|
Name |
Accession |
Description |
Interval |
E-value |
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-331 |
0e+00 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 671.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRWWQRFKWRKKQAIALLHKVGIKDHSRLMDSYSYELT 160
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 241 ADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIPYTKRIKNHKFN 320
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIKGHEFA 320
|
330
....*....|.
gi 515646397 321 CHFPLNMEKKK 331
Cdd:COG4170 321 CHFPLNMEEKK 331
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-330 |
0e+00 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 566.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRWWQRFKWRKKQAIALLHKVGIKDHSRLMDSYSYELT 160
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 241 ADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIPYTKRIKNHKFN 320
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKNHLYA 320
|
330
....*....|
gi 515646397 321 CHFPLNMEKK 330
Cdd:PRK15093 321 CHFPLNMEEE 330
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-324 |
3.41e-121 |
|
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: 351.28 E-value: 3.41e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSaDRMRLGNIDLLQLTPKE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS-GEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIKDHSRLMDSYSYELTDG 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSK-----AEARERAIELLERVGLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 243 TQKLLDAPKHPYTVALLKAMPDFNdwiPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRI-KNHKFN 320
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLD---PDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVgPGHRVA 311
|
....
gi 515646397 321 CHFP 324
Cdd:COG0444 312 CHLY 315
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-326 |
2.96e-104 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 308.59 E-value: 2.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIKDHSRLMDSYSYELT 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNK-----KTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 241 ADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRIKNHKF 319
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRALPEFAQ---DKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLAGRQS 312
|
....*..
gi 515646397 320 NCHFPLN 326
Cdd:PRK11022 313 KCHYPLD 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-263 |
1.12e-88 |
|
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: 275.41 E-value: 1.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIpsysfegRWWQRFKWR--KKQAIALLHKVGIKDHSRLMDSYSYE 158
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVL-------RLHRGLSGAaaRARALELLERVGIPDPERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260
....*....|....*....|....*
gi 515646397 239 ESADTQKLLDAPKHPYTVALLKAMP 263
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAEP 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-309 |
6.83e-80 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 246.56 E-value: 6.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNiDLLQLTP 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGR-EILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAI-------PSYSFEgrwwqrfkwrkkQAIALLHKVGIKDHSRLMD 153
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLmlhkgmsKAEAFE------------ESVRMLDAVKMPEARKRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 154 SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 234 CGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIP 309
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYSIGLLNAVPRLDA---EGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAP 309
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-241 |
7.02e-77 |
|
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: 235.09 E-value: 7.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTpKE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK----PTSGSIIFDGKDLLKLS-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLhKVGIKDHSRLMDSYSYELTDG 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSK-----KEARKEAVLLL-LVGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-263 |
3.63e-72 |
|
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: 232.10 E-value: 3.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIE-IETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTP 80
Cdd:COG1123 259 PLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRvIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIKdhSRLMDSYSYELT 160
Cdd:COG1123 335 RSLRE-LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSR-----AERRERVAELLERVGLP--PDLADRYPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
250 260
....*....|....*....|...
gi 515646397 241 ADTQKLLDAPKHPYTVALLKAMP 263
Cdd:COG1123 487 GPTEEVFANPQHPYTRALLAAVP 509
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-324 |
2.85e-70 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 221.53 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGM-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNID 74
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL----EEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 75 LLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIK-DHsrlMD 153
Cdd:COG4608 82 ITGLSGRELRPL-RRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASK-----AERRERVAELLELVGLRpEH---AD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 154 SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 234 CGQSVESADTQKLLDAPKHPYTVALLKAMPdfndwIPHKEKLQS---LPGSIP-PLqHLPIGCRLGPRCPYAQRQC-VEI 308
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVP-----VPDPERRRErivLEGDVPsPL-NPPSGCRFHTRCPYAQDRCaTEE 306
|
330
....*....|....*..
gi 515646397 309 PYTKRI-KNHKFNCHFP 324
Cdd:COG4608 307 PPLREVgPGHQVACHLA 323
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-251 |
1.43e-69 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 225.55 E-value: 1.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSaDRMRLGNIDLLQLTPK 81
Cdd:COG1123 3 PLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrviARDIAMIFQEPSSCLDPSeKVGHQLIEAIpsysfEGRWWQRfKWRKKQAIALLHKVGIKdhsRLMDSYSYELTD 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNPV-TVGDQIAEAL-----ENLGLSR-AEARARVLELLEAVGLE---RRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250
....*....|
gi 515646397 242 DTQKLLDAPK 251
Cdd:COG1123 226 PPEEILAAPQ 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-265 |
2.73e-67 |
|
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: 211.20 E-value: 2.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLlqltPKE 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPV----TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSysfegrwwQRFKWRKKQAIALLHKVGIkdHSRLMDSYSYELTDG 162
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRI--------HGLPDREERIAELLEQVGL--PPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250 260
....*....|....*....|...
gi 515646397 243 TQKLLDAPKHPYTVALLKAMPDF 265
Cdd:COG1124 223 VADLLAGPKHPYTRELLAASLAF 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-321 |
1.45e-55 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 183.75 E-value: 1.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIE---------TPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGN 72
Cdd:PRK15079 7 VLLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT---DGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 73 iDLLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFE-GRwwQRFKWRKKqaiALLHKVGIKDHsrL 151
Cdd:PRK15079 84 -DLLGMKDDEWRAV-RSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSR--QEVKDRVK---AMMLKVGLLPN--L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 152 MDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK15079 155 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 232 MYCGQSVESADTQKLLDAPKHPYTVALLKA--MPDfndwiPHKEK---LQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCV 306
Cdd:PRK15079 235 MYLGHAVELGTYDEVYHNPLHPYTKALMSAvpIPD-----PDLERnktIQLLEGELPSPINPPSGCVFRTRCPIAGPECA 309
|
330
....*....|....*.
gi 515646397 307 EI-PYTKRIKNHKFNC 321
Cdd:PRK15079 310 KTrPVLEGSFRHAVSC 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-264 |
8.40e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 186.83 E-value: 8.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckenwkvsadrMRL---------- 70
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSI--------------LRLlpsppvvyps 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 71 GNI-----DLLQLTPKERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRWWQRfkwrkKQAIALLHKVGI 145
Cdd:PRK15134 69 GDIrfhgeSLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAAR-----GEILNCLDRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 146 KDHSRLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQW 225
Cdd:PRK15134 144 RQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKL 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 515646397 226 ATRITVMYCGQSVESADTQKLLDAPKHPYTVALLKAMPD 264
Cdd:PRK15134 224 ADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-263 |
7.01e-53 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 183.52 E-value: 7.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENW-KVSADRMRLGN-----IDLL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLRRrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 77 QLTPKERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIKDHSRLMDSYS 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASR-----EEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 157 YELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|....*..
gi 515646397 237 SVESADTQKLLDAPKHPYTVALLKAMP 263
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-264 |
7.16e-52 |
|
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: 179.11 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGM-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkvSADRMRLGNID 74
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 75 LLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGhQLIEaipsysfEGRWWQRFKW----RKKQAIALLHKVGIKdhSR 150
Cdd:COG4172 349 LDGLSRRALRPL-RRRMQVVFQDPFGSLSPRMTVG-QIIA-------EGLRVHGPGLsaaeRRARVAEALEEVGLD--PA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:COG4172 418 ARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVM 497
|
250 260 270
....*....|....*....|....*....|....
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYTVALLKAMPD 264
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-322 |
8.93e-52 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 174.00 E-value: 8.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 16 PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQlTPKERRRVIARDIAMIF 95
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI--E--TPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGIK-DHSrlmDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK11308 99 QNPYGSLNPRKKVGQILEEPLLINTSLSA-----AERREKALAMMAKVGLRpEHY---DRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 255 TVALLKAMPDFNDwIPHKEKLQsLPGSIP-PLqHLPIGCRLGPRCPYAQRQC-VEIPYTKRIKNHKFNCH 322
Cdd:PRK11308 251 TQALLSATPRLNP-DDRRERIK-LTGELPsPL-NPPPGCAFNARCPRAFGRCrQEQPQLRDYDGRLVACF 317
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-261 |
3.10e-44 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 152.16 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MP-LLDIRHLTIEieTPQGMVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLgniDLLQLT 79
Cdd:PRK10418 1 MPqQIELRNIALQ--AAQPLVHGV---SLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLL---DGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 80 PKERRrviARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfkwrKKQAIALLHKVGIKDHSRLMDSYSYEL 159
Cdd:PRK10418 73 PCALR---GRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPAD--------DATLTAALEAVGLENAARVLKLYPFEM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 160 TDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
250 260
....*....|....*....|..
gi 515646397 240 SADTQKLLDAPKHPYTVALLKA 261
Cdd:PRK10418 222 QGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-251 |
2.46e-40 |
|
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: 141.18 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 6 IRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERRR 85
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL--E--RPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 86 vIARDIAMIFQEPSscLDPSEKVGHQLieaipSYSFEGRWWQRfKWRKKQAIALLHKVGIKDHSrlmDSYSYELTDGECQ 165
Cdd:cd03258 80 -ARRRIGMIFQHFN--LLSSRTVFENV-----ALPLEIAGVPK-AEIEERVLELLELVGLEDKA---DAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 166 KVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQK 245
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 515646397 246 LLDAPK 251
Cdd:cd03258 228 VFANPQ 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-229 |
1.21e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.02 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKS--LvakAIVGvCKEnwKVSADRMRLGNIDLLQLT 79
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStlL---NILG-GLD--RPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 80 PKERRRVIARDIAMIFQepsscldpsekvGHQLIE--------AIPSYsFEGRwwqRFKWRKKQAIALLHKVGIKDHsrl 151
Cdd:COG1136 77 ERELARLRRRHIGFVFQ------------FFNLLPeltalenvALPLL-LAGV---SRKERRERARELLERVGLGDR--- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 152 MDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLtTITQWATRI 229
Cdd:COG1136 138 LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRV 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-281 |
1.23e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.43 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 6 IRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERRR 85
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL--E--RPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 86 ViARDIAMIFQEP---SSC--------------LDPSEkvghqlieaipsysfegrwwqrfkwRKKQAIALLHKVGIKDH 148
Cdd:COG1135 80 A-RRKIGMIFQHFnllSSRtvaenvalpleiagVPKAE-------------------------IRKRVAELLELVGLSDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 149 SrlmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATR 228
Cdd:COG1135 134 A---DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDR 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515646397 229 ITVMYCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGS 281
Cdd:COG1135 211 VAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGG 263
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
2-255 |
1.28e-36 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 132.24 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLApTSGSVYYRDRDGGPRDLFALSE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPS----EKVGHQLIEAipsysfeGrwWQRFKWRKKQAIALLHKVGIkDHSRlMDSYS 156
Cdd:COG4107 87 AERRRLRRTDWGMVYQNPRDGLRMDvsagGNIAERLMAA-------G--ERHYGDIRARALEWLERVEI-PLER-IDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 157 YELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250
....*....|....*....
gi 515646397 237 SVESADTQKLLDAPKHPYT 255
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYT 254
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-232 |
1.03e-35 |
|
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: 128.76 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR----PTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARDIAMIFQEpsscldpsekvgHQLIE--------AIPSYsFEGRwwqRFKWRKKQAIALLHKVGIKDHsrlMDSY 155
Cdd:cd03255 77 AAFRRRHIGFVFQS------------FNLLPdltalenvELPLL-LAGV---PKKERRERAEELLERVGLGDR---LNHY 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 156 SYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLtTITQWATRITVM 232
Cdd:cd03255 138 PSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-259 |
2.86e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 134.06 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVK-------AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNID 74
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 75 LLQLTPKERRrviardIAMIFQEPSSCLDPSEKVgHQLIEaipsysfEG-RWWQRF---KWRKKQAIALLHKVGIKDHSR 150
Cdd:PRK15134 354 RRQLLPVRHR------IQVVFQDPNSSLNPRLNV-LQIIE-------EGlRVHQPTlsaAQREQQVIAVMEEVGLDPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 lmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK15134 420 --HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVI 497
|
250 260
....*....|....*....|....*....
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYTVALL 259
Cdd:PRK15134 498 VLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-249 |
3.74e-35 |
|
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: 128.24 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETpqgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKE 82
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL----LKPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RrrviARDIAMIFQEPsscldpsekvghqliEAIPSYS-FE----GR-----WWQRFKWRKKQAIA-LLHKVGIKDHS-R 150
Cdd:COG1120 73 L----ARRIAYVPQEP---------------PAPFGLTvRElvalGRyphlgLFGRPSAEDREAVEeALERTGLEHLAdR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDsysyELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:COG1120 134 PVD----ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLV 209
|
250
....*....|....*....
gi 515646397 231 VMYCGQSVESADTQKLLDA 249
Cdd:COG1120 210 LLKDGRIVAQGPPEEVLTP 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-232 |
1.09e-34 |
|
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: 125.66 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 16 PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEVLVDGKDLTKLSLKELRR----KVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPSscldpsekvgHQLIEAIP----SYSFEGRWWQRfKWRKKQAIALLHKVGIKDhsrLMDSYSYELTDGECQKVMIAM 171
Cdd:cd03225 82 QNPD----------DQFFGPTVeeevAFGLENLGLPE-EEIEERVEEALELVGLEG---LRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 172 AIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-282 |
8.96e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.75 E-value: 8.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGM-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG-VCKENWKVSADRMRLGNI 73
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRlVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 74 DLLQLTPkerrrvIARDIAMIFQEPSSCLDPSEKVGHQLIEAIPSYSF-EGRWWQ-RFKWrkkqaiaLLHKVGIK-DHSR 150
Cdd:PRK10261 392 SPGKLQA------LRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLlPGKAAAaRVAW-------LLERVGLLpEHAW 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 lmdSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK10261 459 ---RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKL---QSLPGSI 282
Cdd:PRK10261 536 VMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRVllsDDLPSNI 590
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-187 |
1.99e-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: 120.45 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPssCL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG----LLSPTEGTILLDGQDLTDDERKSLRKEIG----YVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 103 DPSEKVGHQLIEAIPSYSFegrwwqRFKWRKKQAIALLHKVGIKD-HSRLMDSYSYELTDGECQKVMIAMAIAAKPKVLI 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGL------SKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 515646397 182 ADEPTN 187
Cdd:pfam00005 145 LDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-247 |
6.19e-33 |
|
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: 121.67 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 11 IEIE----TPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRv 86
Cdd:COG1122 1 IELEnlsfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP----TSGEVLVDGKDITKKNLRELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 87 iarDIAMIFQEPSscldpsekvgHQLIEAIP----SYSFEGRWWQRfKWRKKQAIALLHKVGIKDhsrLMDSYSYELTDG 162
Cdd:COG1122 76 ---KVGLVFQNPD----------DQLFAPTVeedvAFGPENLGLPR-EEIRERVEEALELVGLEH---LADRPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
....*
gi 515646397 243 TQKLL 247
Cdd:COG1122 218 PREVF 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-229 |
4.65e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIeieTPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:COG3638 1 PMLELRNLSK---RYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL----VEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRvIARDIAMIFQEPssCLdpsekVGHQ------LIEAIPSYSFEGRWWQRFKWR-KKQAIALLHKVGIKDHSrlmds 154
Cdd:COG3638 74 ALRR-LRRRIGMIFQQF--NL-----VPRLsvltnvLAGRLGRTSTWRSLLGLFPPEdRERALEALERVGLADKA----- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 155 ysYELTD----GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRI 229
Cdd:COG3638 141 --YQRADqlsgGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-262 |
4.95e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.87 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETpQGMVKA------VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNID 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAH-GGLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 75 LLQLTpKERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEA---IPSYSFEGRwwqrfkwrKKQAIALLHKVGIKDhsRL 151
Cdd:PRK10419 76 LAKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPlrhLLSLDKAER--------LARASEMLRAVDLDD--SV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 152 MDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK10419 145 LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
|
250 260 270
....*....|....*....|....*....|.
