|
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: 665.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKWWQRFKWRKKQAITLIHKVGIKDHSRLMDSYSYELT 160
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 241 ADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIPYTKRIKSHKFN 320
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIKGHEFA 320
|
330
....*....|.
gi 515624491 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: 557.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKWWQRFKWRKKQAITLIHKVGIKDHSRLMDSYSYELT 160
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 241 ADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIPYTKRIKSHKFN 320
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKNHLYA 320
|
330
....*....|
gi 515624491 321 CHFPLNMEKK 330
Cdd:PRK15093 321 CHFPLNMEEE 330
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-324 |
7.01e-122 |
|
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: 352.82 E-value: 7.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSaDRMRLGNIDLLQLTPKE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS-GEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIKDHSRLMDSYSYELTDG 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSK-----AEARERAIELLERVGLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 163 QCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 243 TQKLLDAPKHPYTVALLKAMPDFNdwiPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRIKS-HKFN 320
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLD---PDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCrEEEPPLREVGPgHRVA 311
|
....
gi 515624491 321 CHFP 324
Cdd:COG0444 312 CHLY 315
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-326 |
3.06e-104 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 308.59 E-value: 3.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIKDHSRLMDSYSYELT 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNK-----KTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 241 ADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRIKSHKF 319
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRALPEFAQ---DKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLAGRQS 312
|
....*..
gi 515624491 320 NCHFPLN 326
Cdd:PRK11022 313 KCHYPLD 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-263 |
4.66e-89 |
|
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: 276.18 E-value: 4.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHsfegkwwQRFKWR--KKQAITLIHKVGIKDHSRLMDSYSYE 158
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLH-------RGLSGAaaRARALELLERVGIPDPERRLDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260
....*....|....*....|....*
gi 515624491 239 ESADTQKLLDAPKHPYTVALLKAMP 263
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAEP 261
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-309 |
3.67e-81 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 249.64 E-value: 3.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNiDLLQLTP 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGR-EILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKWwQRFKwrkkQAITLIHKVGIKDHSRLMDSYSYELT 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKA-EAFE----ESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 241 ADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCVEIP 309
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVPRLDA---EGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAP 309
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-241 |
4.30e-78 |
|
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: 238.17 E-value: 4.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTpKE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK----PTSGSIIFDGKDLLKLS-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIhKVGIKDHSRLMDSYSYELTDG 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSK-----KEARKEAVLLL-LVGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 163 QCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-263 |
3.96e-73 |
|
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: 234.80 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIE-IETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTP 80
Cdd:COG1123 259 PLLEVRNLSKRyPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRvIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIKdhSRLMDSYSYELT 160
Cdd:COG1123 335 RSLRE-LRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSR-----AERRERVAELLERVGLP--PDLADRYPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
250 260
....*....|....*....|...
gi 515624491 241 ADTQKLLDAPKHPYTVALLKAMP 263
Cdd:COG1123 487 GPTEEVFANPQHPYTRALLAAVP 509
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-324 |
1.97e-72 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 227.31 E-value: 1.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGL-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNID 74
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLfgrtvgvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL----EEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 75 LLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIK-DHsrlMD 153
Cdd:COG4608 82 ITGLSGRELRPL-RRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASK-----AERRERVAELLELVGLRpEH---AD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 154 SYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:COG4608 153 RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 234 CGQSVESADTQKLLDAPKHPYTVALLKAMPdfndwIPHKEKLQS---LPGSIP-PLqHLPIGCRLGPRCPYAQRQC-VEI 308
Cdd:COG4608 233 LGKIVEIAPRDELYARPLHPYTQALLSAVP-----VPDPERRRErivLEGDVPsPL-NPPSGCRFHTRCPYAQDRCaTEE 306
|
330
....*....|....*..
gi 515624491 309 PYTKRIKS-HKFNCHFP 324
Cdd:COG4608 307 PPLREVGPgHQVACHLA 323
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-265 |
4.11e-68 |
|
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: 213.51 E-value: 4.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLlqltPKE 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPV----TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHsfegkwwqRFKWRKKQAITLIHKVGIkdHSRLMDSYSYELTDG 162
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIH--------GLPDREERIAELLEQVGL--PPSFLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 163 QCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250 260
....*....|....*....|...
