|
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: 61.70 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmhevtpgarvegsvlldGEDIYGSGVDPVGVR 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA------------------GELEPDEGIVTWGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMvfqrpnpFPTMSirdnvvaglklqGGrgkkeldeiaERSlkganlwnevkdrldkpggglsggqqqRLCIARAIA 164
Cdd:cd03221 63 VKIGY-------FEQLS------------GG----------EKM---------------------------RLALAKLLL 86
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQdfTIVIVTH 205
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-212 |
1.12e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRM--HEVTPGARVEgsvlLDGEDIYGSGVDPVGVRRT---IGMVFQR 93
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIE----LLGRTVQREGRLARDIRKSranTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVvaglkLQGGRG------------KKELDEIAERSLKGANLWNEVKDRLDkpggGLSGGQQQRLCIAR 161
Cdd:PRK09984 95 FNLVNRLSVLENV-----LIGALGstpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVS----TLSGGQQQRVAIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAAR 212
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-212 |
1.87e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 13 YYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtPGArveGSVLLDGEDIYGSGVDPVG-VRRTIGMVF 91
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIER--PSA---GKIWFSGHDITRLKNREVPfLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNPFPTMSIRDNVVAGLKLQGGRGkkelDEIAER---SLKGANLWNEVKDRldkpGGGLSGGQQQRLCIARAIAVSPD 168
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASG----DDIRRRvsaALDKVGLLDKAKNF----PIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 169 VLLMDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAAR 212
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-204 |
2.03e-11 |
|
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: 61.90 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGARVEGSVLLDGEDiygsgVDPVGVRRTIGMVFQRPNPFPT 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNGQP-----RKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKE-----------LDEIAERSLKGANLWN----EVKdrldkpggglsggqqqRLCIARAIA 164
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDairkkrvedvlLRDLALTRIGGNLVKGisggERR----------------RVSIAVQLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVT 204
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-244 |
2.51e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKST---VLRSLNRMHEvtpGA-RVEGSVLLDGEdiygSGVD-PVGVRRtIGMVFQRPNP 96
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSlinAISGLTRPQK---GRiVLNGRVLFDAE----KGIClPPEKRR-IGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDNVVAGLKlqgGRGKKELDEIAE------------RSLKGAnlwnevkdrlDKpggglsggqqQRLCIARAIA 164
Cdd:PRK11144 88 FPHYKVRGNLRYGMA---KSMVAQFDKIVAllgieplldrypGSLSGG----------EK----------QRVAIGRALL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVI--VTHNMQQAARVSDQTGFfnLEAtgkpGKLIEIDDTEKIFS 242
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPIlyVSHSLDEILRLADRVVV--LEQ----GKVKAFGPLEEVWA 218
|
..
gi 694049011 243 NP 244
Cdd:PRK11144 219 SS 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-205 |
3.29e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRslnrmhevtpgarvegsvLLDGEDIYGSGVdpVGVRR- 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLK------------------ILAGELEPDSGE--VSIPKg 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 86 -TIGMVFQRPNPFPTMSIRDNVVAGLK-------------LQGGRGKKELDEIAERS--LKGANLWN------EVKDRLD 143
Cdd:COG0488 61 lRIGYLPQEPPLDDDLTVLDTVLDGDAelraleaeleeleAKLAEPDEDLERLAELQeeFEALGGWEaearaeEILSGLG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 144 KPGGGLSGGQQQ-------RLCIARAIAVSPDVLLMDEPCSALDpistL-AIEDLIQELKQ-DFTIVIVTH 205
Cdd:COG0488 141 FPEEDLDRPVSElsggwrrRVALARALLSEPDLLLLDEPTNHLD----LeSIEWLEEFLKNyPGTVLVVSH 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-215 |
4.52e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevtPGARVEGSVLLDGEDIYGSGVDPVGvR 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY---PHGTWDGEIYWSGSPLKASNIRDTE-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPNPFPTMSIRDNVVAG--LKLQGGRGkkeldEIAERSLKGANLWNEVK---DRLDKPGGGLSGGQQQRLCI 159
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGneITLPGGRM-----AYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ-DFTIVIVTHNMQQAARVSD 215
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCD 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-215 |
4.92e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSL--NRMHEVTP-GARVEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFP 98
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPrGARVTGDVTLNGEPL--AAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVVAGL---KLQGGRGKKELDEIAERSLKGANlwnevKDRLD-KPGGGLSGGQQQRLCIARAIA---------V 165
Cdd:PRK13547 97 AFSAREIVLLGRyphARRAGALTHRDGEIAWQALALAG-----ATALVgRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 694049011 166 SPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVT--HNMQQAARVSD 215
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHAD 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-206 |
4.94e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.85 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSL--NRMHEVTpgarvEGSVLLDGEDIYGSGVDPVgVRRTIGMVFQRPNPFPT 99
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVT-----SGSILLDGEDILELSPDER-ARAGIFLAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRD------NVVAGLKLQGGRGKKELDEIAE----------RSLkganlwN------EVKdrldkpggglsggqqqRL 157
Cdd:COG0396 92 VSVSNflrtalNARRGEELSAREFLKLLKEKMKelgldedfldRYV------NegfsggEKK----------------RN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 158 CIARAIAVSPDVLLMDEPCSALDpISTLAI-EDLIQELK-QDFTIVIVTHN 206
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLD-IDALRIvAEGVNKLRsPDRGILIITHY 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