gi 515646397 232 MYCGQSVESADTQKLLdAPKHPYTVALLKAM 262
Cdd:PRK10419 225 MDNGQIVETQPVGDKL-TFSSPAGRVLQNAV 254
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
5.46e-31 |
|
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: 115.23 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 5 DIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERr 84
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL----LKPSSGEILLDGKDLASLSPKEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 85 rviARDIAMIFQepsscldpsekvghqlieaipsysfegrwwqrfkwrkkqaiaLLHKVGIKDhsrLMDSYSYELTDGEC 164
Cdd:cd03214 72 ---ARKIAYVPQ------------------------------------------ALELLGLAH---LADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 165 QKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
27-254 |
1.49e-30 |
|
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: 115.68 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRvIARDIAMIFQEPS--SCLDP 104
Cdd:cd03261 20 DLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP----DSGEVLIDGEDISGLSEAELYR-LRRRMGMLFQSGAlfDSLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGHQLIEaipsYSFEGRWWQRfkwrkKQAIALLHKVGIKDHSRLMDSysyELTDGECQKVMIAMAIAAKPKVLIADE 184
Cdd:cd03261 95 FENVAFPLRE----HTRLSEEEIR-----EIVLEKLEAVGLRGAEDLYPA---ELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 185 PTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPkHPY 254
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-229 |
2.18e-30 |
|
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: 115.36 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRViARDIAMIFQE 97
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGSVLIDGTDINKLKGKALRQL-RRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 psscldpsekvgHQLIE-----------AIPSYSFEGRWWQRFKWRKKQ-AIALLHKVGIKDHSRLMDSysyELTDGECQ 165
Cdd:cd03256 87 ------------FNLIErlsvlenvlsgRLGRRSTWRSLFGLFPKEEKQrALAALERVGLLDKAYQRAD---QLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 166 KVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRI 229
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-261 |
7.24e-30 |
|
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: 113.93 E-value: 7.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSAD--RMRLGNIDLLQLTPKERRRVIARDIAMIfqep 98
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI------NRLIEPTsgEIFIDGEDIREQDPVELRRKIGYVIQQI---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 ssCLDPSEKVgHQLIEAIPSysFEGrwWQRFKwRKKQAIALLHKVGIkDHSRLMDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:cd03295 85 --GLFPHMTV-EENIALVPK--LLK--WPKEK-IRERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 515646397 259 LKA 261
Cdd:cd03295 236 VGA 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-254 |
1.57e-29 |
|
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: 113.15 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTieieTPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:COG1127 4 PMIEVRNLT----KSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL----LRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRvIARDIAMIFQepSSCLDPS----EKVGHQLIE--AIPSysfegrwwqrfKWRKKQAIALLHKVGIKDHSRLMDSy 155
Cdd:COG1127 76 ELYE-LRRRIGMLFQ--GGALFDSltvfENVAFPLREhtDLSE-----------AEIRELVLEKLELVGLPGAADKMPS- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 156 syELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:COG1127 141 --ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|....*....
gi 515646397 236 QSVESADTQKLLDAPkHPY 254
Cdd:COG1127 219 KIIAEGTPEELLASD-DPW 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-249 |
2.19e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.46 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIARDIAMIFQEPS 99
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL------LRPTS---GEVRVLGEDVARDPAEVRRRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scLDPSEKVGHQLieaipsysfegRWWQRF-----KWRKKQAIALLHKVGIKDH-SRLMDSYSyeltDGECQKVMIAMAI 173
Cdd:COG1131 84 --LYPDLTVRENL-----------RFFARLyglprKEARERIDELLELFGLTDAaDRKVGTLS----GGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-249 |
2.21e-29 |
|
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: 112.78 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRVIARdIAMIFQE-- 97
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE----PSSGSILLEGTDITKLRGKKLRKLRRR-IGMIFQHyn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 ---PSSCLdpsEKVghqLIEAIPSYSFEGRWWQRFKWRKKQ-AIALLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAI 173
Cdd:TIGR02315 90 lieRLTVL---ENV---LHGRLGYKPTWRSLLGRFSEEDKErALSALERVGLADKA---YQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-239 |
4.48e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKS----LVAKAIvgvckenwKVSADRMRLGNIDLLQLTPKE----RRRviardI 91
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKStllkLLYGEE--------RPTSGQVLVNGQDLSRLKRREipylRRR-----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 92 AMIFQEpsscldpsekvgHQLIE--------AIPsysfegrwwQR---FKWR--KKQAIALLHKVGIKDHsrlMDSYSYE 158
Cdd:COG2884 82 GVVFQD------------FRLLPdrtvyenvALP---------LRvtgKSRKeiRRRVREVLDLVGLSDK---AKALPHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
.
gi 515646397 239 E 239
Cdd:COG2884 217 R 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-279 |
5.31e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.13 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 5 DIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERR 84
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL--E--RPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 85 RViARDIAMIFQepsscldpsekvgH-QLIE--------AIPsysFEGRWWQRFKWRKKQAiALLHKVGIKDHsrlMDSY 155
Cdd:PRK11153 79 KA-RRQIGMIFQ-------------HfNLLSsrtvfdnvALP---LELAGTPKAEIKARVT-ELLELVGLSDK---ADRY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 156 SYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:PRK11153 138 PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 515646397 236 QSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLP 279
Cdd:PRK11153 218 RLVEQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYLARLQAEP 261
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
9.40e-29 |
|
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: 110.60 E-value: 9.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKS----LVAkaivGVckEnwKVSADRMRLGNIDLLQ 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKStllgLLA----GL--D--RPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 78 LTPKERRRVIARDIAMIFQE----PS-SCLD----PSEKVGHQliEAipsysfegrwwqrfkwrKKQAIALLHKVGIKDh 148
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSfqllPTlTALEnvmlPLELAGRR--DA-----------------RARARALLERVGLGH- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 149 srLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDL 219
Cdd:COG4181 139 --RLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
1.15e-28 |
|
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: 111.28 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTP 80
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF----YRPTSGRILFDGRDITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 kerRRVIARDIAMIFQEPS-----SCLD-----PSEKVGHQLIEAIPSYsfeGRWWQRFKWRKKQAIALLHKVGIKDHsr 150
Cdd:COG0411 74 ---HRIARLGIARTFQNPRlfpelTVLEnvlvaAHARLGRGLLAALLRL---PRARREEREARERAEELLERVGLADR-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 lMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:COG0411 146 -ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
....*.
gi 515646397 231 VMYCGQ 236
Cdd:COG0411 225 VLDFGR 230
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-262 |
9.70e-28 |
|
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: 108.76 E-value: 9.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTieieTPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGN-IDLLQLTP 80
Cdd:TIGR02323 2 PLLQVSGLS----KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAeLELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGHQLIEAIpsYSFEGRWWQRFKwrkKQAIALLHKVGIkDHSRLmDSYSYELT 160
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERL--MAIGARHYGNIR---ATAQDWLEEVEI-DPTRI-DDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250 260
....*....|....*....|..
gi 515646397 241 ADTQKLLDAPKHPYTVALLKAM 262
Cdd:TIGR02323 231 GLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
1.25e-27 |
|
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: 107.91 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF----LRPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRviaRDIAMIFQEPS-----SCLDPSEkVGHQLIEaiPSYSFEGRWWQRFKWRKKQAIALLHKVGIkdhSRLMDSYSYE 158
Cdd:cd03219 73 AR---LGIGRTFQIPRlfpelTVLENVM-VAAQART--GSGLLLARARREEREARERAEELLERVGL---ADLADRPAGE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-254 |
1.94e-27 |
|
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: 113.01 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 16 PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL----YEPTSGRILIDGIDLRQIDPASLRR----QIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPS----ScldpsekvghqLIEAI----PSYSFEgrwwqrfkwrkkQAIALLHKVGIKDH-SRLMDSYSYELTD----- 161
Cdd:COG2274 556 QDVFlfsgT-----------IRENItlgdPDATDE------------EIIEAARLAGLHDFiEALPMGYDTVVGEggsnl 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 --GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTItQWATRITVMYCGQSVE 239
Cdd:COG2274 613 sgGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
250
....*....|....*
gi 515646397 240 SADTQKLLDAPKHPY 254
Cdd:COG2274 690 DGTHEELLARKGLYA 704
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-247 |
2.14e-27 |
|
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: 112.20 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLT---IEIEtpQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK----ENWkvsadrMRLGN-- 72
Cdd:TIGR03269 278 PIIKVRNVSkryISVD--RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsgEVN------VRVGDew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 73 IDLLQLTPKERRRViARDIAMIFQEPSscLDPSEKVGHQLIEAIpsySFEgrwwQRFKWRKKQAIALLHKVGIKDHS--R 150
Cdd:TIGR03269 350 VDMTKPGPDGRGRA-KRYIGILHQEYD--LYPHRTVLDNLTEAI---GLE----LPDELARMKAVITLKMVGFDEEKaeE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQ----ILRLLSRMNQinntTIVLIGHDLTTITQWA 226
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEMEQ----TFIIVSHDMDFVLDVC 495
|
250 260
....*....|....*....|.
gi 515646397 227 TRITVMYCGQSVESADTQKLL 247
Cdd:TIGR03269 496 DRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-236 |
3.07e-27 |
|
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: 104.63 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQepss 100
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----LKPTSGEILIDGKDIAKLPLEELRR----RIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekvghqlieaipsysfegrwwqrfkwrkkqaiallhkvgikdhsrlmdsysyeLTDGECQKVMIAMAIAAKPKVL 180
Cdd:cd00267 81 ----------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-238 |
2.29e-26 |
|
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: 105.61 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRvIARDIAMIFQEPss 100
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKP----TSGTVTIDGRDITAKKKKKLKD-LRKKVGLVFQFP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsEkvgHQLIEAI--------PsysfegrwwQRFKWRKKQ----AIALLHKVGIKDHsrLMDSYSYELTDGECQKVM 168
Cdd:TIGR04521 92 -----E---HQLFEETvykdiafgP---------KNLGLSEEEaeerVKEALELVGLDEE--YLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 169 IAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-232 |
3.81e-26 |
|
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: 103.32 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIdLLQLTPKER 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL------ERPTS---GEV-LVDGEPVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRviaRDIAMIFQEPSscLDPSEKVghqlIEAIpSYSFEGRWWQRfKWRKKQAIALLHKVGIKDHSrlmDSYSYELTDGE 163
Cdd:cd03293 71 PG---PDRGYVFQQDA--LLPWLTV----LDNV-ALGLELQGVPK-AEARERAEELLELVGLSGFE---NAYPHQLSGGM 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-246 |
1.76e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSAD--RMRLGNIDLLQL 78
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGV------YQPDsgEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 79 TPKErrrviARD--IAMIFQEPSSCLDPSekVGhqliEAIpsysFEGRWWQRF---KWRK--KQAIALLHKVGIK-DHSR 150
Cdd:COG1129 72 SPRD-----AQAagIAIIHQELNLVPNLS--VA----ENI----FLGREPRRGgliDWRAmrRRARELLARLGLDiDPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDsysyELTDGECQKVMIAMAIAAKPKVLIADEPTndlDPITQSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWATR 228
Cdd:COG1129 137 PVG----DLSVAQQQLVEIARALSRDARVLILDEPT---ASLTEREVERLFRIIRRLkaQGVAIIYISHRLDEVFEIADR 209
|
250
....*....|....*...
gi 515646397 229 ITVMYCGQSVESADTQKL 246
Cdd:COG1129 210 VTVLRDGRLVGTGPVAEL 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-236 |
2.27e-25 |
|
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: 100.16 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKER 83
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL------LKPDS---GEIKVLGKDIKKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARDIAMIFQEPSscLDPSEKVGHQLieaipsysfegrwwqrfkwrkkqaiallhkvgikdhsrlmdsysyELTDGE 163
Cdd:cd03230 68 PEEVKRRIGYLPEEPS--LYENLTVRENL---------------------------------------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-236 |
5.08e-25 |
|
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: 99.18 E-value: 5.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckeNWKVSADrMRLGNIDLLQLTpkER 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---EEPDSGS-ILIDGEDLTDLE--DE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARDIAMIFQEPssCLDPsekvghqlieaipsysfegrwwqrfkwrkkqaiallhkvgikdHSRLMDSYSYELTDGE 163
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFP-------------------------------------------HLTVLENIALGLSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-254 |
5.13e-25 |
|
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: 103.39 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQe 97
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEP----TAGQIFIDGENIMKQSPVELREVRRKKIGMVFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 pSSCLDPsekvgHQLIEAIPSYSFEGRWWQRFKwRKKQAIALLHKVGIKDHsrlMDSYSYELTDGECQKVMIAMAIAAKP 177
Cdd:TIGR01186 79 -QFALFP-----HMTILQNTSLGPELLGWPEQE-RKEKALELLKLVGLEEY---EHRYPDELSGGMQQRVGLARALAAEP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 178 KVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:TIGR01186 149 DILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEY 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-259 |
1.39e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.63 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGM-----VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMrlgnIDLLQ 77
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELL----IDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 78 LTPKERRRVIARdIAMIFQEPSSCLDPSEKVGhQLIEaIP---SYSFEGrwwqrfKWRKKQAIALLHKVGIK-DHSrlmD 153
Cdd:PRK15112 77 LHFGDYSYRSQR-IRMIFQDPSTSLNPRQRIS-QILD-FPlrlNTDLEP------EQREKQIIETLRQVGLLpDHA---S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 154 SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
250 260
....*....|....*....|....*.
gi 515646397 234 CGQSVESADTQKLLDAPKHPYTVALL 259
Cdd:PRK15112 225 QGEVVERGSTADVLASPLHELTKRLI 250
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-246 |
1.91e-24 |
|
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: 99.18 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAD---RMRLGNIDLLQLTP 80
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRviarDIAMIFQEPSscldpsekvghqlieAIPSYSFE----GRWWQRFKWRKK-QAIA--LLHKVGIKD--HSRL 151
Cdd:cd03260 77 LELRR----RVGMVFQKPN---------------PFPGSIYDnvayGLRLHGIKLKEElDERVeeALRKAALWDevKDRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 152 mdsYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQWATRITV 231
Cdd:cd03260 138 ---HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAF 212
|
250
....*....|....*
gi 515646397 232 MYCGQSVESADTQKL 246
Cdd:cd03260 213 LLNGRLVEFGPTEQI 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-218 |
5.47e-24 |
|
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: 97.48 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvCKENwKVSADRMRLGNIDLLQLtpkeRRRVIA---RDIAMI 94
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLI---YKEE-LPTSGTIRVNGQDVSDL----RGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 95 FQEpsSCLDPSEKVGHQLIEAIPSYSFEGRWWQrfkwrkKQAIALLHKVGIKDHSRlmdSYSYELTDGECQKVMIAMAIA 174
Cdd:cd03292 84 FQD--FRLLPDRNVYENVAFALEVTGVPPREIR------KRVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQInNTTIVLIGHD 218
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
6.78e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.24 E-value: 6.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIdllqLTP 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL------EKPTS---GEV----LVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPS-----SCLDpseKVGhqlieaipsYSFEGRWWQRfKWRKKQAIALLHKVGIKDHsrlMDSY 155
Cdd:COG1116 72 GKPVTGPGPDRGVVFQEPAllpwlTVLD---NVA---------LGLELRGVPK-AERRERARELLELVGLAGF---EDAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 156 SYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHD------LttitqwATRI 229
Cdd:COG1116 136 PHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvdeavfL------ADRV 209
|
...
gi 515646397 230 TVM 232
Cdd:COG1116 210 VVL 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-254 |
1.01e-23 |
|
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: 98.10 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:cd03294 18 FKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP----TSGKVLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQepSSCLDPSEKVghqlIEAIpSYSFEGRWWQRfKWRKKQAIALLHKVGIKDHSrlmDSYSYELT 160
Cdd:cd03294 94 KELRELRRKKISMVFQ--SFALLPHRTV----LENV-AFGLEVQGVPR-AEREERAAEALELVGLEGWE---HKYPDELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPIT----QSQILRLLSRMNQinntTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDPLIrremQDELLRLQAELQK----TIVFITHDLDEALRLGDRIAIMKDGR 238
|
250
....*....|....*...
gi 515646397 237 SVESADTQKLLDAPKHPY 254
Cdd:cd03294 239 LVQVGTPEEILTNPANDY 256
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-232 |
1.55e-23 |
|
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: 96.06 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIA-----RDIamifq 96
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL------LKPTS---GSIRVFGKPLEKERKRIGyvpqrRSI----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 97 EPSSCLDPSEKVghqlieAIPSYSFeGRWWQRFKWRKKQAI-ALLHKVGIKDHS-RLMDsysyELTDGECQKVMIAMAIA 174
Cdd:cd03235 80 DRDFPISVRDVV------LMGLYGH-KGLFRRLSKADKAKVdEALERVGLSELAdRQIG----ELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-255 |
4.23e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.15 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGN-IDLLQLT 79
Cdd:PRK11701 4 QPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 80 PKERRRVIARDIAMIFQEPSSCLDPS----EKVGHQLIeAIpsysfegrwwqrfKWR-----KKQAIALLHKVGIkDHSR 150
Cdd:PRK11701 80 EAERRRLLRTEWGFVHQHPRDGLRMQvsagGNIGERLM-AV-------------GARhygdiRATAGDWLERVEI-DAAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMD---SYSyeltDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWAT 227
Cdd:PRK11701 145 IDDlptTFS----GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAH 220
|
250 260
....*....|....*....|....*...