gi 515624491 243 TQKLLDAPKHPYTVALLKAMPDF 265
Cdd:COG1124 223 VADLLAGPKHPYTRELLAASLAF 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-251 |
4.48e-68 |
|
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: 221.32 E-value: 4.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIetPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSaDRMRLGNIDLLQLTPK 81
Cdd:COG1123 3 PLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrviARDIAMIFQEPSSCLDPSeKVGRQLIESIPSHSFEGKWwqrfkwRKKQAITLIHKVGIKdhsRLMDSYSYELTD 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAE------ARARVLELLEAVGLE---RRLDRYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250
....*....|
gi 515624491 242 DTQKLLDAPK 251
Cdd:COG1123 226 PPEEILAAPQ 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-321 |
7.22e-56 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 184.52 E-value: 7.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIE---------TPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGN 72
Cdd:PRK15079 7 VLLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT---DGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 73 iDLLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGRQLIEsiPSHSFEGKW-WQRFKWRKKqaiTLIHKVGIKDHsrL 151
Cdd:PRK15079 84 -DLLGMKDDEWRAV-RSDIQMIFQDPLASLNPRMTIGEIIAE--PLRTYHPKLsRQEVKDRVK---AMMLKVGLLPN--L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 152 MDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK15079 155 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 232 MYCGQSVESADTQKLLDAPKHPYTVALLKA--MPDfndwiPHKEK---LQSLPGSIPPLQHLPIGCRLGPRCPYAQRQCV 306
Cdd:PRK15079 235 MYLGHAVELGTYDEVYHNPLHPYTKALMSAvpIPD-----PDLERnktIQLLEGELPSPINPPSGCVFRTRCPIAGPECA 309
|
330
....*....|....*.
gi 515624491 307 EI-PYTKRIKSHKFNC 321
Cdd:PRK15079 310 KTrPVLEGSFRHAVSC 325
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-264 |
1.45e-54 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 186.45 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckenwkvsadrMRL---------- 70
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSI--------------LRLlpsppvvyps 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 71 GNI-----DLLQLTPKERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSfegkwWQRFKWRKKQAITLIHKVGI 145
Cdd:PRK15134 69 GDIrfhgeSLLHASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHR-----GMRREAARGEILNCLDRVGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 146 KDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQW 225
Cdd:PRK15134 144 RQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKL 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 515624491 226 ATRITVMYCGQSVESADTQKLLDAPKHPYTVALLKAMPD 264
Cdd:PRK15134 224 ADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-263 |
1.96e-53 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 185.06 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENW-KVSADRMRLGN-----IDLL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLRRrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 77 QLTPKERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIKDHSRLMDSYS 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASR-----EEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|....*..
gi 515624491 237 SVESADTQKLLDAPKHPYTVALLKAMP 263
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVP 273
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-322 |
1.54e-52 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 175.92 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 16 PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQlTPKERRRVIARDIAMIF 95
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI--E--TPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPSSCLDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIK-DHSrlmDSYSYELTDGQCQKVMIAMAIA 174
Cdd:PRK11308 99 QNPYGSLNPRKKVGQILEEPLLINTSLSA-----AERREKALAMMAKVGLRpEHY---DRYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 255 TVALLKAMPDFNDwIPHKEKLQsLPGSIP-PLqHLPIGCRLGPRCPYAQRQC-VEIPYTKRIKSHKFNCH 322
Cdd:PRK11308 251 TQALLSATPRLNP-DDRRERIK-LTGELPsPL-NPPPGCAFNARCPRAFGRCrQEQPQLRDYDGRLVACF 317
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-264 |
1.81e-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: 180.65 E-value: 1.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGL-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkvSADRMRLGNID 74
Cdd:COG4172 274 PLLEARDLKVWFPIKRGLfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 75 LLQLTPKERRRViARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKWWQRfkwrKKQAITLIHKVGIKdhSRLMDS 154
Cdd:COG4172 349 LDGLSRRALRPL-RRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAER----RARVAEALEEVGLD--PAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 155 YSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYC 234
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
250 260 270
....*....|....*....|....*....|
gi 515624491 235 GQSVESADTQKLLDAPKHPYTVALLKAMPD 264
Cdd:COG4172 502 GKVVEQGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-261 |
2.58e-43 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 149.85 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MP-LLDIRHLTIEieTPQGLVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLgniDLLQLT 79
Cdd:PRK10418 1 MPqQIELRNIALQ--AAQPLVHGV---SLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLL---DGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 80 PKERRrviARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGkwwqrfkwRKKQAITLIHKVGIKDHSRLMDSYSYEL 159
Cdd:PRK10418 73 PCALR---GRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPA--------DDATLTAALEAVGLENAARVLKLYPFEM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
250 260
....*....|....*....|..