5.32e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgarvegsvlLDGEDIYGSGVdpvgvr 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEP---------DSGTVKLGETV------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 rTIGMVFQRPNPF-PTMSIRDNVVaglklqggRGKKELDEIAERSL------KGANLWNEVKD-----Rldkpggglsgg 152
Cdd:COG0488 379 -KIGYFDQHQEELdPDKTVLDELR--------DGAPGGTEQEVRGYlgrflfSGDDAFKPVGVlsggeK----------- 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 153 qqQRLCIARAIAVSPDVLLMDEPCSALDpISTL-AIEDLIqelkQDF--TIVIVTHNMQQAARVSDQT 217
Cdd:COG0488 439 --ARLALAKLLLSPPNVLLLDEPTNHLD-IETLeALEEAL----DDFpgTVLLVSHDRYFLDRVATRI 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
5.92e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDiYGSGVDP 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-----KGTITINNIN-YNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRRTIGMVFQRPNPFPTMSIRDNVVAGlklqggrgkkeldEIAERSLKGANL--WNEVKDR-------------LDKP 145
Cdd:PRK09700 76 LAAQLGIGIIYQELSVIDELTVLENLYIG-------------RHLTKKVCGVNIidWREMRVRaammllrvglkvdLDEK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 146 GGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFT-IVIVTHNMQQAARVSDQ 216
Cdd:PRK09700 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDR 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-205 |
1.42e-10 |
|
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: 60.92 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDPVGvrRTIGMVFQRPNPFPT 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT-----AGSVRLDGADLSQWDREELG--RHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 mSIRDN-----------VV-----AG-----LKLQGGrgkkeLD-EIAERslkGANLwnevkdrldkpggglsggqqqRL 157
Cdd:COG4618 421 -TIAENiarfgdadpekVVaaaklAGvhemiLRLPDG-----YDtRIGEG---GARLsgg---------------qrqRI 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 158 CIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTH 205
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITH 525
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-216 |
2.01e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRmhEVTPGarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQRPN---PFptmSIRDnVVA-GLkLQGGRGKKELDEIAERSLKGANLWnEVKDRL-------DKpggglsggq 153
Cdd:COG4559 75 RRRAVLPQHSSlafPF---TVEE-VVAlGR-APHGSSAAQDRQIVREALALVGLA-HLAGRSyqtlsggEQ--------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694049011 154 qQRLCIARAIA-------VSPDVLLMDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQAARVSDQ 216
Cdd:COG4559 140 -QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADR 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-247 |
2.29e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 59.62 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIyGSGVDPVGVRRTIGMVFQRPNP-F 97
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQK---GKVLVSGIDT-GDFSKLQGIRKLVGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAG---LKLQGGRGKKELDE-IAERSLKganlwnevKDRLDKPGGGLSGGQQqrlCIARA--IAVSPDVLL 171
Cdd:PRK13644 91 VGRTVEEDLAFGpenLCLPPIEIRKRVDRaLAEIGLE--------KYRHRSPKTLSGGQGQ---CVALAgiLTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 172 MDEPCSALDPISTLAIEDLIQEL-KQDFTIVIVTHNMQQaARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPTQK 247
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMD------RGKIVLEGEPENVLSDVSLQ 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-249 |
3.97e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMhevtpgARVEGSVLLDGEDIYG-SGVDPVGVRRTIGMVFQRPNP 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 F--PTMSIRDNVVAGLKLQggrgKKELDEiAERSLKGANLWNEV----KDRLDKPGGGLSGGQQqRLCIARAIAVSPDVL 170
Cdd:PRK15134 374 SlnPRLNVLQIIEEGLRVH----QPTLSA-AQREQQVIAVMEEVgldpETRHRYPAEFSGGQRQ-RIAIARALILKPSLI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 171 LMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTGFFnleatgKPGKLIEIDDTEKIFSNPTQKA 248
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVL------RQGEVVEQGDCERVFAAPQQEY 521
|
.
gi 694049011 249 T 249
Cdd:PRK15134 522 T 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-236 |
4.29e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAV---SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEV------------------------ 56
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 57 -----------------TPGARVE--------GSVLLDGEDIYGSGVDpvGVRRTIGMVFQRPNPFpTMSIRDNVvaglk 111
Cdd:PTZ00265 1245 deeqnvgmknvnefsltKEGGSGEdstvfknsGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLF-NMSIYENI----- 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 112 lQGGRGKKELDEIaERSLKGA-------NLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPIST 184
Cdd:PTZ00265 1317 -KFGKEDATREDV-KRACKFAaidefieSLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 185 LAIEDLIQELKQ--DFTIVIVTHNMQQAARvSDQTGFFN--------LEATGKPGKLIEIDD 236
Cdd:PTZ00265 1395 KLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNnpdrtgsfVQAHGTHEELLSVQD 1455
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
5.15e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGArvegsvlldgediyGSGVDP 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAPDE--------------GVIKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 VGVRrtIGMVFQRPNPFPTMSIrdNVVAGLKLQGGRGKKELDEIAERsLKGANLwnevkdrLDKPGGGLSGGQQQRLCIA 160
Cdd:PRK09544 65 GKLR--IGYVPQKLYLDTTLPL--TVNRFLRLRPGTKKEDILPALKR-VQAGHL-------IDAPMQKLSGGETQRVLLA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNM 207
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-250 |
6.45e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGK----FHAVSDVTLAVPPRSVTAFIGPSGCGKStvLRSLNRMHEVT-PGARVEGSVLLDGEDIygSGVD 79
Cdd:PRK11022 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDyPGRVMAEKLEFNGQDL--QRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 80 PVGVRRTIG----MVFQRP----NPFPTMSIRdnVVAGLKLQGGRGKKEldeiaeRSLKGANLWNEV-----KDRLDKPG 146
Cdd:PRK11022 80 EKERRNLVGaevaMIFQDPmtslNPCYTVGFQ--IMEAIKVHQGGNKKT------RRQRAIDLLNQVgipdpASRLDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 147 GGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARVSDQTgffnleA 224
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKI------I 225
|
250 260
....*....|....*....|....*.