gi 515646397 228 RITVMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDDPQHPYT 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-253 |
7.76e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 7.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQltPKERRRVIARDIAMIFQE 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--E--EITSGDLIVDGLKVND--PKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 ----PSscLDPSEKVGHQLIEAIPSYSFEGRwwqrfkwrkKQAIALLHKVGIKDHsrlMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK09493 86 fylfPH--LTALENVMFGPLRVRGASKEEAE---------KQARELLAKVGLAER---AHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHP 253
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-236 |
9.75e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLlqlTPKE-RRRVIARDIAMIFQEPS 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP----TSGKIIIDGVDI---TDKKvKLSDIRKKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scldpsekvgHQLIEAIPSYSFE------GRWWQRFKWRKKQAIALlhkVGIkDHSRLMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK13637 94 ----------YQLFEETIEKDIAfgpinlGLSEEEIENRVKRAMNI---VGL-DYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-232 |
1.16e-22 |
|
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: 92.83 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 16 PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIF 95
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL----YDPTSGEILIDGVDLRDLDLESLRKNIA----YVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPsscldpsekvghqlieaipsYSFEGrwwqrfkwrkkqAIAllhkvgikdhsrlmdsysyE--LTDGECQKVMIAMAI 173
Cdd:cd03228 83 QDP--------------------FLFSG------------TIR-------------------EniLSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMnqINNTTIVLIGHDLTTITQwATRITVM 232
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-232 |
1.63e-22 |
|
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: 93.35 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEietpQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwKVSADRMRLGNIDLLQLTPKEr 83
Cdd:cd03259 1 LELKGLSKT----YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE----RPDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 rrviaRDIAMIFQEPssCLDPSEKVghqlIEAIpSYSFEGRWWQRFKWRKKqAIALLHKVGIkdhSRLMDSYSYELTDGE 163
Cdd:cd03259 72 -----RNIGMVFQDY--ALFPHLTV----AENI-AFGLKLRGVPKAEIRAR-VRELLELVGL---EGLLNRYPHELSGGQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-246 |
1.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP----TTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CL--DPSEKVghqlIEAIPsysfegrwwQRFKWR----KKQAIALLHKVGIkdhSR-LMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK13646 97 QLfeDTVERE----IIFGP---------KNFKMNldevKNYAHRLLMDLGF---SRdVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-236 |
3.04e-22 |
|
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: 92.95 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTieiET-PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKE 82
Cdd:cd03263 1 LQIRNLT---KTyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGE------LRPTS---GTAYINGYSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIARDIAMIFQepSSCLDPsEKVGHQLIEaipsysFEGRWWQRFKW-RKKQAIALLHKVGIKDHsrlMDSYSYELTD 161
Cdd:cd03263 69 DRKAARQSLGYCPQ--FDALFD-ELTVREHLR------FYARLKGLPKSeIKEEVELLLRVLGLTDK---ANKRARTLSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-257 |
4.81e-22 |
|
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: 92.78 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERrrviarDIAMIFQEpsSCLDPse 106
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD----SGKILLNGKDITNLPPEKR------DISYVPQN--YALFP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 107 kvgHQLIEAIPSYSFEGRWWQRfKWRKKQAIALLHKVGIkDHsrLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPT 186
Cdd:cd03299 85 ---HMTVYKNIAYGLKKRKVDK-KEIERKVLEIAEMLGI-DH--LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 187 NDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKhPYTVA 257
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK-NEFVA 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-236 |
9.91e-22 |
|
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: 91.55 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERrrviarDIAMIFQe 97
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 pSSCLDP-------------SEKVGHQLIEAipsysfegrwwqrfkwRKKQAIALLhkvGIkDHsrLMDSYSYELTDGEC 164
Cdd:cd03301 80 -NYALYPhmtvydniafglkLRKVPKDEIDE----------------RVREVAELL---QI-EH--LLDRKPKQLSGGQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 165 QKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-244 |
1.50e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRrVIARDIAMIFQE 97
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERP----SAGKIWFSGHDITRLKNREVP-FLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSSCLDPS--EKVGHQLIeaIPSYSFEGRwwqrfkwrKKQAIALLHKVGIKDHSRlmdSYSYELTDGECQKVMIAMAIAA 175
Cdd:PRK10908 88 HHLLMDRTvyDNVAIPLI--IAGASGDDI--------RRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 176 KPKVLIADEPTNDLDPITQSQILRLLSRMNQInNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQ 244
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-238 |
5.72e-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: 87.87 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSAD--RMRLGNIDLLQLTPKERRRviaRDIAMIF 95
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL------YKPDsgEILVDGKEVSFASPRDARR---AGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QepsscldpsekvghqlieaipsysfegrwwqrfkwrkkqaiallhkvgikdhsrlmdsysyeLTDGECQKVMIAMAIAA 175
Cdd:cd03216 82 Q--------------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 176 KPKVLIADEPTNDLDPitqSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03216 100 NARLLILDEPTAALTP---AEVERLFKVIRRLraQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
27-262 |
1.38e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 88.90 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLqLTPKERRRVIaRDIAMIFQepSSCLDP 104
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCI------NLleEPDSGTITVDGEDLT-DSKKDINKLR-RKVGMVFQ--QFNLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGHQLIEAiPsysfegRWWQrfKWRKKQAIA----LLHKVGIKDHsrlMDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:COG1126 91 HLTVLENVTLA-P------IKVK--KMSKAEAEErameLLERVGLADK---ADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 181 IADEPTNDLDPITQSQILRLlsrMNQI--NNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDV---MRDLakEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 515646397 259 LKAM 262
Cdd:COG1126 236 LSKV 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-239 |
1.48e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPK 81
Cdd:PRK13635 4 EIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLP----EAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRviarDIAMIFQEPSScldpsEKVGHQLIEAIpSYSFEGRWWQRFKW--RKKQAialLHKVGIKDhsrLMDSYSYEL 159
Cdd:PRK13635 78 DVRR----QVGMVFQNPDN-----QFVGATVQDDV-AFGLENIGVPREEMveRVDQA---LRQVGMED---FLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 160 TDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQwATRITVMYCGQSVE 239
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
238-305 |
1.98e-20 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 83.60 E-value: 1.98e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 238 VESADTQKLLDAPKHPYTVALLKAMPDFNdwiPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC 305
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLD---PPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-236 |
2.58e-20 |
|
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: 86.72 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEietpqGMVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:cd03215 3 PVLEVRGLSVK-----GAVRDV---SFEVRAGEIVGIAGLVGNGQTELAEALFGL----RPPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrvIARDIAMIfqepsscldPSEkvghqlieaipsysfegrwwqrfkwRKKQAIALLHkvGIKDHSRLmdsySYELTD 161
Cdd:cd03215 71 DA---IRAGIAYV---------PED-------------------------RKREGLVLDL--SVAENIAL----SSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-232 |
3.24e-20 |
|
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: 87.43 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRviardIAMIFQE 97
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK----PTSGRATVAGHDVVREPREVRRR-----IGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSscLDPsEKVGHQ--LIEAipsySFEGRWWQRFKWRKKQAIALLHKVGIKDhsRLMDSYSyeltDGECQKVMIAMAIAA 175
Cdd:cd03265 82 LS--VDD-ELTGWEnlYIHA----RLYGVPGAERRERIDELLDFVGLLEAAD--RLVKTYS----GGMRRRLEIARSLVH 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 176 KPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-236 |
3.47e-20 |
|
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: 87.35 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIrGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLG---------NIDLlqltPKERRRviardIAMIFQE 97
Cdd:cd03297 18 DFDLNEEVT-GIFGASGAGKSTLLRCIAGLEK----PDGGTIVLNgtvlfdsrkKINL----PPQQRK-----IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSscLDPSEKVGHQLIEAIPSysfegrwwQRFKWRKKQAIALLHKVGIkDHsrLMDSYSYELTDGECQKVMIAMAIAAKP 177
Cdd:cd03297 84 YA--LFPHLNVRENLAFGLKR--------KRNREDRISVDELLDLLGL-DH--LLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 178 KVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-323 |
3.83e-20 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 83.18 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 236 QSVESADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRI 314
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKK---RDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECrKEPPALVEI 77
|
90
....*....|
gi 515646397 315 -KNHKFNCHF 323
Cdd:TIGR01727 78 aEGHRVACHL 87
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-218 |
4.84e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.14 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MP---LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQ 77
Cdd:PRK10584 1 MPaenIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG----SSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 78 LTPKERRRVIARDIAMIFQepSSCLDPS----EKVghQLieaiPSYsFEGrwwQRFKWRKKQAIALLHKVGIKDhsRLmD 153
Cdd:PRK10584 77 MDEEARAKLRAKHVGFVFQ--SFMLIPTlnalENV--EL----PAL-LRG---ESSRQSRNGAKALLEQLGLGK--RL-D 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 154 SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHD 218
Cdd:PRK10584 142 HLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-262 |
5.35e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.71 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQE 97
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 ----PSSCLDPSEKVGHQLiEAIPSYSfegrwwqrfkwRKKQAIALLHKVGIKDHSRlmdSYSYELTDGECQKVMIAMAI 173
Cdd:PRK10070 115 falmPHMTVLDNTAFGMEL-AGINAEE-----------RREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHP 253
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
....*....
gi 515646397 254 YTVALLKAM 262
Cdd:PRK10070 260 YVRTFFRGV 268
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-244 |
1.25e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRViarDIAMIFQE 97
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI----HEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 pSSCLDPSEKVGHQLIEAIPSYSFEGRWWQRFKWRKKQAIALLHKVGIKdhsRLMDSYSYELTDGECQKVMIAMAIAAKP 177
Cdd:PRK09700 89 -LSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLK---VDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 178 KVLIADEPTNDLdpiTQSQILRLLSRMNQINN--TTIVLIGHDLTTITQWATRITVMYCGQSVESADTQ 244
Cdd:PRK09700 165 KVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
27-236 |
1.81e-19 |
|
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: 85.27 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLQltPKERRRVIARDIAMIFQepSSCLDP 104
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCI------NLleEPDSGTIIIDGLKLTD--DKKNINELRQKVGMVFQ--QFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGHQLIEAIPsysfegrwwQRFKWRKKQAIA----LLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:cd03262 90 HLTVLENITLAPI---------KVKGMSKAEAEEraleLLEKVGLADKA---DAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-232 |
2.06e-19 |
|
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: 85.46 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPS 99
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---------QPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scldpsekvghQLIEAIP---SYSFEGRWWQ----RFKWRKKQAIALLhkvgikDHSRLMDSYSYELTDGECQKVMIAMA 172
Cdd:cd03267 105 -----------QLWWDLPvidSFYLLAAIYDlppaRFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 173 IAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-260 |
2.90e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.79 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGV---CKENWKVSADRMRL--GNIDLLQLTPKERRRVIARDIAMIFQEPS- 99
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLekpSEGSIVVNGQTINLvrDKDGQLKVADKNQLRLLRTRLTMVFQHFNl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 -SCLDPSEKVGHQLIEAIPSYSFEGRwwqrfkwrkKQAIALLHKVGIKDHSRlmDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:PRK10619 104 wSHMTVLENVMEAPIQVLGLSKQEAR---------ERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQF 251
|
..
gi 515646397 259 LK 260
Cdd:PRK10619 252 LK 253
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-232 |
3.48e-19 |
|
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: 86.29 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRviardIAMIFQE 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRP----TSGTARVAGYDVVREPRKVRRS-----IGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSscldPSEKV-GHQLIEAIpsysfeGRWWQRFKW-RKKQAIALLHKVGIKDHS-RLMDSYSyeltDGECQKVMIAMAIA 174
Cdd:TIGR01188 75 AS----VDEDLtGRENLEMM------GRLYGLPKDeAEERAEELLELFELGEAAdRPVGTYS----GGMRRRLDIAASLI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:TIGR01188 141 HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKE-EGVTILLTTHYMEEADKLCDRIAII 197
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-232 |
8.09e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.14 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPS- 99
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YDPTSGRILIDGVDIRDLTLESLRRQIG----VVPQDTFl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 -----------SCLDPSEKvghQLIEAIpsysfegrwwqrfkwrkkqAIALLHKVgIkdhSRLMDSYSYELTD------- 161
Cdd:COG1132 426 fsgtireniryGRPDATDE---EVEEAA-------------------KAAQAHEF-I---EALPDGYDTVVGErgvnlsg 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQwATRITVM 232
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVL 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
8.61e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.78 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIETpqgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAI----------------VGVCK--------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhVALCEkcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 59 ---ENWKVSADRMRLGNIDLLQLTPKERRRVIARdIAMIFQEpSSCLDPSEKVGHQLIEAIPSYSFEGrwwqrfKWRKKQ 135
Cdd:TIGR03269 77 kvgEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKR-IAIMLQR-TFALYGDDTVLDNVLEALEEIGYEG------KEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 136 AIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLI 215
Cdd:TIGR03269 149 AVDLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
250
....*....|....*.
gi 515646397 216 GH------DLTTITQW 225
Cdd:TIGR03269 226 SHwpevieDLSDKAIW 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-238 |
1.97e-18 |
|
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: 82.30 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDllqLTPKERRRViardIAMIFQEPSS 100
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGKP---IKAKERRKS----IGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CLDpSEKVGHQLIEAIPSYSFEgrwwqrfkwrKKQAIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:cd03226 83 QLF-TDSVREELLLGLKELDAG----------NEQAETVLKDLDL---YALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 181 IADEPTNDLDPITQSQILRLlsrMNQINN--TTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGEL---IRELAAqgKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-236 |
2.20e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRMRLGNIDLLQLTPKERRRvIARDI-------AM 93
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTVQREGR-LARDIrksrantGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 94 IFQEPS--SCLDPSEKVghqLIEAIPSYSFegrWWQRFKW----RKKQAIALLHKVGIKD--HSRLMdsysyELTDGECQ 165
Cdd:PRK09984 91 IFQQFNlvNRLSVLENV---LIGALGSTPF---WRTCFSWftreQKQRALQALTRVGMVHfaHQRVS-----TLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 166 KVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-255 |
2.27e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.04 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKA------IVGVCKENWKVSADRMRLGNID 74
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 75 LLQLtpkeRRRViardiAMIFQEPSSCLDPS--EKV--GHQLIEAIPSysfEGRWWQRFKWRKKQAiALLHKVgiKDHsr 150
Cdd:PRK14247 77 VIEL----RRRV-----QMVFQIPNPIPNLSifENValGLKLNRLVKS---KKELQERVRWALEKA-QLWDEV--KDR-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 lMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK14247 140 -LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVA 216
|
250 260
....*....|....*....|....*
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK14247 217 FLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-247 |
2.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.12 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDLLQLT-PKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---------SGEIKIDGITiSKENLKEIRKKIGIIFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekvghQLI----EAIPSYSFEGRwwqRFKWRKKQAI--ALLHKVGIKDHsrlMDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK13632 95 ----------QFIgatvEDDIAFGLENK---KVPPKKMKDIidDLAKKVGMEDY---LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLL 247
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
2.60e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETpQGMVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLQL 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHG-QTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCI------NLleQPEAGTIRVGDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 79 TP----KERRRVIARDIAMIFQepSSCLDPSEKVGHQLIEAIPSYSFEGRwwqrfkwrkKQAIA----LLHKVGIKDHSr 150
Cdd:PRK11264 71 RSlsqqKGLIRQLRQHVGFVFQ--NFNLFPHRTVLENIIEGPVIVKGEPK---------EEATArareLLAKVGLAGKE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 lmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11264 139 --TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAI 215
|
250 260
....*....|....*....|....*
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK11264 216 FMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-255 |
3.78e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDR-MSLTLNEGEIRGLVGESGSGKSLVAKAI---VGVCKENWKVSADRMRLGNiDLLQLTPKERRRviarDIAMIFQ 96
Cdd:PRK14246 23 KAILKdITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKIKVDGKVLYFGK-DIFQIDAIKLRK----EVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 97 EPSScldpsekVGHQLIEAIPSYSFEGRWWQRFKWRKKQAIALLHKVGI--KDHSRLmDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK14246 98 QPNP-------FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkEVYDRL-NSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNqiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
.