gi 515624491 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 |
1.18e-39 |
|
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: 139.64 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 6 IRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERRR 85
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL--E--RPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 86 vIARDIAMIFQEPSscLDPSEKVgrqlIESIpSHSFEGKWWQRfKWRKKQAITLIHKVGIKDHSrlmDSYSYELTDGQCQ 165
Cdd:cd03258 80 -ARRRIGMIFQHFN--LLSSRTV----FENV-ALPLEIAGVPK-AEIEERVLELLELVGLEDKA---DAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQK 245
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 515624491 246 LLDAPK 251
Cdd:cd03258 228 VFANPQ 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-281 |
2.17e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.36 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 6 IRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERRR 85
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL--E--RPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 86 ViARDIAMIFQEP---SSC--------------LDPSEkvgrqliesipshsfegkwwqrfkwRKKQAITLIHKVGIKDH 148
Cdd:COG1135 80 A-RRKIGMIFQHFnllSSRtvaenvalpleiagVPKAE-------------------------IRKRVAELLELVGLSDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 149 SrlmDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATR 228
Cdd:COG1135 134 A---DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDR 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515624491 229 ITVMYCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLPGS 281
Cdd:COG1135 211 VAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGG 263
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
2-255 |
2.49e-36 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 131.47 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRLGNIDLLQLTP 80
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLApTSGSVYYRDRDGGPRDLFALSE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCLDPS----EKVGRQLIESipshsfeGkwWQRFKWRKKQAITLIHKVGIkDHSRlMDSYS 156
Cdd:COG4107 87 AERRRLRRTDWGMVYQNPRDGLRMDvsagGNIAERLMAA-------G--ERHYGDIRARALEWLERVEI-PLER-IDDLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250
....*....|....*....
gi 515624491 237 SVESADTQKLLDAPKHPYT 255
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYT 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-259 |
4.52e-36 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 136.37 E-value: 4.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVK-------AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNID 74
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 75 LLQLTPKERRrviardIAMIFQEPSSCLDPSEKVGRQLIESIPSHSFEGKWWQRfkwrKKQAITLIHKVGIKDHSRlmDS 154
Cdd:PRK15134 354 RRQLLPVRHR------IQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLSAAQR----EQQVIAVMEEVGLDPETR--HR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 155 YSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYC 234
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 515624491 235 GQSVESADTQKLLDAPKHPYTVALL 259
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-229 |
4.81e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.78 E-value: 4.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKS--LvakAIVGvCKEnwKVSADRMRLGNIDLLQLT 79
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStlL---NILG-GLD--RPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 80 PKERRRVIARDIAMIFQEPsscldpsekvgrQLIES--------IPsHSFEGKwwqRFKWRKKQAITLIHKVGIKDHsrl 151
Cdd:COG1136 77 ERELARLRRRHIGFVFQFF------------NLLPEltalenvaLP-LLLAGV---SRKERRERARELLERVGLGDR--- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 152 MDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLtTITQWATRI 229
Cdd:COG1136 138 LDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRV 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-232 |
2.19e-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: 127.99 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR----PTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRVIARDIAMIFQEPS-----SCLD----PSEKVGRQLIEsipshsfegkwwqrfkwRKKQAITLIHKVGIKDHsrlMDS 154
Cdd:cd03255 77 AAFRRRHIGFVFQSFNllpdlTALEnvelPLLLAGVPKKE-----------------RRERAEELLERVGLGDR---LNH 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 155 YSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLtTITQWATRITVM 232
Cdd:cd03255 137 YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIEL 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-282 |