gi 694049011 225 TGKPGKLIEIDDTEKIFSNPTQKATE 250
Cdd:PRK11022 226 VMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-205 |
1.57e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAV-SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygSGVDPVG 82
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-----EGEIRLDGRPL--SSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 83 VRRTIGMVFQRPnpfptMSIRDNVVAGLKLqgGRgkkeldEIAE----RSLKGANLWNEVKD-------RLDKPGGGLSG 151
Cdd:PRK10790 413 LRQGVAMVQQDP-----VVLADTFLANVTL--GR------DISEeqvwQALETVQLAELARSlpdglytPLGEQGNNLSV 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 152 GQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-216 |
1.77e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLrslNRMHEVTPgarVEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTmSI 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLP---YQGSLKINGIEL--RELDPESWRKHLSWVGQNPQLPHG-TL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNVVAGlklqggrgKKEL-DEIAERSLKGANLWNEVKDR---LDKPGGGLSGGQQQ----RLCIARAIAVSPDVLLMDE 174
Cdd:PRK11174 440 RDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLpqgLDTPIGDQAAGLSVgqaqRLALARALLQPCQLLLLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 694049011 175 PCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAARVsDQ 216
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQ 552
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-215 |
2.35e-09 |
|
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: 55.13 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIygsGVDPVGVRRTIGMVF-----QR 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPV---TRRSPRDAIRAGIAYvpedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVVAGLKLQGGrgkkeldeiaerslkgaNLwnevkdrldkpggglsggqqQRLCIARAIAVSPDVLLMD 173
Cdd:cd03215 87 EGLVLDLSVAENIALSSLLSGG-----------------NQ--------------------QKVVLARWLARDPRVLILD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSD 215
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCD 172
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-254 |
2.62e-09 |
|
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: 55.99 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmHEVTPGARVEGSVLLDGEDIYGSGVDPVGVR 84
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPDHGTATYIMRSGAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTI----GMVFQRPnpfptmsiRDnvvaGLKLQ---GGRGKKELDEIAERSL----KGANLW-NEVK---DRLDKPGGGL 149
Cdd:TIGR02323 82 RLMrtewGFVHQNP--------RD----GLRMRvsaGANIGERLMAIGARHYgnirATAQDWlEEVEidpTRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 150 SGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTI--VIVTHNMQQAARVSDQTgffnleATGK 227
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRL------LVMQ 223
|
250 260
....*....|....*....|....*..
gi 694049011 228 PGKLIEIDDTEKIFSNPTQKATEDYIS 254
Cdd:TIGR02323 224 QGRVVESGLTDQVLDDPQHPYTQLLVS 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-194 |
3.33e-09 |
|
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: 54.94 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 9 DVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSL-NRMHevtpGARVEGSVLLDGEDIygsgvdPVGVRRTI 87
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKT----AGVITGEILINGRPL------DKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 88 GMVFQRPNPFPTMSIRdnvvaglklqggrgkkeldEIAERS--LKGANlwneVKDRldkpggglsggqqQRLCIARAIAV 165
Cdd:cd03232 82 GYVEQQDVHSPNLTVR-------------------EALRFSalLRGLS----VEQR-------------KRLTIGVELAA 125
|
170 180
....*....|....*....|....*....
gi 694049011 166 SPDVLLMDEPCSALDPISTLAIEDLIQEL 194
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-205 |
4.23e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 16 KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPgarVEGSVLLDGEDIY--GSGVDPVGVRRTIGMVFQR 93
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP---VAGCVDVPDNQFGreASLIDAIGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PN------------PFPTMSirdnvvaglklqggRGKKEldeiaerslkganlwnevkdrldkpggglsggqqqRLCIAR 161
Cdd:COG2401 119 LNavglsdavlwlrRFKELS--------------TGQKF-----------------------------------RFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 694049011 162 AIAVSPDVLLMDEPCSALDP----ISTLAIEDLIQELKQdfTIVIVTH 205
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRqtakRVARNLQKLARRAGI--TLVVATH 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-258 |
4.28e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI-YGsgvDPVGVRRTIGMVFQRPNPF 97
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-----SGELLIDDHPLhFG---DYSYRSQRIRMIFQDPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 --PTMSIRDNVVAGLKLQGGRGKKELDEIAERSLKGANLwneVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PRK15112 100 lnPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 176 CSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAARVSDQTGFFNleatgkPGKLIEIDDTEKIFSNPTQKATEDYI 253
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMH------QGEVVERGSTADVLASPLHELTKRLI 250
|
....*
gi 694049011 254 SGRFG 258
Cdd:PRK15112 251 AGHFG 255
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-208 |
5.29e-09 |
|
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: 55.03 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRS-LNRMHevtpgaRVEGSVLLDGEDIYGSGVDPVGVRRTIGMVFQRPNPFP 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAiLGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 -TMSIRDNVVAGLKLQGGRGKKELD-----------------EIAERslkGANLwnevkdrldkpggglSGGQQQRLCIA 160
Cdd:cd03290 91 lNATVEENITFGSPFNKQRYKAVTDacslqpdidllpfgdqtEIGER---GINL---------------SGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 161 RAIAVSPDVLLMDEPCSALD-PISTLAIEDLIQELKQD--FTIVIVTHNMQ 208
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-204 |
1.02e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.44 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGARVEGSVLLDGEDIygsgvDPVGVRRTIGMVFQRPNPF 97
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI-----DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRD--NVVAGLKLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKPGGGLSGG--QQQRLCIARAIAVSPDVLLMD 173
Cdd:TIGR00955 112 PTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSggERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|.