gi 515646397 255 T 255
Cdd:PRK14246 248 T 248
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
4.97e-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: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEietpQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckENWKVSADRM-----RLGNIDL 75
Cdd:COG1119 1 DPLLELRNVTVR----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---DLPPTYGNDVrlfgeRRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 76 LQLtpkeRRR--VIARDIAMIFQEPSSCLDpsekvghqlieAIPS--YSFEGRWWQRFKWRKKQAIALLHKVGIKDhsrL 151
Cdd:COG1119 74 WEL----RKRigLVSPALQLRFPRDETVLD-----------VVLSgfFDSIGLYREPTDEQRERARELLELLGLAH---L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 152 MDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:COG1119 136 ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLL 215
|
.
gi 515646397 232 M 232
Cdd:COG1119 216 L 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-255 |
1.04e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 19 MVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK--ENWKVSADRMRLG-NIDLLQLTPKERRRviarDIAMIF 95
Cdd:PRK14267 19 VIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEARVEGEVRLFGrNIYSPDVDPIEVRR----EVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPSS----CLDPSEKVGHQLIEAIPSysfEGRWWQRFKWRKKQAiALLHKVgiKDhsRLMDsYSYELTDGECQKVMIAM 171
Cdd:PRK14267 92 QYPNPfphlTIYDNVAIGVKLNGLVKS---KKELDERVEWALKKA-ALWDEV--KD--RLND-YPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 172 AIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNqiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
....
gi 515646397 252 HPYT 255
Cdd:PRK14267 241 HELT 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-246 |
1.29e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPqgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:COG3845 256 VVLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL----RPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRviaRDIAMIfqepsscldPSEKVGHQLieaIPSYS--------------FEGRWWQRFKWRKKQAIALLHKVGIK- 146
Cdd:COG3845 329 ERRR---LGVAYI---------PEDRLGRGL---VPDMSvaenlilgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRt 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 147 -DHSRLMDSYSyeltDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQIL-RLLSRMNQinNTTIVLIGHDLTTITQ 224
Cdd:COG3845 394 pGPDTPARSLS----GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHqRLLELRDA--GAAVLLISEDLDEILA 467
|
250 260
....*....|....*....|....*..
gi 515646397 225 WATRITVMYCGQ-----SVESADTQKL 246
Cdd:COG3845 468 LSDRIAVMYEGRivgevPAAEATREEI 494
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-260 |
1.33e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKErrrvIARDIAMIFQEPsscL 102
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP----QSGTVFLGDKPISMLSSRQ----LARRLALLPQHH---L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 103 DPSEKVGHQLIE--AIPSYSFEGRWWQRFKWRKKQAIALLHKVGIKDHsRLMDsysyeLTDGECQKVMIAMAIAAKPKVL 180
Cdd:PRK11231 87 TPEGITVRELVAygRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADR-RLTD-----LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAdtqklldAPKHPYTVALLK 260
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLR 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-247 |
1.56e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETpQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENW---KVSADRMRLGNIDLLQlt 79
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEgkvKIDGELLTAENVWNLR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 80 pkerrrviaRDIAMIFQEPSScldpsEKVGhQLIEAIPSYSFEGRWWQRFKWRKKQAIALLHkvgikdhSRLMDSYSYE- 158
Cdd:PRK13642 81 ---------RKIGMVFQNPDN-----QFVG-ATVEDDVAFGMENQGIPREEMIKRVDEALLA-------VNMLDFKTREp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 --LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:PRK13642 139 arLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGE 217
|
250
....*....|.
gi 515646397 237 SVESADTQKLL 247
Cdd:PRK13642 218 IIKEAAPSELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-238 |
1.80e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.59 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrviARDIAMIFQepSSCLDPSEKVgHQLIE--AIPsysfegrwWQRFKWRKKQAI-ALLHKVGIkdhSRLMDSYSYE 158
Cdd:PRK13548 73 EL----ARRRAVLPQ--HSSLSFPFTV-EEVVAmgRAP--------HGLSRAEDDALVaAALAQVDL---AHLAGRDYPQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIA------AKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:PRK13548 135 LSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLL 214
|
....*.
gi 515646397 233 YCGQSV 238
Cdd:PRK13548 215 HQGRLV 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-248 |
2.82e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsadrmrL----GNIDLLQLTPKERRRVIARDIAMIF 95
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI-------------LvptsGEVRVLGYVPFKRRKEFARRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 qepsscldpsekvGH--QL---IEAIPSYSFEGRWW----QRFKWRKKQAIALLhkvGIKDhsrLMDSYSYELTDGECQK 166
Cdd:COG4586 102 -------------GQrsQLwwdLPAIDSFRLLKAIYripdAEYKKRLDELVELL---DLGE---LLDTPVRQLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 167 VMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
..
gi 515646397 247 LD 248
Cdd:COG4586 243 KE 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-250 |
4.47e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKaIVGvckENWKVSADRMRLGNIDLLQLTPKerrrVIARDIAMIFQEpsscLDPS 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLG---RHQPPSEGEILLDAQPLESWSSK----AFARKVAYLPQQ----LPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 106 EKVGHQLIEAIPSYSFEG---RWWQRFKWRKKQAIALlhkVGIKD-HSRLMDSysyeLTDGECQKVMIAMAIAAKPKVLI 181
Cdd:PRK10575 98 EGMTVRELVAIGRYPWHGalgRFGAADREKVEEAISL---VGLKPlAHRLVDS----LSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 182 ADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-255 |
5.49e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvCKENWKVSADRMRlGNIDLLQLTPKERRRVIA--RDIAMIFQEPS- 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTL---NRMNDKVSGYRYS-GDVLLGGRSIFNYRDVLEfrRRVGMLFQRPNp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 ---SCLDpSEKVGHQLIEAIPSYSFEGrwwqrfkwrkkQAIALLHKVGIKD--HSRLMDSySYELTDGECQKVMIAMAIA 174
Cdd:PRK14271 113 fpmSIMD-NVLAGVRAHKLVPRKEFRG-----------VAQARLTEVGLWDavKDRLSDS-PFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMnqINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
.
gi 515646397 255 T 255
Cdd:PRK14271 258 T 258
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-241 |
6.70e-17 |
|
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: 78.03 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIARdIAMIFQE 97
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL------IKPDS---GEITFDGKSYQKNIEALRR-IGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSscLDPSEKVGHQLieaipsysfegRWWQRFKWRKKQAI-ALLHKVGIKDH-SRLMDSYSYeltdGECQKVMIAMAIAA 175
Cdd:cd03268 81 PG--FYPNLTARENL-----------RLLARLLGIRKKRIdEVLDVVGLKDSaKKKVKGFSL----GMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 176 KPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-238 |
7.21e-17 |
|
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: 78.09 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE---------NWKVSADRMRLGNIdllqltPKERRrvia 88
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdsgevlfdgKPLDIAARNRIGYL------PEERG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 89 rdiamifqepsscLDPSEKVGHQLIeaipsysfegrWWQRFKWRKKQAIA-----LLHKVGIKDH--SRLMdsysyELTD 161
Cdd:cd03269 81 -------------LYPKMKVIDQLV-----------YLAQLKGLKKEEARrrideWLERLELSEYanKRVE-----ELSK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQ---SQILRLLSRmnqiNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVellKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-286 |
8.25e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQgmvkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KErrrviaRDIAMIFQepSSCLDPsekvgHQLIEAIPSYSFEGRWWQR--FKWRKKQAIALLHkvgikdhsrlMDSYS-- 156
Cdd:PRK11607 89 YQ------RPINMMFQ--SYALFP-----HMTVEQNIAFGLKQDKLPKaeIASRVNEMLGLVH----------MQEFAkr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 157 --YELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPI----TQSQILRLLSRMnqinNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11607 146 kpHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 231 VMYCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEK----LQSlPGSIPPLQ 286
Cdd:PRK11607 222 IMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEdglvIDS-PGLVHPLK 280
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-251 |
8.81e-17 |
|
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: 78.05 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRrviardIAMIFQe 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLPPHKRP------VNTVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 pSSCLDPSEKVGHQLieAIPsysfegrwwQRFKWRKKQAIA-----LLHKVGIKDHSRLMDSysyELTDGECQKVMIAMA 172
Cdd:cd03300 80 -NYALFPHLTVFENI--AFG---------LRLKKLPKAEIKervaeALDLVQLEGYANRKPS---QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 173 IAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-261 |
9.66e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.87 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERrrviarDIAMIFQE------- 97
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLTALPPAER------PVSMLFQEnnlfphl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 -----------PSSCLDPSEKvghqlieaipsysfegrwwqrfkwrkKQAIALLHKVGIKDhsrLMDSYSYELTDGECQK 166
Cdd:COG3840 87 tvaqniglglrPGLKLTAEQR--------------------------AQVEQALERVGLAG---LLDRLPGQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 167 VMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|....*
gi 515646397 247 LDAPKHPYTVALLKA 261
Cdd:COG3840 218 LDGEPPPALAAYLGI 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-247 |
1.49e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKS-----LVAKAIVGVCKENW-------KVSADRMRLGNIDLLQLTPKERR---- 84
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEKLVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 85 RVIARDIAMIFQEPSscldpsekvgHQLIEA-------IPSYSFeGRWWQRFKWRKKQAIALlhkVGIkDHSRLMDSySY 157
Cdd:PRK13651 101 KEIRRRVGVVFQFAE----------YQLFEQtiekdiiFGPVSM-GVSKEEAKKRAAKYIEL---VGL-DESYLQRS-PF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 158 ELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQS 237
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
250
....*....|
gi 515646397 238 VESADTQKLL 247
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
1.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.25 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNidllQLTPKERRRVIARDIAMIFQEPSSc 101
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----EKVKSGEIFYNN----QAITDDNFEKLRKHIGIVFQNPDN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 102 ldpsekvghQLIEAIPSYSFE-GRWWQRFKWRKKQAIA--LLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:PRK13648 95 ---------QFVGSIVKYDVAfGLENHAVPYDEMHRRVseALKQVDMLERA---DYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLT 220
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-219 |
2.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.92 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLgNIDLLQLTPKER 83
Cdd:PRK13640 6 VEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPD---DNPNSKI-TVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARdIAMIFQEPSScldpsEKVGHQLIEAIpSYSFEGRWWQRFKwRKKQAIALLHKVGIKDHsrlMDSYSYELTDGE 163
Cdd:PRK13640 80 WDIREK-VGIVFQNPDN-----QFVGATVGDDV-AFGLENRAVPRPE-MIKIVRDVLADVGMLDY---IDSEPANLSGGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDL 219
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-257 |
2.07e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.96 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKErrrviaRDIAMIFQEPS 99
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL--E--DPTSGEILIGGRDVTDLPPKD------RNIAMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scLDPS----EKVGHQLieaipsysfegrwwqrfKWRK--KQAIA-----LLHKVGIKDhsrLMDSYSYELTDGECQKVM 168
Cdd:COG3839 86 --LYPHmtvyENIAFPL-----------------KLRKvpKAEIDrrvreAAELLGLED---LLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 169 IAMAIAAKPKVLIADEPTNDLDP----ITQSQILRLLSRMnqinNTTIVLIGHDLT---TItqwATRITVMYCGQSVESA 241
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL----GTTTIYVTHDQVeamTL---ADRIAVMNDGRIQQVG 216
|
250
....*....|....*.
gi 515646397 242 DTQKLLDAPKHPYtVA 257
Cdd:COG3839 217 TPEELYDRPANLF-VA 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
2.15e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KErrrvIARDIAMIFQEPSSCLDPSekvGHQLIEA--IPSYSFEGRWWQRFKWRKKQAIAllhKVGIkdhSRLMDSYSYE 158
Cdd:PRK09536 73 RA----ASRRVASVPQDTSLSFEFD---VRQVVEMgrTPHRSRFDTWTETDRAAVERAME---RTGV---AQFADRPVTS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIgHDL 219
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDL 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-236 |
3.04e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQltpKERRrviardiamiFQEPS 99
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI------YTRDA---GSILYLG---KEVT----------FNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 ScldpSEKVG----HQLIEAIPSYS-----FEGR----WWQRFKWRK--KQAIALLHKVGIKDHSRLMDSysyELTDGEC 164
Cdd:PRK10762 75 S----SQEAGigiiHQELNLIPQLTiaeniFLGRefvnRFGRIDWKKmyAEADKLLARLNLRFSSDKLVG---ELSIGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 165 QKVMIAMAIAAKPKVLIADEPTndlDPITQSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPT---DALTDTETESLFRVIRELksQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-249 |
3.15e-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: 76.76 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGV-CKENWKVSADRMRLGNIDLLQLtpkeRRRV-------------I 87
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWL----RRQVgvvlqenvlfnrsI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 88 ARDIAMIFQEPsscldPSEKV--------GHQLIEAIPsysfEGrwwqrfkwrkkqaiallhkvgikdHSRLMDSYSYEL 159
Cdd:cd03252 93 RDNIALADPGM-----SMERVieaaklagAHDFISELP----EG------------------------YDTIVGEQGAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 160 TDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRllsRMNQI-NNTTIVLIGHDLTTITQwATRITVMYCGQSV 238
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMR---NMHDIcAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
|
250
....*....|.
gi 515646397 239 ESADTQKLLDA 249
Cdd:cd03252 216 EQGSHDELLAE 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
4.10e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPqgmvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADrmrlGNIDLLQLTP 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVE----GRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERR---RVIARDIAMIFQEPSscLDPsekvghqlieaIPSYSFEGRWWQRFKWRKKQAIALLHKVGIKDhSRLMDSYSY 157
Cdd:PRK14258 77 YERRvnlNRLRRQVSMVHPKPN--LFP-----------MSVYDNVAYGVKIVGWRPKLEIDDIVESALKD-ADLWDEIKH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 158 -------ELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQwATRIT 230
Cdd:PRK14258 143 kihksalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR-LSDFT 221
|
250 260
....*....|....*....|....*.
gi 515646397 231 VMY------CGQSVESADTQKLLDAP 250
Cdd:PRK14258 222 AFFkgnenrIGQLVEFGLTKKIFNSP 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-243 |
4.42e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKS-LVaKAIVGVckenwkVSADRmrlGNIdLL---QLTPKERRRVIARDIAMIF 95
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKStLM-KILYGL------YQPDS---GEI-LIdgkPVRIRSPRDAIALGIGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPSscldpsekvghqLIEaipsySF----------EGRWWQRFKWRK--KQAIALLHKVGIK-DhsrlMDSYSYELTDG 162
Cdd:COG3845 87 QHFM------------LVP-----NLtvaenivlglEPTKGGRLDRKAarARIRELSERYGLDvD----PDAKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLdpiTQSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRLaaEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
...
gi 515646397 241 ADT 243
Cdd:COG3845 223 VDT 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-248 |
5.36e-16 |
|
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: 75.55 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERrrvIARDIAMIFQE 97
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL----LPPRSGSIRFDGRDITGLPPHER---ARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PssCLDPSEKVGHQLIEAIpsysfEGRWWQRFKWRKKQAIALLhkvgikdhSRL---MDSYSYELTDGECQKVMIAMAIA 174
Cdd:cd03224 84 R--RIFPELTVEENLLLGA-----YARRRAKRKARLERVYELF--------PRLkerRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQInNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-247 |
6.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMrlgnIDLLQLTPkE 82
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQII----IDGDLLTE-E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIARDIAMIFQEPSScldpsEKVGhQLIEAIPSYSFE--GRWWQRFKWRKKQAIALlhkVGIKDhsrLMDSYSYELT 160
Cdd:PRK13650 75 NVWDIRHKIGMVFQNPDN-----QFVG-ATVEDDVAFGLEnkGIPHEEMKERVNEALEL---VGMQD---FKEREPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITqWATRITVMYCGQsVES 240
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VES 220
|
....*..
gi 515646397 241 ADTQKLL 247
Cdd:PRK13650 221 TSTPREL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-255 |
7.98e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAI--VGVCKENWKVSADRMRLG-NIdllqL 78
Cdd:PRK14239 4 PILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGhNI----Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 79 TPKERRRVIARDIAMIFQEPS----SCLD--------PSEKVGHQLIEAIPSYSFEGRWWQRfkwrkkqaiallhkvgIK 146
Cdd:PRK14239 76 SPRTDTVDLRKEIGMVFQQPNpfpmSIYEnvvyglrlKGIKDKQVLDEAVEKSLKGASIWDE----------------VK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 147 DhsRLMDSySYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLsrMNQINNTTIVLIGHDLTTITQWA 226
Cdd:PRK14239 140 D--RLHDS-ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRIS 214
|
250 260
....*....|....*....|....*....