8.86e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 133.83 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGL-------VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG-VCKENWKVSADRMRLGNI 73
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRlVESQGGEIIFNGQRIDTL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 74 DLLQLTPkerrrvIARDIAMIFQEPSSCLDPSEKVGRQLIESIPSHSF-EGKWWQ-RFKWrkkqaitLIHKVGIK-DHSR 150
Cdd:PRK10261 392 SPGKLQA------LRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLlPGKAAAaRVAW-------LLERVGLLpEHAW 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 lmdSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK10261 459 ---RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 231 VMYCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKL---QSLPGSI 282
Cdd:PRK10261 536 VMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSRQRPQRVllsDDLPSNI 590
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-249 |
2.90e-34 |
|
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: 125.93 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETpqglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKE 82
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL----LKPSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RrrviARDIAMIFQEPS-----SCLDpsekV---GRqliesIPSHSfegkWWQRFKWRKKQAI-TLIHKVGIKDHS-RLM 152
Cdd:COG1120 73 L----ARRIAYVPQEPPapfglTVRE----LvalGR-----YPHLG----LFGRPSAEDREAVeEALERTGLEHLAdRPV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 153 DsysyELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:COG1120 136 D----ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLL 211
|
250
....*....|....*..
gi 515624491 233 YCGQSVESADTQKLLDA 249
Cdd:COG1120 212 KDGRIVAQGPPEEVLTP 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-229 |
2.23e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.63 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIeieTPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:COG3638 1 PMLELRNLSK---RYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL----VEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRvIARDIAMIFQEPssCLdpsekVGRQ------LIESIPSHSFEGKWWQRFKWR-KKQAITLIHKVGIKDHSrlmds 154
Cdd:COG3638 74 ALRR-LRRRIGMIFQQF--NL-----VPRLsvltnvLAGRLGRTSTWRSLLGLFPPEdRERALEALERVGLADKA----- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 155 ysYELTD----GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRI 229
Cdd:COG3638 141 --YQRADqlsgGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-187 |
2.46e-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: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPssCL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG----LLSPTEGTILLDGQDLTDDERKSLRKEIG----YVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 DPSEKVGRQLIESIPSHSFegkwwqRFKWRKKQAITLIHKVGIKD-HSRLMDSYSYELTDGQCQKVMIAMAIAAKPKILI 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGL------SKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 515624491 182 ADEPTN 187
Cdd:pfam00005 145 LDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-254 |
2.77e-32 |
|
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: 120.30 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 11 IEIEtpqGLVKAVDR------MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERR 84
Cdd:cd03261 1 IELR---GLTKSFGGrtvlkgVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP----DSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RvIARDIAMIFQEPS--SCLDPSEKVGRQLIEsipsHSFEGKWWQRFKWRKKqaitlIHKVGIKDHSRLMDSysyELTDG 162
Cdd:cd03261 74 R-LRRRMGMLFQSGAlfDSLTVFENVAFPLRE----HTRLSEEEIREIVLEK-----LEAVGLRGAEDLYPA---ELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 163 QCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
250
....*....|..
gi 515624491 243 TQKLLDAPkHPY 254
Cdd:cd03261 221 PEELRASD-DPL 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-262 |
6.70e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.18 E-value: 6.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETpQGLVKA------VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNID 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAH-GGLSGKhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 75 LLQLTpKERRRVIARDIAMIFQEPSSCLDPSEKVGRQLIES---IPSHSFEGkwwqrfkwRKKQAITLIHKVGIKDhsRL 151
Cdd:PRK10419 76 LAKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPlrhLLSLDKAE--------RLARASEMLRAVDLDD--SV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 152 MDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK10419 145 LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMV 224
|
250 260 270
....*....|....*....|....*....|.