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDFTIVIVT 204
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-205 |
1.25e-08 |
|
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: 55.05 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 15 GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrmheVTPGARVEGSVLLDGEDIYGsgVDPVGVRRTIGMVFQRP 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----VGIWPPTSGSVRLDGADLKQ--WDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 95 NPFPTmSIRDN------------VVAGLKLQGGRgkkEL---------DEIAERslkGANLwnevkdrldkpggglSGGQ 153
Cdd:TIGR01842 402 ELFPG-TVAENiarfgenadpekIIEAAKLAGVH---ELilrlpdgydTVIGPG---GATL---------------SGGQ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 154 QQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTH 205
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITH 512
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-209 |
1.75e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevtpgARVEGSVLLDGEDIYGSGvdPVGVRRT-IGMVFQRPNPF 97
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-----TRDAGSILYLGKEVTFNG--PKSSQEAgIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGLKLQGGRGK---KELDEIAERSLKGANlwneVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDE 174
Cdd:PRK10762 92 PQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLN----LRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 694049011 175 PCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQ 209
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELKsQGRGIVYISHRLKE 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-212 |
2.45e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 7 LKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLrSLnrmhevTPGARV--EGSVLLDGEDIYGSgvdpvGVR 84
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SL------IAGARKiqQGRVEVLGGDMADA-----RHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIG-----MvfqrP-----NPFPTMSIRDNV--VAGLKlqgGRGKKE-------------LDEIAERS---LKGAnlwn 136
Cdd:NF033858 72 RAVCpriayM----PqglgkNLYPTLSVFENLdfFGRLF---GQDAAErrrridellratgLAPFADRPagkLSGG---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 137 eVKDRLDkpggglsggqqqrLCIarAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD---FTIVIVTHNMQQAAR 212
Cdd:NF033858 141 -MKQKLG-------------LCC--ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-205 |
4.57e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 2 AKRLDLKDVNIYYGKFHA-VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmhevtpgarvegsvlldgeDI--YGSG- 77
Cdd:COG4178 360 DGALALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA--------------------GLwpYGSGr 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 VD-PVGVRrtigMVF--QRPNpFPTMSIRDNVVaglkLQGGRGKKELDEIAErSLKGANLwNEVKDRLDkpggglsgGQQ 154
Cdd:COG4178 420 IArPAGAR----VLFlpQRPY-LPLGTLREALL----YPATAEAFSDAELRE-ALEAVGL-GHLAERLD--------EEA 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694049011 155 Q-----------RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:COG4178 481 DwdqvlslgeqqRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-208 |
2.00e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.86 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIYGsgvDPVGVRRTIGMVF-QRPNP 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPTS---GEVRVLGYVPFK---RRKEFARRIGVVFgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDNvvagLKLQG-------GRGKKELDEIAERsLkganlwnEVKDRLDKPggglsggqQQRL-------C-IAR 161
Cdd:COG4586 108 WWDLPAIDS----FRLLKaiyripdAEYKKRLDELVEL-L-------DLGELLDTP--------VRQLslgqrmrCeLAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQDF--TIVIVTHNMQ 208
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-207 |
2.46e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 3 KRLDLKDVNIYYGKFHAVS---DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLL-DGEDIygSGV 78
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT-----EGDIIInDSHNL--KDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 79 DPVGVRRTIGMVFQRPNPFpTMSIRDNVVAGL-------------KLQGGRGKKELDEIAERSLKGANLWNEVKDRLDKP 145
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLF-SNSIKNNIKYSLyslkdlealsnyyNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSN 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 146 GGGLSGG--------------------------------------------QQQRLCIARAIAVSPDVLLMDEPCSALDP 181
Cdd:PTZ00265 533 ELIEMRKnyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnasklsggQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260
....*....|....*....|....*...
gi 694049011 182 ISTLAIEDLIQELK--QDFTIVIVTHNM 207
Cdd:PTZ00265 613 KSEYLVQKTINNLKgnENRITIIIAHRL 640
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-245 |
2.73e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVdpVGVRRTIGMVFQRPNPFpTMSI 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDVAKFGL--TDLRRVLSIIPQSPVLF-SGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNvvaglklqggrgkkeLDEIAERSlkGANLWN-----EVKDRLDKPG-----------GGLSGGQQQRLCIARAIAVS 166
Cdd:PLN03232 1327 RFN---------------IDPFSEHN--DADLWEaleraHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 167 PDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQaarVSDQTGFFNLEAtgkpGKLIEIDDTEKIFSNPT 245
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT---IIDCDKILVLSS----GQVLEYDSPQELLSRDT 1461
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-217 |
5.10e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 9 DVNIYYGKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGarvEGSVLldgediyGSGVDPVGVRRTI 87
Cdd:PRK15056 11 DVTVTWRNGHtALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG---KISIL-------GQPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 88 GMVFQRPN---PFPTMsIRDNVVAGLKLQGG---RGKKELDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIAR 161
Cdd:PRK15056 81 AYVPQSEEvdwSFPVL-VEDVVMMGRYGHMGwlrRAKKRDRQIVTAALARVDM----VEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 162 AIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQT 217
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYT 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-216 |
5.48e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.45 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIyygkFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLrslNRMHEVTPGarvEGSVLLDGEDIygSGVDPVGVR 84
Cdd:COG4138 1 LQLNDVAV----AGRLGPISAQVNAGELIHLIGPNGAGKSTLL---ARMAGLLPG---QGEILLNGRPL--SDWSAAELA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 85 RTIGMVFQR-PNPFP-------TMSIRDNVVAGLKlqggrgKKELDEIAERsLKganlwneVKDRLDKPGGGLSGGQQQR 156
Cdd:COG4138 69 RHRAYLSQQqSPPFAmpvfqylALHQPAGASSEAV------EQLLAQLAEA-LG-------LEDKLSRPLTQLSGGEWQR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 157 LCIARAIA-VSPDV------LLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQ 216
Cdd:COG4138 135 VRLAAVLLqVWPTInpegqlLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADR 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-212 |
7.43e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 14 YGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDiygsgVDP--VGVRRTIGMvf 91
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWLFGQP-----VDAgdIATRRRVGY-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 qrpnpfptMS----------IRDNVV--AGL-KLQGGRGKKELDEIAER-SLKganlwnEVKDRL--DKPggglsGGQQQ 155
Cdd:NF033858 344 --------MSqafslygeltVRQNLElhARLfHLPAAEIAARVAEMLERfDLA------DVADALpdSLP-----LGIRQ 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQAAR 212
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAER 463
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-205 |
8.33e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 12 IYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrmhevtpgARVEGSvlLDGEDIYGSGVdpvgvrrTIGMVF 91
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM---------AGVDKD--FNGEARPQPGI-------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 92 QRPNPFPTMSIRDNVVAGLKlQGGRGKKELDEIAER--------------------SLKGANLWN-----EVK-DRL--- 142
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVA-EIKDALDRFNEISAKyaepdadfdklaaeqaelqeIIDAADAWDldsqlEIAmDALrcp 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 143 --DKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQdfTIVIVTH 205
Cdd:TIGR03719 154 pwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-143 |
9.06e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 16 KFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtPGARVEGSVLLDGEDIYGSGVDPvgvRRTIGMVFQRPN 95
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE--GNVSVEGDIHYNGIPYKEFAEKY---PGEIIYVSEEDV 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 96 PFPTMSIRDNVVAGLKLQGG---RG-----KKELDeIAERSLKGAN--LWNEVKDRLD 143
Cdd:cd03233 94 HFPTLTVRETLDFALRCKGNefvRGisggeRKRVS-IAEALVSRASvlCWDNSTRGLD 150
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-216 |
1.07e-06 |
|
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: 49.03 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 5 LDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPgarVEGSVL----------------L 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 69 DGEDIYGSG-------VDPVG--------VRRTIGMVFQRPNP-FPTMSIRDNVVAGLKLQGGRGKKELDeiaerslKGA 132
Cdd:TIGR03269 78 VGEPCPVCGgtlepeeVDFWNlsdklrrrIRKRIAIMLQRTFAlYGDDTVLDNVLEALEEIGYEGKEAVG-------RAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 133 NLWNEVK--DRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQ 208
Cdd:TIGR03269 151 DLIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPE 230
|
....*...