gi 515646397 227 TRITVMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK14239 215 DRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-254 |
9.24e-16 |
|
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: 75.45 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 9 LTIEIETPQ---GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERrr 85
Cdd:cd03296 1 MSIEVRNVSkrfGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD----SGTILFGGEDATDVPVQER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 86 viarDIAMIFQEPS--SCLDPSEKVGHQL-IEAIPSYSFEGRwwqrfkwRKKQAIALLHKVGIkdhSRLMDSYSYELTDG 162
Cdd:cd03296 75 ----NVGFVFQHYAlfRHMTVFDNVAFGLrVKPRSERPPEAE-------IRAKVHELLKLVQL---DWLADRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
250
....*....|..
gi 515646397 243 TQKLLDAPKHPY 254
Cdd:cd03296 221 PDEVYDHPASPF 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-219 |
1.11e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 77.07 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTI--------------------EIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeN 60
Cdd:COG4175 1 MPKIEVRNLYKifgkrperalklldqgkskdEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCL------N 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 61 --WKVSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQepSSCLDP----SEKVGHQL-IEAIPSysfegrwwqrfKWRK 133
Cdd:COG4175 75 rlIEPTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQ--HFALLPhrtvLENVAFGLeIQGVPK-----------AERR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 134 KQAIALLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPIT----QSQILRLLSRMNQinn 209
Cdd:COG4175 142 ERAREALELVGLAGWE---DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIrremQDELLELQAKLKK--- 215
|
250
....*....|
gi 515646397 210 tTIVLIGHDL 219
Cdd:COG4175 216 -TIVFITHDL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-242 |
1.11e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.43 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWK-------VSADRMRLGNIDLLQLTPKERR-RVIARDI 91
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiYIGDKKNNHELITNPYSKKIKNfKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 92 AMIFQEPSSCL--DPSEK--------VGHQLIEAipsysfegrwwqrfkwrKKQAIALLHKVGIKDhsRLMDSYSYELTD 161
Cdd:PRK13631 119 SMVFQFPEYQLfkDTIEKdimfgpvaLGVKKSEA-----------------KKLAKFYLNKMGLDD--SYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
.
gi 515646397 242 D 242
Cdd:PRK13631 259 T 259
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-250 |
1.12e-15 |
|
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: 76.68 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkvsAD--RMRLGNiDLLQLT------PKERRRviardIAMIFQEP 98
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLER------PDsgRIRLGG-EVLQDSargiflPPHRRR-----IGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 SscLDPSEKVGHQLIEAipsYSFEGRWWQRFKWRkkQAIALLhkvGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:COG4148 87 R--LFPHLSVRGNLLYG---RKRAPRAERRISFD--EVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-240 |
1.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.55 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP----TQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekvghQLIE--AIPSYSFEGrwwQRFKWRKKQAIAL----LHKVGIKDHsrLMDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK13649 97 ----------QLFEetVLKDVAFGP---QNFGVSQEEAEALarekLALVGISES--LFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-257 |
1.63e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.67 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSADRMRLgNI-----DLLQLTPKERRRVIARDIAMIFQEPSsc 101
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVL------NLLEMPRSGTL-NIagnhfDFSKTPSDKAIRELRRNVGMVFQQYN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 102 LDPSEKVGHQLIEA---IPSYSFEGRwwqrfkwrKKQAIALLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:PRK11124 93 LWPHLTVQQNLIEApcrVLGLSKDQA--------LARAEKLLERLRLKPYA---DRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTqkllDAPKHPYTVA 257
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTEA 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-217 |
1.76e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 24 DRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkvsaDRMRLGNIDLLQLTPkerrrviardiamifqepsscld 103
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-------GTPVAGCVDVPDNQF----------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 104 PSEKVghqLIEAIPSysfegrwwqrfKWRKKQAIALLHKVGIKDHSRLMDSYSyELTDGECQKVMIAMAIAAKPKVLIAD 183
Cdd:COG2401 97 GREAS---LIDAIGR-----------KGDFKDAVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....
gi 515646397 184 EPTNDLDPITQSQILRLLSRMNQINNTTIVLIGH 217
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-235 |
2.46e-15 |
|
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: 73.94 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQlTPKE 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP----DAGFATVDGFDVVK-EPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRRVIArdiamiFQEPSSCLDPSEKVGHQLIEAIPSYSFEGrwwQRFKWRKKQAIALLhkvGIKDhsrLMDSYSYELTDG 162
Cdd:cd03266 76 ARRRLG------FVSDSTGLYDRLTARENLEYFAGLYGLKG---DELTARLEELADRL---GMEE---LLDRRVGGFSTG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 163 ECQKVMIAMAIAAKPKVLIADEPTNDLDpITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:cd03266 141 MRQKVAIARALVHDPPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-251 |
2.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP----SSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CLdpSEKVGHQLIEAIP-SYSFEGrwwqrfKWRKKQAIALLHKVGIKDHsrLMDSYSYELTDGECQKVMIAMAIAAKPKV 179
Cdd:PRK13641 97 QL--FENTVLKDVEFGPkNFGFSE------DEAKEKALKWLKKVGLSED--LISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 180 LIADEPTNDLDPITQSQILRLLSRMnQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-236 |
3.77e-15 |
|
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: 73.73 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPSS 100
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGKILLDGQDITKLPMHKRAR---LGIGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CLDPSEKvghQLIEAIpsysFEGRWWQRFKWRKKqAIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:cd03218 87 FRKLTVE---ENILAV----LEIRGLSKKEREEK-LEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-238 |
5.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP----TEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekvghQLIE--AIPSYSFEGrwwQRFKWRKKQAIAL----LHKVGIKdhSRLMDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK13643 96 ----------QLFEetVLKDVAFGP---QNFGIPKEKAEKIaaekLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-236 |
5.46e-15 |
|
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: 71.86 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPKERRRVI---ARDIAMifqeps 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILG----LLRPTSGRVRLDGADISQWDPNELGDHVgylPQDDEL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scLDPSekvghqLIEAIpsysfegrwwqrfkwrkkqaiallhkvgikdhsrlmdsysyeLTDGECQKVMIAMAIAAKPKV 179
Cdd:cd03246 88 --FSGS------IAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 180 LIADEPTNDLDPITQSQILRLLSRMnQINNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-249 |
8.91e-15 |
|
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: 72.65 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvcKENWKVSADRMRLGNIDLLQLTPKERRR--------------V 86
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYDVDSGRILIDGHDVRDYTLASLRRqiglvsqdvflfndT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 87 IARDIAmiFQEPSSCLDPSEKVG-----HQLIEAIPsysfEGrwwqrfkwrkkqaialLHKV----GIKdhsrlmdsysy 157
Cdd:cd03251 92 VAENIA--YGRPGATREEVEEAAraanaHEFIMELP----EG----------------YDTVigerGVK----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 158 eLTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVlIGHDLTTITQwATRITVMYCGQS 237
Cdd:cd03251 139 -LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFV-IAHRLSTIEN-ADRIVVLEDGKI 214
|
250
....*....|..
gi 515646397 238 VESADTQKLLDA 249
Cdd:cd03251 215 VERGTHEELLAQ 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-218 |
1.08e-14 |
|
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: 71.30 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 17 QGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRL--GNIDLLQLtpkeRRRViardiAM 93
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGEPLdySRKGLLER----RQRV-----GL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 94 IFQEPSSCL---DPSEKVGHQLIEAipsysfeGRWWQRFKWRKKQAIALLhkvgikDHSRLMDSYSYELTDGECQKVMIA 170
Cdd:TIGR01166 73 VFQDPDDQLfaaDVDQDVAFGPLNL-------GLSEAEVERRVREALTAV------GASGLRERPTHCLSGGEKKRVAIA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515646397 171 MAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHD 218
Cdd:TIGR01166 140 GAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRA-EGMTVVISTHD 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-237 |
1.75e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEietpqGMVKavdrMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK15439 267 PVLTVEDLTGE-----GFRN----ISLEVRAGEILGLAGVVGAGRTELAETLYGL----RPARGGRIMLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrvIARDIAMIfqepsscldPSEKVGHQL-IEA-----IPSYSFEGR-WWQRfkwRKKQAiALL----HKVGIK-DHS 149
Cdd:PRK15439 334 QR---LARGLVYL---------PEDRQSSGLyLDAplawnVCALTHNRRgFWIK---PAREN-AVLeryrRALNIKfNHA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 150 rlmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRI 229
Cdd:PRK15439 398 ---EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRV 473
|
....*...
gi 515646397 230 TVMYCGQS 237
Cdd:PRK15439 474 LVMHQGEI 481
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-248 |
1.79e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.46 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQepss 100
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI----YLPQRGRVKVMGREVNAENEKWVRS----KVGLVFQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 clDPSEKVghqlieaipsysFEGRWWQ-----------RFKWRKKQAIALLHKVGIKDhsrLMDSYSYELTDGECQKVMI 169
Cdd:PRK13647 87 --DPDDQV------------FSSTVWDdvafgpvnmglDKDEVERRVEEALKAVRMWD---FRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 170 AMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-245 |
1.94e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADrmrlGNIDLlqltpkERRRVIARDIAmifqeps 99
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHG---SYE----GEILF------DGEVCRFKDIR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scldPSEKVG----HQLIEAIPSYS-----FEGRWWQRFK---WRK--KQAIALLHKVGIKDH--SRLMDsysyeLTDGE 163
Cdd:NF040905 74 ----DSEALGiviiHQELALIPYLSiaeniFLGNERAKRGvidWNEtnRRARELLAKVGLDESpdTLVTD-----IGVGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPT---NDLDpitqSQ-ILRLLSRMNQINNTTIvLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTaalNEED----SAaLLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLRDGRTIE 219
|
....*.
gi 515646397 240 SADTQK 245
Cdd:NF040905 220 TLDCRA 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-251 |
3.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.59 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNiDLLQLTPKERR-RVIARDIAMIFQEPSscldps 105
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP----TSGTVTIGE-RVITAGKKNKKlKPLRKKVGIVFQFPE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 106 ekvgHQLIE-------AIPSYSFeGRWWQRFKWRKKQAIALlhkVGIkDHSrLMDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:PRK13634 96 ----HQLFEetvekdiCFGPMNF-GVSEEDAKQKAREMIEL---VGL-PEE-LLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVES-------ADTQKL----L 247
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQgtpreifADPDELeaigL 245
|
....
gi 515646397 248 DAPK 251
Cdd:PRK13634 246 DLPE 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-238 |
3.92e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.66 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG-VCKENWKVSADRMRLGNIdllqltpkERRRVIARDIAMIFQEPSS 100
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAlLIPSEGKVYVDGLDTSDE--------ENLWDIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekvghQLIEAIP----SYSFEGRWWQRFKWRKKQAIALlHKVGI---KDHSRLMdsysyeLTDGECQKVMIAMAI 173
Cdd:PRK13633 97 ----------QIVATIVeedvAFGPENLGIPPEEIRERVDESL-KKVGMyeyRRHAPHL------LSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQwATRITVMYCGQSV 238
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-254 |
6.09e-14 |
|
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: 69.48 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIETpqgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckENWKVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRviaRDIAMIFQEPsscldpsekvghqliEAIPSysfegrwwqrfkwrkkqaiallhkVGIKDHSRLMDsysYELTDGE 163
Cdd:cd03217 75 AR---LGIFLAFQYP---------------PEIPG------------------------VKNADFLRYVN---EGFSGGE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHD---LTTITqwATRITVMYCGQSVES 240
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKS 186
|
250
....*....|....
gi 515646397 241 ADTQKLLDAPKHPY 254
Cdd:cd03217 187 GDKELALEIEKKGY 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-245 |
9.27e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.06 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKaIVGvCKEnwKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG-CLD--KPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRVIARDIAMIFQEPS--SCLDPSEKVghqlieAIPS-YSFEGRwwqrfKWRKKQAIALLHKVGIKDHsrlMDSYSYE 158
Cdd:PRK10535 79 ALAQLRREHFGFIFQRYHllSHLTAAQNV------EVPAvYAGLER-----KQRLLRAQELLQRLGLEDR---VEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVlIGHDlTTITQWATRITVMYCGQSV 238
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGEIV 222
|
....*..
gi 515646397 239 ESADTQK 245
Cdd:PRK10535 223 RNPPAQE 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-240 |
9.38e-14 |
|
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: 68.49 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIetPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSadrmrLGNIDLLQLTPKER 83
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG----DLKPQ-----QGEITLDGVPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARDIAMIFQEPsscldpsekvghqlieaipsYSFEGrwwqrfkwrkkqaiALLHKVGIKdhsrlmdsysyeLTDGE 163
Cdd:cd03247 70 EKALSSLISVLNQRP--------------------YLFDT--------------TLRNNLGRR------------FSGGE 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLsrMNQINNTTIVLIGHDLTTITQwATRITVMYCGQSVES 240
Cdd:cd03247 104 RQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-255 |
1.07e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNwkvsadRM------------- 68
Cdd:COG1117 10 PKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL------N------RMndlipgarvegei 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 69 RLGNIDLLQLT---PKERRRViardiAMIFQEP----------------------SSCLDpsEKVGHQLieaipsysfeg 123
Cdd:COG1117 74 LLDGEDIYDPDvdvVELRRRV-----GMVFQKPnpfpksiydnvayglrlhgiksKSELD--EIVEESL----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 124 rwwqrfkwrkKQAiALLHKVgiKDhsRLMDSySYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSR 203
Cdd:COG1117 136 ----------RKA-ALWDEV--KD--RLKKS-ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 204 MNQinNTTIVLIGHDLttitQWATRIT----VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:COG1117 200 LKK--DYTIVIVTHNM----QQAARVSdytaFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-200 |
1.85e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.28 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEIETpQGMVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAdRMRLGNIDLLQLtPKER 83
Cdd:COG4136 2 LSLENLTITLGG-RPLLAPLS---LTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASG-EVLLNGRRLTAL-PAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRviardIAMIFQEPssCLDPSEKVGHQLIEAIPSySFEGRwwqrfkWRKKQAIALLHKVGIKDHSrlmDSYSYELTDGE 163
Cdd:COG4136 76 RR-----IGILFQDD--LLFPHLSVGENLAFALPP-TIGRA------QRRARVEQALEEAGLAGFA---DRDPATLSGGQ 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 515646397 164 CQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRL 200
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-251 |
1.92e-13 |
|
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: 68.84 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPSs 100
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD----AGKILIDGQDITHLPMHERAR---LGIGYLPQEAS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cldpsekVGHQL-----IEAIpsysFEGRWWQRFKWRKKQAIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAA 175
Cdd:TIGR04406 87 -------IFRKLtveenIMAV----LEIRKDLDRAEREERLEALLEEFQI---SHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 176 KPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-249 |
2.29e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 38 LVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTpkerRRVIARDIAMIFQEPSSCLDP---SEKVGHQLIE 114
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMG----YYPLTEGEIRLDGRPLSSLS----HSVLRQGVAMVQQDPVVLADTflaNVTLGRDISE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 115 AipsysfegRWWQRFKwrKKQAIALLHKV--GIkdHSRLMDSYSyELTDGecQKVMIAMA--IAAKPKVLIADEPTNDLD 190
Cdd:PRK10790 444 E--------QVWQALE--TVQLAELARSLpdGL--YTPLGEQGN-NLSVG--QKQLLALArvLVQTPQILILDEATANID 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 191 PITQSQILRLLSRMNQinNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK10790 509 SGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-236 |
2.36e-13 |
|
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: 67.99 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGeIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSs 100
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLT---------PPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cLDPSEKVGHQL-----IEAIPSysfegrwwqrfKWRKKQAIALLHKVGIKDH-SRLMDSYSyeltDGECQKVMIAMAIA 174
Cdd:cd03264 83 -VYPNFTVREFLdyiawLKGIPS-----------KEVKARVDEVLELVNLGDRaKKKIGSLS----GGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-242 |
2.97e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSADRMRLgNI-----DLLQLTPKERRRVIARDIA 92
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL------NLLETPDSGQL-NIaghqfDFSQKPSEKAIRLLRQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 93 MIFQEPSscLDPSEKVGHQLIEAiPSysfegrwwQRFKWRKKQAIA----LLHKVGIKDHSrlmDSYSYELTDGECQKVM 168
Cdd:COG4161 86 MVFQQYN--LWPHLTVMENLIEA-PC--------KVLGLSKEQAREkamkLLARLRLTDKA---DRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 169 IAMAIAAKPKVLIADEPTNDLDPITQSQILRLLsrmNQINNTTI--VLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEII---RELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-229 |
3.66e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckeNWKVSADRMRLGNiDLLQLTPK 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQ-PMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRVIARDIAMIFQEPSSCLDPS--EKVGHQLI--EAIPSYSfegrwwqrfkwrKKQAIALLHKVGIKDHSRLMDSysy 157
Cdd:PRK11629 80 AKAELRNQKLGFIYQFHHLLPDFTalENVAMPLLigKKKPAEI------------NSRALEMLAAVGLEHRANHRPS--- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 158 ELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLttitQWATRI 229
Cdd:PRK11629 145 ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-246 |
4.05e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWK----VSADRMRLGNIdl 75
Cdd:PRK13549 3 EYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgTYEgeiiFEGEELQASNI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 76 lqltpkerRRVIARDIAMIFQEPSscLDPSEKVGhqliEAIpsysFEGRWWQRFK---WRK--KQAIALLHKVG--IKDH 148
Cdd:PRK13549 77 --------RDTERAGIAIIHQELA--LVKELSVL----ENI----FLGNEITPGGimdYDAmyLRAQKLLAQLKldINPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 149 SRLMDsysyeLTDGECQKVMIAMAIAAKPKVLIADEPTNDLdpiTQSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWA 226
Cdd:PRK13549 139 TPVGN-----LGLGQQQLVEIAKALNKQARLLILDEPTASL---TESETAVLLDIIRDLkaHGIACIYISHKLNEVKAIS 210
|
250 260
....*....|....*....|
gi 515646397 227 TRITVMYCGQSVESADTQKL 246
Cdd:PRK13549 211 DTICVIRDGRHIGTRPAAGM 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-204 |
7.09e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPSS 100
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD----AGNIIIDDEDISLLPLHARAR---RGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CLDPSekVGHQLIEAIpsysfEGRWWQRFKWRKKQAIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:PRK10895 90 FRRLS--VYDNLMAVL-----QIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180
....*....|....*....|....