gi 515624491 232 MYCGQSVESADTQKLLdAPKHPYTVALLKAM 262
Cdd:PRK10419 225 MDNGQIVETQPVGDKL-TFSSPAGRVLQNAV 254
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-232 |
1.28e-31 |
|
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: 117.57 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 16 PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEVLVDGKDLTKLSLKELRR----KVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPSS---CLDPSEKV-----GRQLIEsipshsfegkwwqrfKWRKKQAITLIHKVGIKDhsrLMDSYSYELTDGQCQKV 167
Cdd:cd03225 82 QNPDDqffGPTVEEEVafgleNLGLPE---------------EEIEERVEEALELVGLEG---LRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-247 |
1.93e-31 |
|
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: 117.82 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 11 IEIE----TPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRv 86
Cdd:COG1122 1 IELEnlsfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP----TSGEVLVDGKDITKKNLRELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 87 iarDIAMIFQEPSScldpsekvgrQLIESI--------PshsfegkwwQRFKWRKKQAITLIHK----VGIKDhsrLMDS 154
Cdd:COG1122 76 ---KVGLVFQNPDD----------QLFAPTveedvafgP---------ENLGLPREEIRERVEEalelVGLEH---LADR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 155 YSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYC 234
Cdd:COG1122 131 PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDD 209
|
250
....*....|...
gi 515624491 235 GQSVESADTQKLL 247
Cdd:COG1122 210 GRIVADGTPREVF 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-261 |
4.57e-31 |
|
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: 117.02 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSAD--RMRLGNIDLLQLTPKERRRVIARDIAMIfqep 98
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI------NRLIEPTsgEIFIDGEDIREQDPVELRRKIGYVIQQI---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 ssCLDPSEKVgRQLIESIPShsFEGkwWQRFKwRKKQAITLIHKVGIkDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:cd03295 85 --GLFPHMTV-EENIALVPK--LLK--WPKEK-IRERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 179 ILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 515624491 259 LKA 261
Cdd:cd03295 236 VGA 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
7.17e-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: 114.84 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 5 DIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERr 84
Cdd:cd03214 1 EVENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL----LKPSSGEILLDGKDLASLSPKEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 rviARDIAMIFQepsscldpsekvgrqliesipshsfegkwwqrfkwrkkqaitLIHKVGIKDhsrLMDSYSYELTDGQC 164
Cdd:cd03214 72 ---ARKIAYVPQ------------------------------------------ALELLGLAH---LADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 165 QKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-249 |
2.00e-30 |
|
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: 115.47 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRVIARdIAMIFQE-- 97
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE----PSSGSILLEGTDITKLRGKKLRKLRRR-IGMIFQHyn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 ---PSSCLdpsEKVgrqLIESIPSHSFEGKWWQRFKWRKKQ-AITLIHKVGIKDHSrlmDSYSYELTDGQCQKVMIAMAI 173
Cdd:TIGR02315 90 lieRLTVL---ENV---LHGRLGYKPTWRSLLGRFSEEDKErALSALERVGLADKA---YQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-229 |
2.02e-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: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRViARDIAMIFQE 97
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGSVLIDGTDINKLKGKALRQL-RRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSScldpsekVGRQ------LIESIPSHSFEGKWWQRFKWRKKQ-AITLIHKVGIKDHSRLMDSysyELTDGQCQKVMIA 170
Cdd:cd03256 87 FNL-------IERLsvlenvLSGRLGRRSTWRSLFGLFPKEEKQrALAALERVGLLDKAYQRAD---QLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 171 MAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRI 229
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-254 |
2.54e-30 |
|
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: 115.08 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 11 IEIEtpqGLVKA------VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERR 84
Cdd:COG1127 6 IEVR---NLTKSfgdrvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL----LRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RvIARDIAMIFQepSSCLDPS----EKVGRQLIE--SIPShsfegkwwqrfKWRKKQAITLIHKVGIKDHSRLMDSysyE 158
Cdd:COG1127 79 E-LRRRIGMLFQ--GGALFDSltvfENVAFPLREhtDLSE-----------AEIRELVLEKLELVGLPGAADKMPS---E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
250
....*....|....*.