gi 694049011 209 QAARVSDQ 216
Cdd:TIGR03269 231 VIEDLSDK 238
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-212 |
1.07e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 22 DVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDgediygsgvdpvgvrRTIGMVFQRP---NPfp 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-----EGRVWAE---------------RSIAYVPQQAwimNA-- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 tmSIRDNVV--------------------AGLKLQGGRGKKELDEiaerslKGANLWNEVKdrldkpggglsggqqQRLC 158
Cdd:PTZ00243 736 --TVRGNILffdeedaarladavrvsqleADLAQLGGGLETEIGE------KGVNLSGGQK---------------ARVS 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDP-ISTLAIEDLIQELKQDFTIVIVTHNMQQAAR 212
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPR 847
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-206 |
1.15e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 21 SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVtpgarVEGSVLLDGEDI----YGSGVDPVGVRrtigmvfqrpNP 96
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKLDGGDIddpdVAEACHYLGHR----------NA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 F-PTMSIRDNVVAGLKLQGGRgkkelDEIAERSLKGANLwnevKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PRK13539 84 MkPALTVAENLEFWAAFLGGE-----ELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 694049011 176 CSALDPISTLAIEDLIQE-LKQDFTIVIVTHN 206
Cdd:PRK13539 155 TAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
36-215 |
1.25e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 36 IGPSGCGKSTVLRSLNrmhevtpgarveGSVLLD-GEDIYGSGV-------DPVgvRRTIGMVFqrpnpfptmsirDNVV 107
Cdd:PRK11147 35 VGRNGAGKSTLMKILN------------GEVLLDdGRIIYEQDLivarlqqDPP--RNVEGTVY------------DFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 108 AGLKLQGGRGK------------------KELDEIAERsLKGANLW------NEVKDRL----DKPGGGLSGGQQQRLCI 159
Cdd:PRK11147 89 EGIEEQAEYLKryhdishlvetdpseknlNELAKLQEQ-LDHHNLWqlenriNEVLAQLgldpDAALSSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 160 ARAIAVSPDVLLMDEPCSALDpISTlaIEDLIQELKqDF--TIVIVTH------NMqqAARVSD 215
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLK-TFqgSIIFISHdrsfirNM--ATRIVD 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-207 |
1.74e-06 |
|
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: 48.79 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTpgaRVEGSVLLDGediygsgvdpvgvrrTIGMVFQRPnPFPTMSI 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---KVEGHVHMKG---------------SVAYVPQQA-WIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNVVAGLKLQGGRGKKELD-----------------EIAErslKGANLWNEVKDRldkpggglsggqqqrLCIARAIAV 165
Cdd:TIGR00957 716 RENILFGKALNEKYYQQVLEacallpdleilpsgdrtEIGE---KGVNLSGGQKQR---------------VSLARAVYS 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 694049011 166 SPDVLLMDEPCSALDP-ISTLAIEDLI--QELKQDFTIVIVTHNM 207
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGI 822
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-213 |
1.76e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSL-NRMHevtpGARVEGSVLLDGEDIYGSgvdpvgVRRTIGMVFQRPNPFP 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQ----GNNFTGTILANNRKPTKQ------ILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 TMSIRDNVV--AGLKLQGGRGKKELDEIAERSLKGANLW---NEVKDrlDKPGGGLSGGQQQRLCIARAIAVSPDVLLMD 173
Cdd:PLN03211 154 HLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTkceNTIIG--NSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 694049011 174 EPCSALDPISTLAIEDLIQELKQDFTiVIVTHNMQQAARV 213
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-212 |
3.17e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGArvegsVLLDGEDIYGSGVDPvgVRRTIGMVFQRPNPFPTmSI 102
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGE-----IRVNGREIGAYGLRE--LRRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDN-----------VVAGLKLQGGRGK--KELDEIAERSLKGANLWNEVKDRLdkpggglsggqqqrLCIARA-IAVSPD 168
Cdd:PTZ00243 1401 RQNvdpfleassaeVWAALELVGLRERvaSESEGIDSRVLEGGSNYSVGQRQL--------------MCMARAlLKKGSG 1466
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 694049011 169 VLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQAAR 212
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQ 1510
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-215 |
3.53e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDI-YGSGVDPVGVrrTIGMVFQRPNPF 97
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDGQEMrFASTTAALAA--GVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGlKLQGGRG---KKELDEIAERSLKganlwnEVKDRLDKPGGGLSGGQQQR--LCIARAIAVSPDVLLM 172
Cdd:PRK11288 92 PEMTVAENLYLG-QLPHKGGivnRRLLNYEAREQLE------HLGVDIDPDTPLKYLSIGQRqmVEIAKALARNARVIAF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 694049011 173 DEPCSALdpiSTLAIEDL---IQELKQDFTIVI-VTHNMQQAARVSD 215
Cdd:PRK11288 165 DEPTSSL---SAREIEQLfrvIRELRAEGRVILyVSHRMEEIFALCD 208
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-216 |
4.26e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEvtpgaRVEGSVLLDGEDI-YGSGVDpvGVRRTIGMVFQRPNPF 97
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEIdFKSSKE--ALENGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 PTMSIRDNVVAGLKLQGG----RGK---------KELDEIAERSLKGANLwnevkdrldkpggglSGGQQQRLCIARAIA 164
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTKGmfvdQDKmyrdtkaifDELDIDIDPRAKVATL---------------SVSQMQMIEIAKAFS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 165 VSPDVLLMDEPCSALDPISTLAIEDLIQELKQD-FTIVIVTHNMQQAARVSDQ 216
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDE 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-205 |
4.84e-06 |
|
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: 45.61 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPGaRVEgsvLLDGEDIYgsgvdpvgvrrtigMVFQRPNpFPT 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-RIG---MPEGEDLL--------------FLPQRPY-LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVA--GLKLQGGrgkkeldeiaERSlkganlwnevkdrldkpggglsggqqqRLCIARAIAVSPDVLLMDEPCS 177
Cdd:cd03223 78 GTLREQLIYpwDDVLSGG----------EQQ---------------------------RLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*...