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRM 204
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-249 |
8.03e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEietpqGMVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPK 81
Cdd:COG1129 255 VVLEVEGLSVG-----GVVRDV---SFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrvIARDIAMIfqepsscldPSEKVGHQLIE--------AIPSY-SFEGRWWQRFKWRKKQAIALLHKVGIK--DHSR 150
Cdd:COG1129 323 DA---IRAGIAYV---------PEDRKGEGLVLdlsireniTLASLdRLSRGGLLDRRRERALAEEYIKRLRIKtpSPEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDSysyeLTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRIT 230
Cdd:COG1129 391 PVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRIL 465
|
250 260
....*....|....*....|....
gi 515646397 231 VMYCGQSV-----ESADTQKLLDA 249
Cdd:COG1129 466 VMREGRIVgeldrEEATEEAIMAA 489
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-247 |
8.18e-13 |
|
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: 66.79 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvcKENWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQEP- 98
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL----ERFYDPTSGEILLDGVDIRDLNLRWLRS----QIGLVSQEPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 ----------SSCLDPSEKVghQLIEAIpsysfegrwwqrfkwrkKQAIAllHKVGIKdhsrLMDSYSYE-------LTD 161
Cdd:cd03249 88 lfdgtiaeniRYGKPDATDE--EVEEAA-----------------KKANI--HDFIMS----LPDGYDTLvgergsqLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMnqINNTTIVLIGHDLTTItQWATRITVMYCGQSVESA 241
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
....*.
gi 515646397 242 DTQKLL 247
Cdd:cd03249 220 THDELM 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-232 |
8.90e-13 |
|
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: 66.36 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenWKVSAD-RMRLGNIDLLQLTPKERrrviarDIAMIFQEPS--SC 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAG-----FETPQSgRVLINGVDVTAAPPADR------PVSMLFQENNlfAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 102 LDPSEKVGHQLIEAIpsysfegrwwqRFKWRKKQAI-ALLHKVGIKDhsrLMDSYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:cd03298 85 LTVEQNVGLGLSPGL-----------KLTAEDRQAIeVALARVGLAG---LEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-238 |
1.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 67.18 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGN--IDLLQLTPKERRRviarDIAMIFQEPS 99
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP----SSGRILFDGkpIDYSRKGLMKLRE----SVGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scldpsekvgHQLIEA--IPSYSFEGRWWQRFKWR-KKQAIALLHKVGIkdhSRLMDSYSYELTDGECQKVMIAMAIAAK 176
Cdd:PRK13636 93 ----------NQLFSAsvYQDVSFGAVNLKLPEDEvRKRVDNALKRTGI---EHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515646397 177 PKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
22-235 |
1.79e-12 |
|
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: 65.88 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVC-KENWKVSAD-----RMRLGNIDLLQLTPKERRRVIARDiamif 95
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILrPTSGEIIFDghpwtRKDLHKIGSLIESPPLYENLTARE----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 qepsscldpSEKVgHQLIEAIPSYSFEgrwwqrfkwrkkqaiALLHKVGIKDHSRlmdSYSYELTDGECQKVMIAMAIAA 175
Cdd:TIGR03740 90 ---------NLKV-HTTLLGLPDSRID---------------EVLNIVDLTNTGK---KKAKQFSLGMKQRLGIAIALLN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 176 KPKVLIADEPTNDLDPITqSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIG-IQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
2.53e-12 |
|
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: 67.39 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQgmvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:TIGR02868 333 PTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL----LDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRVIArdiamIFQEPSSCLDPSekVGHQLIEAIPSYSFEGRWWqrfkwrkkqaiaLLHKVGIKDHSR-LMDSYSYELT 160
Cdd:TIGR02868 406 EVRRRVS-----VCAQDAHLFDTT--VRENLRLARPDATDEELWA------------ALERVGLADWLRaLPDGLDTVLG 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 161 D-------GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDL 219
Cdd:TIGR02868 467 EggarlsgGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-243 |
2.68e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.65 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 9 LTIEIETPQ---GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRr 85
Cdd:PRK10851 1 MSIEIANIKksfGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRLHARDRK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 86 viardIAMIFQEPS---------------SCLDPSEKVGHQLIeaipsysfegrwwqrfkwrKKQAIALLHKVGIkdhSR 150
Cdd:PRK10851 76 -----VGFVFQHYAlfrhmtvfdniafglTVLPRRERPNAAAI-------------------KAKVTQLLEMVQL---AH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK10851 129 LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
250
....*....|...
gi 515646397 231 VMYCGqSVESADT 243
Cdd:PRK10851 209 VMSQG-NIEQAGT 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-239 |
3.62e-12 |
|
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: 64.82 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADR--MRLGNIDLLQLTPKE-RRRviardIAMIFQEP----- 98
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSLLLALFRL------VELSSgsILIDGVDISKIGLHDlRSR-----ISIIPQDPvlfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 --SSCLDPSEKvghqlieaipsYSFEGRWwqrfkwrkkQAialLHKVGIKDH-SRLMDSYSYELTDGEC-------QKVM 168
Cdd:cd03244 93 tiRSNLDPFGE-----------YSDEELW---------QA---LERVGLKEFvESLPGGLDTVVEEGGEnlsvgqrQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 169 IAMAIAAKPKVLIADEPTNDLDPITQSQILRLLsrMNQINNTTIVLIGHDLTTITQwATRITVMYCGQSVE 239
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-239 |
3.90e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG--VCKENWKVSADRMRLGNIDLLqltpKERRRvIARDIAMIFQEP 98
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliISETGQTIVGDYAIPANLKKI----KEVKR-LRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 SSCL--DPSEKVghqlIEAIPSYSFEGRwwqrfKWRKKQAIALLHKVGI-KDHSRlmdSYSYELTDGECQKVMIAMAIAA 175
Cdd:PRK13645 100 EYQLfqETIEKD----IAFGPVNLGENK-----QEAYKKVPELLKLVQLpEDYVK---RSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 176 KPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-250 |
5.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 6 IRHLTIEIETPQGmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRLGNIDLLQltpkERR 84
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIDTGDFSKLQ----GIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 85 RViardIAMIFQEPSscldpSEKVGHQLIEAIpSYSFEGRWWQRFKWRKKQAIALLhKVGikdhsrlMDSYSYE----LT 160
Cdd:PRK13644 77 KL----VGIVFQNPE-----TQFVGRTVEEDL-AFGPENLCLPPIEIRKRVDRALA-EIG-------LEKYRHRspktLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 161 DGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTItQWATRITVMYCGQSVES 240
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
250
....*....|
gi 515646397 241 ADTQKLLDAP 250
Cdd:PRK13644 217 GEPENVLSDV 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
132-240 |
8.65e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.71 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 132 RKKQAialLHKVGIKDHSRlmdSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTT 211
Cdd:PRK13639 117 RVKEA---LKAVGMEGFEN---KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGIT 189
|
90 100
....*....|....*....|....*....
gi 515646397 212 IVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK13639 190 IIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
8.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.44 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTieiETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGNidllQLTp 80
Cdd:PRK13652 1 MHLIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT---SGSVLIRGE----PIT- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQEPSS------------------CLDpSEKVGHQLIEAipsysfegrwwqrfkwrkkqaialLHK 142
Cdd:PRK13652 70 KENIREVRKFVGLVFQNPDDqifsptveqdiafgpinlGLD-EETVAHRVSSA------------------------LHM 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 143 VGIKDhsrLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTI 222
Cdd:PRK13652 125 LGLEE---LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLV 201
|
250 260
....*....|....*....|....*...
gi 515646397 223 TQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:PRK13652 202 PEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-217 |
8.99e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLTIEieTPQGMVKaVDRMSLTLNEGEiRGLV-GESGSGKSLVAKAIVGVckenWKVSAdrmrlGNIDLlqltPKE 82
Cdd:COG4178 363 LALEDLTLR--TPDGRPL-LEDLSLSLKPGE-RLLItGPSGSGKSTLLRAIAGL----WPYGS-----GRIAR----PAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 83 RRrviardiaMIF--QEP-----SscldpsekvghqLIEAIpSYSFEGRWWQRfkwrkKQAIALLHKVGIKDHSRLMD-- 153
Cdd:COG4178 426 AR--------VLFlpQRPylplgT------------LREAL-LYPATAEAFSD-----AELREALEAVGLGHLAERLDee 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 154 -SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRmnQINNTTIVLIGH 217
Cdd:COG4178 480 aDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
27-191 |
9.08e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 64.44 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAI----------VGVCKENWKVSADRMrlgnidlLQLTPKERRRV--IARDIAMI 94
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCInlletpdsgeIRVGGEEIRLKPDRD-------GELVPADRRQLqrIRTRLGMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 95 FQepSSCLDPSEKVGHQLIEA------IPsysfegrwwqrfkwrKKQAI----ALLHKVGIKDhsrLMDSYSYELTDGEC 164
Cdd:COG4598 101 FQ--SFNLWSHMTVLENVIEApvhvlgRP---------------KAEAIeraeALLAKVGLAD---KRDAYPAHLSGGQQ 160
|
170 180
....*....|....*....|....*..
gi 515646397 165 QKVMIAMAIAAKPKVLIADEPTNDLDP 191
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-276 |
1.46e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.97 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLL--QLTPKERRRviardIAMIFQE 97
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI------LAPDS---GEVLWDgePLDPEDRRR-----IGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSscLDPSEKVGHQLI-----------EAipsysfegrwwqrfkwrKKQAIALLHKVGIKDHsrlMDSYSYELTDGECQK 166
Cdd:COG4152 80 RG--LYPKMKVGEQLVylarlkglskaEA-----------------KRRADEWLERLGLGDR---ANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 167 VMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
250 260 270
....*....|....*....|....*....|....*..
gi 515646397 247 LDA-PKHPYTV------ALLKAMPDFNDWIPHKEKLQ 276
Cdd:COG4152 217 RRQfGRNTLRLeadgdaGWLRALPGVTVVEEDGDGAE 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-251 |
2.30e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRlgnIDLLQLTpkeRRRVIARDIAMIFQepSSCL 102
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP----TEGQIF---IDGEDVT---HRSIQQRDICMVFQ--SYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 103 DP----SEKVGHQLieaipsySFEGRWWQRFKWRKKQAIALLHKVGIKDhsRLMDSYSyeltDGECQKVMIAMAIAAKPK 178
Cdd:PRK11432 90 FPhmslGENVGYGL-------KMLGVPKEERKQRVKEALELVDLAGFED--RYVDQIS----GGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-248 |
2.84e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIARDIAMIFQEPSscL 102
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGM------TSPDA---GKITVLGVPVPARARLARARIGVVPQFDN--L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 103 DPSEKVGHQLIeaipsysFEGRWWqRFKWRKKQAI--ALLhkvgikDHSRL---MDSYSYELTDGECQKVMIAMAIAAKP 177
Cdd:PRK13536 126 DLEFTVRENLL-------VFGRYF-GMSTREIEAVipSLL------EFARLeskADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 178 KVLIADEPTNDLDPITQSQI---LR-LLSRmnqinNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIwerLRsLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-249 |
4.44e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKE--RRRVIArdiamiFQEPS 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---------RLASGKISILGQPTRQalQKNLVA------YVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 SCLDPSEKVGHQLIEAIPSYSFEGrWWQRFKWRKKQAI-ALLHKVGIKDHSRLMDSysyELTDGECQKVMIAMAIAAKPK 178
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYGHMG-WLRRAKKRDRQIVtAALARVDMVEFRHRQIG---ELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 179 VLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIgHDLTTITQWATrITVMYCGQSVESADTQKLLDA 249
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVST-HNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-245 |
5.11e-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: 63.31 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTI-EIETPQgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAdrmrlgNIDLLQLTPK 81
Cdd:TIGR02633 257 ILEARNLTCwDVINPH--RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNV------FINGKPVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRVIARDIAMIFQE-PSSCLDPSEKVGHQL-IEAIPSYSFEGRWWQRfkwRKKQAI-ALLHKVGIKDHSRLMDSYSye 158
Cdd:TIGR02633 329 NPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCFKMRIDAA---AELQIIgSAIQRLKVKTASPFLPIGR-- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMY----C 234
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGegklK 482
|
250
....*....|.
gi 515646397 235 GQSVESADTQK 245
Cdd:TIGR02633 483 GDFVNHALTQE 493
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-236 |
5.45e-11 |
|
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: 61.72 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckEN-WKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPSSCldp 104
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALL-----ENfYQPQGGQVLLDGKPISQYEHKYLHSKVS----LVGQEPVLF--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGHQLIEAIPSYSFEgrwwqrfkwrkkQAIALLHKVGIKDH-SRLMDSYSYE-------LTDGECQKVMIAMAIAAK 176
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFE------------CVKEAAQKAHAHSFiSELASGYDTEvgekgsqLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 177 PKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-239 |
6.10e-11 |
|
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: 60.89 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 19 MVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRLGNIDLLQLtpkeRRRviardIAMIFQE 97
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL----RSS-----LTIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PS-------SCLDPSEKvghqlieaipsYSFEgrwwQRFKwrkkqaiALLHKVGikdhsrlmdsySYELTDGECQKVMIA 170
Cdd:cd03369 91 PTlfsgtirSNLDPFDE-----------YSDE----EIYG-------ALRVSEG-----------GLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 171 MAIAAKPKVLIADEPTNDLDPITQSQILRLLSRmnQINNTTIVLIGHDLTTITQWAtRITVMYCGQSVE 239
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKE 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-260 |
9.81e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKErrrvIARDIAMIFQEPSScldPS 105
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP----AHGHVWLDGEHIQHYASKE----VARRIGLLAQNATT---PG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 106 EKVGHQLIEaipsysfEGRWWQR---FKWRKKQAIAL---LHKVGIKDhsrLMDSYSYELTDGECQKVMIAMAIAAKPKV 179
Cdd:PRK10253 95 DITVQELVA-------RGRYPHQplfTRWRKEDEEAVtkaMQATGITH---LADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 180 LIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESAdtqklldAPKHPYTVALL 259
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELI 237
|
.
gi 515646397 260 K 260
Cdd:PRK10253 238 E 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-219 |
1.55e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLqlTPKERRRVIARDIAMIfqePSSC 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP----YQHGSITLDGKPVE--GPGAERGVVFQNEGLL---PWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 102 LDPSEKVGHQLiEAIPSYSfegrwwqrfkwRKKQAIALLHKVGIKD-HSRlmdsYSYELTDGECQKVMIAMAIAAKPKVL 180
Cdd:PRK11248 87 VQDNVAFGLQL-AGVEKMQ-----------RLEIAHQMLKKVGLEGaEKR----YIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 515646397 181 IADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDL 219
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-231 |
1.82e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 19 MVKAVDRMSLTLNEGEIR-----GLVGESGSGKSLVAKAIVGVCKenwkvsADRmrlGNIDLlqltpkerrrviARDIAM 93
Cdd:COG1245 347 LTKSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLK------PDE---GEVDE------------DLKISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 94 IFQEPSSclDPSEKVGHQLIEAIPSySFEGRWWQrfkwrkkqaIALLHKVGIKdhsRLMDSYSYELTDGECQKVMIAMAI 173
Cdd:COG1245 406 KPQYISP--DYDGTVEEFLRSANTD-DFGSSYYK---------TEIIKPLGLE---KLLDKNVKDLSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-248 |
2.18e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.98 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADR--MRLGNIDLlQLTPKERRRViardiAMIFQEP---- 98
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGF------LTPASgsLTLNGQDH-TTTPPSRRPV-----SMLFQENnlfs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 --------SSCLDPSEKVGHQlieaipsysfegrwwQRfkwRKKQAIAllHKVGIKDH-SRLmdsySYELTDGECQKVMI 169
Cdd:PRK10771 85 hltvaqniGLGLNPGLKLNAA---------------QR---EKLHAIA--RQMGIEDLlARL----PGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 170 AMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-249 |
2.31e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGA----LPRTSGYVTLDGHEVVTRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERrrvIARDIAMIFQEPSS---CLDPSEKVGHQLIeAIPSYSfegRWWQRFKWRKKQA-----IALLHkvgIKDHSrlMD 153
Cdd:PRK10762 323 DG---LANGIVYISEDRKRdglVLGMSVKENMSLT-ALRYFS---RAGGSLKHADEQQavsdfIRLFN---IKTPS--ME 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 154 SYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK10762 391 QAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMH 469
|
250 260
....*....|....*....|.
gi 515646397 234 CGQ-----SVESADTQKLLDA 249
Cdd:PRK10762 470 EGRisgefTREQATQEKLMAA 490
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-255 |
2.94e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.80 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKA------IVGVCKENWKVSadrMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVEGKVT---FHGKNLYAPDVDPVEVRR----RIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPssclDPSEKVGHQLIEAIPSYS-FEGRWWQRFKWRKKQAiALLHKVgiKDhsRLMDSySYELTDGECQKVMIAMAIA 174
Cdd:PRK14243 98 QKP----NPFPKSIYDNIAYGARINgYKGDMDELVERSLRQA-ALWDEV--KD--KLKQS-GLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLttitQWATRITVMYC-------------GQSVESA 241
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNM----QQAARVSDMTAffnveltegggryGYLVEFD 241
|
250
....*....|....
gi 515646397 242 DTQKLLDAPKHPYT 255
Cdd:PRK14243 242 RTEKIFNSPQQQAT 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-232 |
3.88e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsaDRMRLGNIDL--LQLTPKERRRVIARDIAMIFQ-E 97
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---------DKRAGGEIRLngKDISPRSPLDAVKKGMAYITEsR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 PSSCLDPSEKVGHQLieAIPSYSFEGRW---WQRFKWRKKQAIALLHK--VGIKDHSrlMDSYSYELTDGECQKVMIAMA 172
Cdd:PRK09700 348 RDNGFFPNFSIAQNM--AISRSLKDGGYkgaMGLFHEVDEQRTAENQRelLALKCHS--VNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 173 IAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVF 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-246 |
5.73e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWKvsadrmrlGNI--DLLQLT 79
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgTWD--------GEIywSGSPLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 80 PKERRRVIARDIAMIFQEPSSCLDPS--EKV--GHQLieAIPSysfeGRWWQRFKWRKKQAIALLHKVGIKDHSRLMDSY 155
Cdd:TIGR02633 69 ASNIRDTERAGIVIIHQELTLVPELSvaENIflGNEI--TLPG----GRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 156 SYeltdGECQKVMIAMAIAAKPKVLIADEPTNDLDPiTQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:TIGR02633 143 GG----GQQQLVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
250
....*....|.
gi 515646397 236 QSVESADTQKL 246
Cdd:TIGR02633 218 QHVATKDMSTM 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
162-215 |
6.06e-10 |
|
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: 57.95 E-value: 6.06e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515646397 162 GECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLI 215
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSI 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-249 |
7.55e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 21 KAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRViarDIAMIFQEPss 100
Cdd:PRK15439 28 KGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD----SGTLEIGGNPCARLTPAKAHQL---GIYLVPQEP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 CLDPSEKVGHQLIEAIPSYsfegrwwQRFKWRKKQAIALLhKVGIKDHsrlMDSYSYELTDGecQKVMIAMAIAAKPKVL 180
Cdd:PRK15439 96 LLFPNLSVKENILFGLPKR-------QASMQKMKQLLAAL-GCQLDLD---SSAGSLEVADR--QIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 181 IADEPTNDLDPITQSqilRLLSRMNQINNTT--IVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK15439 163 ILDEPTASLTPAETE---RLFSRIRELLAQGvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-235 |
8.92e-10 |
|
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: 58.05 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRMRLGNI--DLLQLTPKERRRVIArdiamiFQEPSSCLDP 104
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISG------RVEGGGTTSGQIlfNGQPRKPDQFQKCVA------YVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGhqliEAIPSYS-FEGRWWQRFKWRKKQ-AIALLHKVGikdHSRLMDSYSYELTDGECQKVMIAMAIAAKPKVLIA 182
Cdd:cd03234 95 GLTVR----ETLTYTAiLRLPRKSSDAIRKKRvEDVLLRDLA---LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 183 DEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM------YCG 235
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLssgeivYSG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-290 |
8.96e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVG---------VCKEN--WKVS--------ADRMRLGNIDLLQLTPKERRRVI 87
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerQSQFShiTRLSfeqlqklvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 88 ARDIAMIFQEPSSCLDPSEKVGhqlIEAIPSysfegrwwQRFKWrkkqaiallhkvgikdhsrlmdsysyeLTDGECQKV 167
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQFG---ITALLD--------RRFKY---------------------------LSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 168 MIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLL 247
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515646397 248 -DApkhpyTVALLKampdfndwipHKEKLQ--SLPGSIPPLQHLPI 290
Cdd:PRK10938 224 qQA-----LVAQLA----------HSEQLEgvQLPEPDEPSARHAL 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
145-229 |
2.27e-09 |
|
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: 55.15 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 145 IKDHSRLMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinntTIVLIGHDLTTITQ 224
Cdd:cd03221 57 VTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQ 132
|
....*
gi 515646397 225 WATRI 229
Cdd:cd03221 133 VATKI 137
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-247 |
4.12e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.53 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 16 PQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVgvckENWKVSADRMRLGNIDLLQLTPKERRRVIA------- 88
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----RAWDPQQGEILLNGQPIADYSEAALRQAISvvsqrvh 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 89 ------RDiamifqepsscldpsekvghQLIEAIPSYSFEgrwwqrfkwrkkQAIALLHKVG----IKDHSRLmDSYSYE 158
Cdd:PRK11160 425 lfsatlRD--------------------NLLLAAPNASDE------------ALIEVLQQVGleklLEDDKGL-NAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 ----LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQinNTTIVLIGHDLTTITQWaTRITVMYC 234
Cdd:PRK11160 472 ggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDN 548
|
250
....*....|...
gi 515646397 235 GQSVESADTQKLL 247
Cdd:PRK11160 549 GQIIEQGTHQELL 561
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-252 |
5.40e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLtpKERRRVIARDIAMIFQEPSSCLDPS 105
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTW--RKAFGVIPQKVFIFSGTFRKNLDPY 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 106 EkvghqlieaipsysfegRWWQRFKWRkkqaiaLLHKVGIKDH-SRLMDSYSYELTDGEC-------QKVMIAMAIAAKP 177
Cdd:TIGR01271 1316 E-----------------QWSDEEIWK------VAEEVGLKSViEQFPDKLDFVLVDGGYvlsnghkQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 178 KVLIADEPTNDLDPITQSQILRLLSRmnQINNTTIVLIGHDLTTITQWATRITVMycGQSVESADT-QKLLDAPKH 252
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIE--GSSVKQYDSiQKLLNETSL 1444
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-231 |
6.31e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 19 MVKAVDRMSLTLNEGEIR-----GLVGESGSGKSLVAKAIVGVckenwkvsadrmrlgnidllqLTPKERRRVIARDIAM 93
Cdd:PRK13409 346 LTKKLGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGV---------------------LKPDEGEVDPELKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 94 IFQEPSSclDPSEKVGhQLIEAIPSySFEGRWWQrfkwrkkqaIALLHKVGIKdhsRLMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK13409 405 KPQYIKP--DYDGTVE-DLLRSITD-DLGSSYYK---------SEIIKPLQLE---RLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-190 |
7.53e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.61 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVG---------VCKENWKVS--------------ADRMRLGNIDLLQLtpKER 83
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGelepdsgevSIPKGLRIGylpqeppldddltvLDTVLDGDAELRAL--EAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 84 RRVIARDIAMIFQEPsscldpsEKVG--HQLIEAIPSYSFEGRwwqrfkwrkkqAIALLHKVGIK--DHSRLMDSYSyel 159
Cdd:COG0488 96 LEELEAKLAEPDEDL-------ERLAelQEEFEALGGWEAEAR-----------AEEILSGLGFPeeDLDRPVSELS--- 154
|
170 180 190
....*....|....*....|....*....|.
gi 515646397 160 tDGECQKVMIAMAIAAKPKVLIADEPTNDLD 190
Cdd:COG0488 155 -GGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-219 |
1.35e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEietpQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRmrlGNI--DLLQLTP 80
Cdd:PRK11831 7 LVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG------QIAPDH---GEIlfDGENIPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIA--RDIAMIFQEPSSCLDPS--EKVGHQLIE--AIPSYSFegrwwqrfkwrKKQAIALLHKVGIKDHSRLMDS 154
Cdd:PRK11831 74 MSRSRLYTvrKRMSMLFQSGALFTDMNvfDNVAYPLREhtQLPAPLL-----------HSTVMMKLEAVGLRGAAKLMPS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 155 ysyELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDL 219
Cdd:PRK11831 143 ---ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-242 |
3.34e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEN-----WKVSA-DRMRLGNIDLLQltpkerrrviarDIAMIFQeps 99
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkgavlWQGKPlDYSKRGLLALRQ------------QVATVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 sclDPSEKVGHQLIEAIPSYSFE--GRWWQRFKWRKKQAIALLhkvgikDHSRLMDSYSYELTDGECQKVMIAMAIAAKP 177
Cdd:PRK13638 85 ---DPEQQIFYTDIDSDIAFSLRnlGVPEAEITRRVDEALTLV------DAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 178 KVLIADEPTNDLDPITQSQILRLLSRMNQINNtTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-234 |
4.03e-08 |
|
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: 55.02 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 11 IEIETPQGMvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDllqltpkerrrvIARD 90
Cdd:TIGR01257 935 VKIFEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKD------------IETN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 91 IAMIFQEPSSCldPSEKV-GHQLI--EAIPSYS-FEGRWWQRFKWRKKqaiALLHKVGIKdHSRlmDSYSYELTDGECQK 166
Cdd:TIGR01257 998 LDAVRQSLGMC--PQHNIlFHHLTvaEHILFYAqLKGRSWEEAQLEME---AMLEDTGLH-HKR--NEEAQDLSGGMQRK 1069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 167 VMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNqiNNTTIVLIGHDLTTITQWATRITV-----MYC 234
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR--SGRTIIMSTHHMDEADLLGDRIAIisqgrLYC 1140
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
33-236 |
4.56e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.14 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 33 GEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQltpkerrrviAR-DIAMIFQEPSscLDPSEKVghq 111
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETP----SAGELLAGTAPLAE----------AReDTRLMFQDAR--LLPWKKV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 112 lIEAIpSYSFEGRWwqrfkwrKKQAIALLHKVGIKDHSrlmDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDP 191
Cdd:PRK11247 99 -IDNV-GLGLKGQW-------RDAALQALAAVGLADRA---NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515646397 192 ITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-232 |
5.44e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.16 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKS----LVAKAIvgvckenwKVSADRMRLGNIDLLQlTPKerrRVIARDIAMIFQEP 98
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKStllsMISRLL--------PPDSGEVLVDGLDVAT-TPS---RELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 99 SscLDPSEKVgHQLIeaipsySFeGRW-WQRFK-----WRK-KQAIALLHKVGIKDhsRLMDsysyELTDGECQKVMIAM 171
Cdd:COG4604 85 H--INSRLTV-RELV------AF-GRFpYSKGRltaedREIiDEAIAYLDLEDLAD--RYLD----ELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 172 AIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVM 232
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-229 |
7.01e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 24 DRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRMRLgNID-------LLQLTPKERRRVIARDIAMIFQ 96
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNG------EVLLDDGRI-IYEqdlivarLQQDPPRNVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 97 EPSSCL------------DPSEKVGHQLIEAIPSYSFEGRWwqRFKWRKKQAIALLhkvGIKDHSRLMdsysyELTDGEC 164
Cdd:PRK11147 93 EQAEYLkryhdishlvetDPSEKNLNELAKLQEQLDHHNLW--QLENRINEVLAQL---GLDPDAALS-----SLSGGWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 165 QKVMIAMAIAAKPKVLIADEPTNDLDpITQSQILR--LLSRmnqinNTTIVLIGHDLTTITQWATRI 229
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD-IETIEWLEgfLKTF-----QGSIIFISHDRSFIRNMATRI 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-257 |
9.29e-08 |
|
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: 53.80 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWKVSADRMRLGNIDLLQLtpKERRRVIARDIAMIFQEPSSCLDP 104
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDL--RFKITIIPQDPVLFSGSLRMNLDP 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 sekvghqlieaIPSYSFEGRWWqrfkwrkkqAIALLHkvgIKDH-SRLMDSYSYE-------LTDGECQKVMIAMAIAAK 176
Cdd:TIGR00957 1383 -----------FSQYSDEEVWW---------ALELAH---LKTFvSALPDKLDHEcaeggenLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 177 PKVLIADEPTNDLDPITQSQILRLLSrmNQINNTTIVLIGHDLTTITQWaTRITVMYCGQSVESADTQKLLDAPKHPYTV 256
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
.
gi 515646397 257 A 257
Cdd:TIGR00957 1517 A 1517
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-98 |
1.26e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIETPQgMVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGvcKENWKVSADRMRLGNIDLLQLTPK 81
Cdd:CHL00131 6 PILEIKNLHASVNENE-ILKGLN---LSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGESILDLEPE 79
|
90
....*....|....*..
gi 515646397 82 ERRRviaRDIAMIFQEP 98
Cdd:CHL00131 80 ERAH---LGIFLAFQYP 93
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-232 |
1.28e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.91 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 2 PLLDIRHLTIEIetpqGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK11300 4 PLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF----YKPTGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ErrrvIAR-DIAMIFQEPSscLDPSEKVGHQLIEAIPSYSFEGRWWQRFK---WRKKQAIAL------LHKVGIKDHS-R 150
Cdd:PRK11300 76 Q----IARmGVVRTFQHVR--LFREMTVIENLLVAQHQQLKTGLFSGLLKtpaFRRAESEALdraatwLERVGLLEHAnR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 151 LMDSYSYeltdGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11300 150 QAGNLAY----GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
..
gi 515646397 231 VM 232
Cdd:PRK11300 226 VV 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-235 |
1.77e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 28 LTLNEGEIRGLVGESGSGKSLVAKAIVGVckENwkVSADRMRLGNIDLLQLTPKERrrviarDIAMIFQepSSCLDPSEK 107
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGL--ED--ITSGDLFIGEKRMNDVPPAER------GVGMVFQ--SYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 108 VGHQLieaipsySF----EGRWWQRFKWRKKQAIALLHKvgikDHsrLMDSYSYELTDGECQKVMIAMAIAAKPKVLIAD 183
Cdd:PRK11000 92 VAENM-------SFglklAGAKKEEINQRVNQVAEVLQL----AH--LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515646397 184 EPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
158-217 |
1.81e-07 |
|
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: 50.23 E-value: 1.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 158 ELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMnqinNTTIVLIGH 217
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-232 |
1.82e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTIEIETPQgmvkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckENwkVSADRMRLGNIDLLQLtP 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ET--PDSGRIMLDGQDITHV-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRrviarDIAMIFQepSSCLDPS-------------EKVGHQLIEAipsysfegrwwqrfkwRKKQAIALLHKVGIKD 147
Cdd:PRK09452 83 AENR-----HVNTVFQ--SYALFPHmtvfenvafglrmQKTPAAEITP----------------RVMEALRMVQLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 148 HSrlmdsySYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQI---LRLLSRMNQInntTIVLIGHDLTTITQ 224
Cdd:PRK09452 140 RK------PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQRKLGI---TFVFVTHDQEEALT 210
|
....*...