gi 694049011 178 ALDPISTLAIEDLIQELKqdFTIVIVTH 205
Cdd:cd03223 121 ALDEESEDRLYQLLKELG--ITVISVGH 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-194 |
6.06e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 9 DVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrmhevtpGARVEGSVLLDGEDIYGSGVDPVGVRRTIG 88
Cdd:TIGR00956 768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL--------AERVTTGVITGGDRLVNGRPLDSSFQRSIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 89 MVFQRPNPFPTMSIRDNVV--AGLKLQGGRGKKELDEIAERSLKGANLwNEVKDRL-DKPGGGLSGGQQQRLCIARAIAV 165
Cdd:TIGR00956 840 YVQQQDLHLPTSTVRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEM-ESYADAVvGVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190
....*....|....*....|....*....|
gi 694049011 166 SPDVLL-MDEPCSALDPISTLAIEDLIQEL 194
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-208 |
1.07e-05 |
|
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: 46.44 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYY--GKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMhevtpgARVEGSVLLDGedIYGSGVDPV 81
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDG--VSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 82 GVRRTIGMVFQRPNPFpTMSIRDNVVAGLKLQGGRGKKELDEIAERSLkganlWNEVKDRLD----KPGGGLSGGQQQRL 157
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIF-SGTFRKNLDPYEQWSDEEIWKVAEEVGLKSV-----IEQFPDKLDfvlvDGGYVLSNGHKQLM 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 694049011 158 CIARAIAVSPDVLLMDEPCSALDPIsTLAIedLIQELKQDF---TIVIVTHNMQ 208
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPV-TLQI--IRKTLKQSFsncTVILSEHRVE 1413
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-217 |
2.87e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHevtPGARVEGSVLLDGE-----DIYGSGvdpvgvRRTIGMVFQR 93
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY---PHGSYEGEILFDGEvcrfkDIRDSE------ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 94 PNPFPTMSIRDNVVAGlklqggrgkkeldeiAERSLKGANLWNEVKDR----LDK------PGGGLSGGQQQR---LCIA 160
Cdd:NF040905 87 LALIPYLSIAENIFLG---------------NERAKRGVIDWNETNRRarelLAKvgldesPDTLVTDIGVGKqqlVEIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694049011 161 RAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDQT 217
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSI 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-180 |
3.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgaRVEGSVLLDGediygsgvdpvgvrrTIGMVFQRPNPF 97
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASVVIRG---------------TVAYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 98 pTMSIRDNVVAGLKLQGGRGKKELD-----------------EIAERslkGANLWNEVKDRldkpggglsggqqqrLCIA 160
Cdd:PLN03130 692 -NATVRDNILFGSPFDPERYERAIDvtalqhdldllpggdltEIGER---GVNISGGQKQR---------------VSMA 752
|
170 180
....*....|....*....|
gi 694049011 161 RAIAVSPDVLLMDEPCSALD 180
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALD 772
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-208 |
3.43e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 20 VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLnrMHEVTPGarvegsvlldgEDiygsgvDPVGVRRTIGMVFQRPNPFpT 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHA-----------ET------SSVVIRGSVAYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKELDEIAERS----LKGANLwNEVKDRldkpGGGLSGGQQQRLCIARAIAVSPDVLLMDEP 175
Cdd:PLN03232 693 ATVRENILFGSDFESERYWRAIDVTALQHdldlLPGRDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190
....*....|....*....|....*....|....
gi 694049011 176 CSALDP-ISTLAIEDLIQELKQDFTIVIVTHNMQ 208
Cdd:PLN03232 768 LSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLH 801
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-253 |
3.56e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 1 MAKRLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmhEVTPGARVEGSVLLDGEDIYGSGVdp 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFEGEELQASNI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 vgvRRT----IGMVFQRPNPFPTMSIRDNVVAGLKLQGGrGKKELDEIAERSLKganLWNEVKDRLD--KPGGGLSGGQQ 154
Cdd:PRK13549 77 ---RDTeragIAIIHQELALVKELSVLENIFLGNEITPG-GIMDYDAMYLRAQK---LLAQLKLDINpaTPVGNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 155 QRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQAARVSDqtgffnleatgkpgKLIE 233
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISD--------------TICV 215
|
250 260
....*....|....*....|
gi 694049011 234 IDDTEKIFSNPTQKATEDYI 253
Cdd:PRK13549 216 IRDGRHIGTRPAAGMTEDDI 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-208 |
4.29e-05 |
|
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: 43.69 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAV-SDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMhevtpgARVEGSVLLDGedIYGSGVDPVGVRRTIGMVFQRPNP 96
Cdd:cd03289 17 NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDG--VSWNSVPLQKWRKAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FpTMSIRDNvvagLKLQGGRGKKELDEIAER-SLKgaNLWNEVKDRLD----KPGGGLSGGQQQRLCIARAIAVSPDVLL 171
Cdd:cd03289 89 F-SGTFRKN----LDPYGKWSDEEIWKVAEEvGLK--SVIEQFPGQLDfvlvDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 694049011 172 MDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQ 208
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-207 |
5.79e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 32 VTAFIGPSGCGKSTVLRSL---------NRMHEVTPGARVE---GSVLLDG-EDIYGSGVDPVgvrRTIGMVFQRPnpfp 98
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVLKrfrGTELQNYfKKLYNGEIKVV---HKPQYVDLIP---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 tMSIRDNVVAGLKLQGGRGKkeLDEIAERsLKGANLWnevkdrlDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSA 178
Cdd:PRK13409 174 -KVFKGKVRELLKKVDERGK--LDEVVER-LGLENIL-------DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180
....*....|....*....|....*....
gi 694049011 179 LDPISTLAIEDLIQELKQDFTIVIVTHNM 207
Cdd:PRK13409 243 LDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
159-244 |
3.13e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.43 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQ--DFTIVIVTHNMQQAARVSDqtgFFNLEATgkpGKLIEIDD 236
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWAD---TITVLYC---GQTVESGP 242
|
....*...
gi 694049011 237 TEKIFSNP 244
Cdd:COG4170 243 TEQILKSP 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-209 |
3.83e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 41.54 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTPG-ARVEG-SVLLDGEDIYgsgvdpvgvrRTIGMVFQRPNP 96
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGkSILTNISDVH----------QNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 97 FPTMSIRDNVVAGLKLQGgRGKKELDEIAERSLKGANLwNEVKDRLdkpGGGLSGGQQQRLCIARAIAVSPDVLLMDEPC 176
Cdd:TIGR01257 2024 DDLLTGREHLYLYARLRG-VPAEEIEKVANWSIQSLGL-SLYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190
....*....|....*....|....*....|....
gi 694049011 177 SALDPISTLAIEDLIQE-LKQDFTIVIVTHNMQQ 209
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEE 2132
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
156-205 |
6.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 6.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIqeLKQDFTIVIVTH 205
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
159-216 |
6.59e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 6.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 159 IARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELKQD--FTIVIVTHNMQQAARVSDQ 216
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADK 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-243 |
7.13e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVdpVGVRRTIGMVFQRPNPFpTMSI 102
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDISKFGL--MDLRKVLGIIPQAPVLF-SGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNV----------------VAGLKLQGGRGKKELDeiAERSLKGANLwnEVKDRldkpggglsggqqQRLCIARAIAVS 166
Cdd:PLN03130 1330 RFNLdpfnehndadlwesleRAHLKDVIRRNSLGLD--AEVSEAGENF--SVGQR-------------QLLSLARALLRR 1392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694049011 167 PDVLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTHNMQQaarVSDQTGFFNLEAtgkpGKLIEIDDTEKIFSN 243
Cdd:PLN03130 1393 SKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNT---IIDCDRILVLDA----GRVVEFDTPENLLSN 1462
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-214 |
7.47e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 32 VTAFIGPSGCGKSTVLRSLNRMheVTPGArveGSVLLDGEDIygSGVDPVGVRRT-IGMVFQRPNPFPTMSIRDNVVAGL 110
Cdd:PRK15439 39 VHALLGGNGAGKSTLMKIIAGI--VPPDS---GTLEIGGNPC--ARLTPAKAHQLgIYLVPQEPLLFPNLSVKENILFGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 111 KLQGGRGKKELDEIAERS------LKGANLwnEVKDRldkpggglsggqqQRLCIARAIAVSPDVLLMDEPCSALDPIST 184
Cdd:PRK15439 112 PKRQASMQKMKQLLAALGcqldldSSAGSL--EVADR-------------QIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190
....*....|....*....|....*....|....*
gi 694049011 185 LAIEDLIQEL-KQDFTIVIVTHNM----QQAARVS 214
Cdd:PRK15439 177 ERLFSRIRELlAQGVGIVFISHKLpeirQLADRIS 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-175 |
7.76e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.39 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 18 HAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNrmhevtpGAR--VEGSVLLDGEDIYGSGVdPVGVRRTIGMVfqrpn 95
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALF-------GADpaDSGEIRLDGKPVRIRSP-RDAIRAGIAYV----- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 96 P--------FPTMSIRDNVV-AGLKLQGGRG---KKELDEIAER-----SLKGANLWNEVKDrldkpggglsggqqqrL- 157
Cdd:COG1129 333 PedrkgeglVLDLSIRENITlASLDRLSRGGlldRRRERALAEEyikrlRIKTPSPEQPVGN----------------Ls 396
|
170 180
....*....|....*....|....*
gi 694049011 158 -------CIARAIAVSPDVLLMDEP 175
Cdd:COG1129 397 ggnqqkvVLAKWLATDPKVLILDEP 421
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-242 |
1.26e-03 |
|
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: 39.12 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 23 VTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVtpgarVEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFpTMSI 102
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHTLRSRLSIILQDPILF-SGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 103 RDNVVAGLKLQGGRGKKELdEIAERSLKGANLWNEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDpi 182
Cdd:cd03288 112 RFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID-- 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 183 stLAIEDLIQELKQ----DFTIVIVTHNMQQAARVsdqtgffNLEATGKPGKLIEIDDTEKIFS 242
Cdd:cd03288 189 --MATENILQKVVMtafaDRTVVTIAHRVSTILDA-------DLVLVLSRGILVECDTPENLLA 243
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-213 |
1.46e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.15 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 35 FIGPSGCGKSTVLrslNRMHEVTPGarvEGSVLLDGEDIygSGVDPVGVRRTIGMVFQRPNPFPTMSirdnVVAGLKLQG 114
Cdd:PRK03695 27 LVGPNGAGKSTLL---ARMAGLLPG---SGSIQFAGQPL--EAWSAAELARHRAYLSQQQTPPFAMP----VFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 115 GRG------KKELDEIAERsLKganlwneVKDRLDKPGGGLSGGQQQRLCIARAI-AVSPDV------LLMDEPCSALDP 181
Cdd:PRK03695 95 PDKtrteavASALNEVAEA-LG-------LDDKLGRSVNQLSGGEWQRVRLAAVVlQVWPDInpagqlLLLDEPMNSLDV 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 694049011 182 ISTLAIEDLIQEL-KQDFTIVIVTHNM----QQAARV 213
Cdd:PRK03695 167 AQQAALDRLLSELcQQGIAVVMSSHDLnhtlRHADRV 203
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
30-127 |
1.53e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 38.90 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 30 RSVTAFIGPSGCGKSTVL----------RSLNRMHEVTPGaRVegsVLLDGEDiygsgvDPVGVRRTIGMVFQRPNPFPT 99
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLAldlavavatgRDWLGERRVKQG-RV---VYLAAED------PRDGLRRRLKAIGAHLGDEDA 70
|
90 100
....*....|....*....|....*...