gi 515646397 225 WATRITVM 232
Cdd:PRK09452 211 MSDRIVVM 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-243 |
1.88e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRlgnIDLLQLTPKERRRVIARDIAMIFQEPS 99
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG----NYQPDAGSIL---IDGQEMRFASTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scLDPSEKVGHQLieaipsysFEGRWWQRFKW-RKKQAIA----LLHKVG--IKDHSRLMdsysyELTDGECQKVMIAMA 172
Cdd:PRK11288 90 --LVPEMTVAENL--------YLGQLPHKGGIvNRRLLNYeareQLEHLGvdIDPDTPLK-----YLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515646397 173 IAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADT 243
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRA-EGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDD 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-250 |
2.50e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 26 MSLTLNEGEIRGLVGESGSGKSLVAKAI------------------------------VGVC-----------KENWKVS 64
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIerlydptegdiiindshnlkdinlkwwrskIGVVsqdpllfsnsiKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 65 ADRMRlgniDLLQLTP------------KERRRVIARDIAMIFQEPSSCLDPSEkvghqLIEAIPSYSfegrwwqrfKWR 132
Cdd:PTZ00265 484 LYSLK----DLEALSNyynedgndsqenKNKRNSCRAKCAGDLNDMSNTTDSNE-----LIEMRKNYQ---------TIK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 133 KKQAIALLHKVGIKDH-SRLMDSY-------SYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRM 204
Cdd:PTZ00265 546 DSEVVDVSKKVLIHDFvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515646397 205 NQINNTTIVLIGHDLTTItQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:PTZ00265 626 KGNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-238 |
2.79e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRhltiEIETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-------------NWKvSADR 67
Cdd:PRK11614 3 KVMLSFD----KVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtsgrivfdgkditDWQ-TAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 68 MRlgniDLLQLTPkERRRVIARdiaMIFQEPSscldpsekvghqlieAIPSYsFEGRwwQRFKWRKKQAIALLHKVGIKD 147
Cdd:PRK11614 78 MR----EAVAIVP-EGRRVFSR---MTVEENL---------------AMGGF-FAER--DQFQERIKWVYELFPRLHERR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 148 HSRlmdsySYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWAT 227
Cdd:PRK11614 132 IQR-----AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLAD 205
|
250
....*....|.
gi 515646397 228 RITVMYCGQSV 238
Cdd:PRK11614 206 RGYVLENGHVV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-257 |
4.46e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwkvsADRMRLGNIDL--LQLTPKERRRVIARDIAM---------IF 95
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYG---------ATRRTAGQVYLdgKPIDIRSPRDAIRAGIMLcpedrkaegII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 96 QEPSscldpsekVGHQL-IEAIPSYSFEGrWWQRFKWRKKQAIALLHKVGIKDHSRlmDSYSYELTDGECQKVMIAMAIA 174
Cdd:PRK11288 344 PVHS--------VADNInISARRHHLRAG-CLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSV-----ESADTQKLLDA 249
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALSL 491
|
250
....*....|
gi 515646397 250 --PKHPYTVA 257
Cdd:PRK11288 492 alPRTSAAVA 501
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-98 |
5.00e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 3 LLDIRHLTIEIETpQGMVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGvcKENWKVSADRMRLGNIDLLQLTPKE 82
Cdd:PRK09580 1 MLSIKDLHVSVED-KAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90
....*....|....*.
gi 515646397 83 RrrvIARDIAMIFQEP 98
Cdd:PRK09580 75 R---AGEGIFMAFQYP 87
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-280 |
5.05e-07 |
|
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: 50.24 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLtpKERRRVIARDIaMIFQEP-SSC 101
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKW--RKAFGVIPQKV-FIFSGTfRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 102 LDPSEkvghqlieaipsysfegrwwqrfKWRKKQAIALLHKVGIKDH-SRLMDSYSYELTDGEC-------QKVMIAMAI 173
Cdd:cd03289 97 LDPYG-----------------------KWSDEEIWKVAEEVGLKSViEQFPGQLDFVLVDGGCvlshghkQLMCLARSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 174 AAKPKVLIADEPTNDLDPITqSQILRLLSRmNQINNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLLDAPKHp 253
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT-YQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSH- 229
|
250 260
....*....|....*....|....*..
gi 515646397 254 ytvallkampdFNDWIPHKEKLQSLPG 280
Cdd:cd03289 230 -----------FKQAISPSDRLKLFPR 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-236 |
5.20e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 4 LDIRHLT-IEIETPQgmVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKvsadrmrlGNI--DLLQLTP 80
Cdd:PRK13549 260 LEVRNLTaWDPVNPH--IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWE--------GEIfiDGKPVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KERRRVIARDIAMIFQE-PSSCLDPSEKVGHQL-IEAIPSYSFegrwWQRFKWRKKQAIAL--LHKVGIKDHSRLMDSYS 156
Cdd:PRK13549 330 RNPQQAIAQGIAMVPEDrKRDGIVPVMGVGKNItLAALDRFTG----GSRIDDAAELKTILesIQRLKVKTASPELAIAR 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 157 yeLTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLlsrMNQI--NNTTIVLIGHDLTTITQWATRITVMYC 234
Cdd:PRK13549 406 --LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKL---INQLvqQGVAIIVISSELPEVLGLSDRVLVMHE 480
|
..
gi 515646397 235 GQ 236
Cdd:PRK13549 481 GK 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-233 |
6.51e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 32 EGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIARDIAMIFQEPSSCL-DPSEKVGH 110
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPN---------LGDYD----EEPSWDEVLKRFRGTELQDYFKKLaNGEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 111 --QLIEAIPSYsFEGRwwqrfkwrkkqAIALLHKV---GIKDH-------SRLMDSYSYELTDGECQKVMIAMAIAAKPK 178
Cdd:COG1245 165 kpQYVDLIPKV-FKGT-----------VRELLEKVderGKLDElaeklglENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 179 VLIADEPTNDLDpITQ----SQILRLLSRMnqinNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:COG1245 233 FYFFDEPSSYLD-IYQrlnvARLIRELAEE----GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-231 |
1.01e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 19 MVKAVDRMSL-----TLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDLLQLTPKERRRVIARDIAM 93
Cdd:cd03237 6 MKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPD---------EGDIEIELDTVSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 94 IFQepsscldpsekvghQLIEAIPSYSFEGRWWQrfkwrkkqaIALLHKVGIKdhsRLMDSYSYELTDGECQKVMIAMAI 173
Cdd:cd03237 77 TVR--------------DLLSSITKDFYTHPYFK---------TEIAKPLQIE---QILDREVPELSGGELQRVAIAACL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITV 231
Cdd:cd03237 131 SKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-246 |
1.97e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGNidllQLTPKERRRVIARDIAMIFQEPS 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGK----EIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 SCLDPSekvghqlieaipsySFEGRWWQRFKwrkKQAIALLHKVGIKDHSRLMDSYSYE---------LTDGECQKVMIA 170
Cdd:PRK10982 84 LVLQRS--------------VMDNMWLGRYP---TKGMFVDQDKMYRDTKAIFDELDIDidprakvatLSVSQMQMIEIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 171 MAIAAKPKVLIADEPTNDLdpiTQSQILRLLSRMNQINNT--TIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-236 |
2.16e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 28 LTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSAD--RMRLGNIDL------LQLTPKERRrviardIAMIFQEps 99
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGL------TRPQkgRIVLNGRVLfdaekgICLPPEKRR------IGYVFQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 100 scldpsekvgHQLIeaiPSYSFEGRWwqRFKWRKK------QAIALLhkvGIKDhsrLMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK11144 85 ----------ARLF---PHYKVRGNL--RYGMAKSmvaqfdKIVALL---GIEP---LLDRYPGSLSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK11144 144 LTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-233 |
3.06e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 32 EGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIARDIAMIFQE-----PSSCLDPSE 106
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPN---------LGKFD----DPPDWDEILDEFRGSELQNyftklLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 107 KVghQLIEAIPsysfegrwwqrfKWRKKQAIALLHKV---GIKDH-------SRLMDSYSYELTDGECQKVMIAMAIAAK 176
Cdd:cd03236 92 KP--QYVDLIP------------KAVKGKVGELLKKKderGKLDElvdqlelRHVLDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 177 PKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVlIGHDLTTITQWATRITVMY 233
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCLY 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-238 |
9.33e-06 |
|
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: 45.72 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 10 TIEIETPQGMVKA--VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADrMRLGNIDllqltPKERRRVI 87
Cdd:cd03233 8 NISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIP-----YKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 88 ARDIAMIFQEPSSclDPSEKVGHQLieaipsysfegrwwqRFKWRKKQaiallhkvgikdhsrlmDSYSYELTDGECQKV 167
Cdd:cd03233 82 PGEIIYVSEEDVH--FPTLTVRETL---------------DFALRCKG-----------------NEFVRGISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 168 MIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLighdltTITQ-----WAT--RITVMYCGQSV 238
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFV------SLYQasdeiYDLfdKVLVLYEGRQI 199
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-248 |
1.08e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.96 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 30 LNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMrlgnIDLLQLTPKERRRVIArdiamiFQEPSSCLDPSEKVG 109
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL----LNGMPIDAKEMRAISA------YVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 110 HQLIeaipsYSFEGRWWQRFKWRKKQAI--ALLHKVGIKD--HSRLMDSYSYE-LTDGECQKVMIAMAIAAKPKVLIADE 184
Cdd:TIGR00955 118 EHLM-----FQAHLRMPRRVTKKEKRERvdEVLQALGLRKcaNTRIGVPGRVKgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 185 PTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-250 |
1.17e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkVSADRMRLGNIDLLQLTPKE---RRRVIARD----IAM-IFQ-- 96
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-----PGSGSIQFAGQPLEAWSAAElarHRAYLSQQqtppFAMpVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 97 ---EPSSC-LDPSEKVGHQLIEAipsysfegrwwqrfkwrkkqaiallhkVGIKDhsrLMDSYSYELTDGECQKVMIAMA 172
Cdd:PRK03695 91 tlhQPDKTrTEAVASALNEVAEA---------------------------LGLDD---KLGRSVNQLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 173 I-----AAKP--KVLIADEPTNDLDpITQSQIL-RLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQ 244
Cdd:PRK03695 141 VlqvwpDINPagQLLLLDEPMNSLD-VAQQAALdRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
....*.
gi 515646397 245 KLLDAP 250
Cdd:PRK03695 219 EVLTPE 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-249 |
1.30e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 46.34 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRViarDIAMIFQEpsscL 102
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD----AGSISLCGEPVPSRARHARQRV---GVVPQFDN----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 103 DPSEKVGHQLIeaipsysFEGRWwqrFKWRKKQAIALLHkvGIKDHSRL---MDSYSYELTDGECQKVMIAMAIAAKPKV 179
Cdd:PRK13537 92 DPDFTVRENLL-------VFGRY---FGLSAAAARALVP--PLLEFAKLenkADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515646397 180 LIADEPTNDLDPITQSQI---LR-LLSRmnqinNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMwerLRsLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-222 |
2.04e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 2.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 159 LTDGECQKVMIA--MAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNtTIVLIGHDLTTI 222
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL 152
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-222 |
3.99e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 3.99e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515646397 155 YSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTI 222
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-236 |
4.31e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.83 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 1 MPLLDIRHLTieiETPQGMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTP 80
Cdd:PRK11650 1 MAGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--E--RITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 81 KErrrviaRDIAMIFQepSSCLDPsekvgHQLIEAIPSYSfegrwwqrFKWRK--KQAIA--LLHKVGIKDHSRLMDSYS 156
Cdd:PRK11650 74 AD------RDIAMVFQ--NYALYP-----HMSVRENMAYG--------LKIRGmpKAEIEerVAEAARILELEPLLDRKP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 157 YELTDGECQKVmiAM--AIAAKPKVLIADEPTNDLDPITQSQ----ILRLLSRMnqinNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11650 133 RELSGGQRQRV--AMgrAIVREPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRL----KTTSLYVTHDQVEAMTLADRVV 206
|
....*.
gi 515646397 231 VMYCGQ 236
Cdd:PRK11650 207 VMNGGV 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-233 |
5.29e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 29 TLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIAR----DIAMIFQEPSsclDP 104
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN---------LGDYE----EEPSWDEVLKRfrgtELQNYFKKLY---NG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 105 SEKVGH--QLIEAIPSYsFEGRWWQrfkwrkkqaiaLLHKV---GIKDH-------SRLMDSYSYELTDGECQKVMIAMA 172
Cdd:PRK13409 159 EIKVVHkpQYVDLIPKV-FKGKVRE-----------LLKKVderGKLDEvverlglENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515646397 173 IAAKPKVLIADEPTNDLDpITQ----SQILRLLSRmnqinNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLD-IRQrlnvARLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-219 |
1.06e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 18 GMVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsadrmrlgnidllqLTPKERrrVIARDiamifqe 97
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL---------------------VAPDEG--VIKRN------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 98 psscldPSEKVGH--QLIEAIPSYSFEGRWWQRFK--WRKKQAIALLHKVgikDHSRLMDSYSYELTDGECQKVMIAMAI 173
Cdd:PRK09544 65 ------GKLRIGYvpQKLYLDTTLPLTVNRFLRLRpgTKKEDILPALKRV---QAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515646397 174 AAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDL 219
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
158-233 |
1.49e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.79 E-value: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515646397 158 ELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQINNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-236 |
1.74e-04 |
|
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: 42.13 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGV-------CKENWKVSAdRMRLG-----------NI----DLLQ 77
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIyppdsgtVTVRGRVSS-LLGLGggfnpeltgreNIylngRLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 78 LTPKERRRVIaRDIAMiFQEPSSCLDpsEKVGHqlieaipsYSfegrwwqrfkwrkkqaiallhkVGIKdhSRLmdsysy 157
Cdd:cd03220 114 LSRKEIDEKI-DEIIE-FSELGDFID--LPVKT--------YS----------------------SGMK--ARL------ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515646397 158 eltdgecqkvMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03220 152 ----------AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-218 |
1.90e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.13 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwkvsadrmrlgnidllQLTPKERRRVIARDIAMIF--QEPSS 100
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG---------------------ELEPDSGTVKLGETVKIGYfdQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 101 cLDPSEKVghqlIEAIPSYSFEGRwwqrfkwrKKQAIALLhkvgikdhSRLM----DSYSY--ELTDGECQKVMIAMAIA 174
Cdd:COG0488 390 -LDPDKTV----LDELRDGAPGGT--------EQEVRGYL--------GRFLfsgdDAFKPvgVLSGGEKARLALAKLLL 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515646397 175 AKPKVLIADEPTNDLDPITQSQILRLLsrmnqinNT---TIVLIGHD 218
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEAL-------DDfpgTVLLVSHD 488
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
139-218 |
1.99e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 139 LLHKVGI--KDHSRLMDsysyELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITqsqILRLLSRMNQINNTTIVlIG 216
Cdd:PRK15064 138 LLLGVGIpeEQHYGLMS----EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMII-IS 209
|
..
gi 515646397 217 HD 218
Cdd:PRK15064 210 HD 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
159-247 |
6.73e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.16 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMnQINNTTIVlIGHDLTTITQwATRITVMYCGQSV 238
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIV 557
|
....*....
gi 515646397 239 ESADTQKLL 247
Cdd:PRK11176 558 ERGTHAELL 566
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
151-222 |
1.12e-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: 38.89 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515646397 151 LMDSYSYELTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQIL-----RLLSRMNQINNTTIVLIGHDLTTI 222
Cdd:smart00382 53 IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-248 |
1.67e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEN-----WKVSADRMRLG-----------NIDL----LQLTPK 81
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNkgtvdIKGSAALIAISsglngqltgieNIELkglmMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 82 ERRRVIARDIAmiFQEpsscldpsekVGHQLIEAIPSYSfegrwwqrfkwrkkqaiallhkVGIKdhSRLmdsysyeltd 161
Cdd:PRK13545 119 KIKEIIPEIIE--FAD----------IGKFIYQPVKTYS----------------------SGMK--SRL---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 162 gecqkvMIAMAIAAKPKVLIADEPTNDLDpitQSQILRLLSRMNQI--NNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK13545 153 ------GFAISVHINPDILVIDEALSVGD---QTFTKKCLDKMNEFkeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
....*....
gi 515646397 240 SADTQKLLD 248
Cdd:PRK13545 224 YGDIKEVVD 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-243 |
7.94e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.79 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515646397 159 LTDGECQKVMIAMAIAAKPKVLIADEPTNDLDPITQSQILRLLSRMNQiNNTTIVLIGHDLTTITQWATRITVMYCGQS- 237
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
....*...
gi 515646397 238 --VESADT 243
Cdd:PRK10982 471 giVDTKTT 478
|
|
| |