gi 694049011 100 MSIRDNVVAGLKLQGGRGKKELDEIAER 127
Cdd:cd01125 71 ALAENLVIENLRGKPVSIDAEAPELERI 98
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-62 |
1.55e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 3 KRLDLkdVNiyYGKFHavsDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMheVTPGARV 62
Cdd:pfam13555 2 TRLQL--IN--WGTFD---GHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL--LVPAKRA 52
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
28-52 |
1.63e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 39.72 E-value: 1.63e-03
10 20
....*....|....*....|....*
gi 694049011 28 PPRSVTAFIGPSGCGKSTVLRSLNR 52
Cdd:COG5192 67 PPPFIVAVVGPPGTGKSTLIRSLVR 91
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
16-52 |
1.83e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 38.47 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 694049011 16 KFHA-VSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNR 52
Cdd:cd01882 24 KLHVpVVDRTPEEPPPLVVVVVGPPGVGKSTLIRSLIK 61
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-209 |
2.50e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 15 GKFH-AVSDVTLAVPPRSVTAFIGPSGCGKSTVLrslNRMHEVT-PGarvEGSVlldgeDIYGSGVDpvgVRRTIGMVFQ 92
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLS---NLIAGVTmPN---KGTV-----DIKGSAAL---IAISSGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 93 rpnpfpTMSIRDNVVAGLKLqgGRGKKELDEIAERSLKGAnlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPDVLLM 172
Cdd:PRK13545 100 ------LTGIENIELKGLMM--GLTKEKIKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVI 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 694049011 173 DEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQ 209
Cdd:PRK13545 168 DEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQ 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-210 |
2.75e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 4 RLDLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMH------EVTPGARVEGSvlldGEDIYGsg 77
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysnDLTLFGRRRGS----GETIWD-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 78 vdpvgVRRTIGMVFQ------RPNpfptMSIRDNVVAGLklqggrgkkeLDEI------AERSLKGANLWnevKDRL--- 142
Cdd:PRK10938 334 -----IKKHIGYVSSslhldyRVS----TSVRNVILSGF----------FDSIgiyqavSDRQQKLAQQW---LDILgid 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694049011 143 ----DKPGGGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQEL--KQDFTIVIVTHNMQQA 210
Cdd:PRK10938 392 krtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLisEGETQLLFVSHHAEDA 465
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
156-209 |
2.81e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.26 E-value: 2.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIQELK-QDFTIVIVTHNMQQ 209
Cdd:PRK13546 151 KLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQ 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-203 |
3.42e-03 |
|
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: 38.12 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 25 LAVP-PRSVTAFIGPSGCGKSTVLRSLNrmHEVTPG--------------ARVEGSVLLDG-EDIYGSGVDPVgvrRTIG 88
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILA--GKLKPNlgkfddppdwdeilDEFRGSELQNYfTKLLEGDVKVI---VKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 89 MVFQRPNPFptmsiRDNVVAGLKLQGGRGKkeLDEIAERSlkganlwnEVKDRLDKPGGGLSGGQQQRLCIARAIAVSPD 168
Cdd:cd03236 95 YVDLIPKAV-----KGKVGELLKKKDERGK--LDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 694049011 169 VLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIV 203
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
6-180 |
3.81e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 38.67 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 6 DLKDVNIYYGKFHAVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSL-NRmhevTPGARVEGSVLLDG----EDIYGsgvdp 80
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLaGR----KTGGYIEGDIRISGfpkkQETFA----- 952
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 81 vgvrRTIGMVFQRPNPFPTMSIRDNVV--AGLKLQGGRGKKE----LDEIAE----RSLKGA--------NLWNEVKdrl 142
Cdd:PLN03140 953 ----RISGYCEQNDIHSPQVTVRESLIysAFLRLPKEVSKEEkmmfVDEVMElvelDNLKDAivglpgvtGLSTEQR--- 1025
|
170 180 190
....*....|....*....|....*....|....*...
gi 694049011 143 dkpggglsggqqQRLCIARAIAVSPDVLLMDEPCSALD 180
Cdd:PLN03140 1026 ------------KRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
156-205 |
4.42e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 4.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDpISTlaIEDLIQELKQ-DFTIVIVTH 205
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INT--IRWLEDVLNErNSTMIIISH 210
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-56 |
5.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.60 E-value: 5.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 694049011 17 FHAVSDVTLavPPRSVTAFIGPSGCGKSTVLRSLNRMHEV 56
Cdd:COG4637 10 FKSLRDLEL--PLGPLTVLIGANGSGKSNLLDALRFLSDA 47
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-205 |
5.20e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 37.77 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 19 AVSDVTLAVPPRSVTAFIGPSGCGKSTVLRSLNRMHEVTpgarvEGSVLLDGEDIYGSGVDpvGVRRTIGMVFQRPNPFp 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPFLF- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 99 tmsiRDNVVAGLKLqgGRGKKELDEIAErslkGANLWNEVKDRLDKPGGGLSGG----------QQQRLCIARAIAVSPD 168
Cdd:PRK10789 402 ----SDTVANNIAL--GRPDATQQEIEH----VARLASVHDDILRLPQGYDTEVgergvmlsggQKQRISIARALLLNAE 471
|
170 180 190
....*....|....*....|....*....|....*..
gi 694049011 169 VLLMDEPCSALDPISTLAIEDLIQELKQDFTIVIVTH 205
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-207 |
5.76e-03 |
|
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: 36.20 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 29 PRSVTAFIGPSGCGKSTVLRSLnrMHEVTPgaRVEGSVLLDGEDIYGsgvdpvgvrrtigmvfqrpnpfPTMSIRDNVVA 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--ARELGP--PGGGVIYIDGEDILE----------------------EVLDQLLLIIV 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694049011 109 GLKLQGGRGKKELDEIaerslkganlwnevkdrldkpggglsggqqqrlcIARAIAVSPDVLLMDEPCSALDPISTLAIE 188
Cdd:smart00382 55 GGKKASGSGELRLRLA----------------------------------LALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*
gi 694049011 189 D------LIQELKQDFTIVIVTHNM 207
Cdd:smart00382 101 LleelrlLLLLKSEKNLTVILTTND 125
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-205 |
7.97e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.43 E-value: 7.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 694049011 156 RLCIARAIAVSPDVLLMDEPCSALDPIS-TLAIEDLIQELKQD--FTIVIVTH 205
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQknFQLIVITH 181
|
|
| |