gi 515624491 239 ESADTQKLLDAPkHPY 254
Cdd:COG1127 222 AEGTPEELLASD-DPW 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-249 |
5.26e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.01 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 11 IEIEtpqGLVK------AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERR 84
Cdd:COG1131 1 IEVR---GLTKrygdktALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL------LRPTS---GEVRVLGEDVARDP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RVIARDIAMIFQEPSscLDPSEKVGRQLiesipshsfegKWWQRF-----KWRKKQAITLIHKVGIKDH-SRLMDSYSye 158
Cdd:COG1131 69 AEVRRRIGYVPQEPA--LYPDLTVRENL-----------RFFARLyglprKEARERIDELLELFGLTDAaDRKVGTLS-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 ltDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG1131 134 --GGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
250
....*....|.
gi 515624491 239 ESADTQKLLDA 249
Cdd:COG1131 211 ADGTPDELKAR 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-279 |
3.64e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.51 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 5 DIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKERR 84
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL--E--RPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RViARDIAMIFQE---PSScldpsekvgRQLIESI--PshsFEGKWWQRFKWRKKQAiTLIHKVGIKDHsrlMDSYSYEL 159
Cdd:PRK11153 79 KA-RRQIGMIFQHfnlLSS---------RTVFDNValP---LELAGTPKAEIKARVT-ELLELVGLSDK---ADRYPAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 515624491 240 SADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEKLQSLP 279
Cdd:PRK11153 222 QGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYLARLQAEP 261
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-254 |
4.54e-28 |
|
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: 114.55 E-value: 4.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 16 PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL----YEPTSGRILIDGIDLRQIDPASLRR----QIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPsscldpsekvgrQLIE-SI--------PSHSFEgkwwqrfkwrkkQAITLIHKVGIKDH-SRLMDSYSYELTD---- 161
Cdd:COG2274 556 QDV------------FLFSgTIrenitlgdPDATDE------------EIIEAARLAGLHDFiEALPMGYDTVVGEggsn 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 ---GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTItQWATRITVMYCGQSV 238
Cdd:COG2274 612 lsgGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIV 688
|
250
....*....|....*.
gi 515624491 239 ESADTQKLLDAPKHPY 254
Cdd:COG2274 689 EDGTHEELLARKGLYA 704
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-236 |
2.08e-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: 105.02 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQepss 100
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----LKPTSGEILIDGKDIAKLPLEELRR----RIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgrqliesipshsfegkwwqrfkwrkkqaitlihkvgikdhsrlmdsysyeLTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd00267 81 ----------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
2.22e-27 |
|
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: 107.82 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTP 80
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF----YRPTSGRILFDGRDITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 kerRRVIARDIAMIFQEPS-----SCLDpSEKVGRQlieSIPSHSFEGKWWQRFKWRK------KQAITLIHKVGIKDHs 149
Cdd:COG0411 74 ---HRIARLGIARTFQNPRlfpelTVLE-NVLVAAH---ARLGRGLLAALLRLPRARReerearERAEELLERVGLADR- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 150 rlMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRI 229
Cdd:COG0411 146 --ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRI 223
|
....*..
gi 515624491 230 TVMYCGQ 236
Cdd:COG0411 224 VVLDFGR 230
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-262 |
2.43e-27 |
|
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: 107.61 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTieieTPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGN-IDLLQLTP 80
Cdd:TIGR02323 2 PLLQVSGLS----KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAeLELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPSSCL----DPSEKVGRQLIESIPSHsfegkwwqrFKWRKKQAITLIHKVGIkDHSRLmDSYS 156
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRDGLrmrvSAGANIGERLMAIGARH---------YGNIRATAQDWLEEVEI-DPTRI-DDLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:TIGR02323 147 RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
250 260
....*....|....*....|....*.
gi 515624491 237 SVESADTQKLLDAPKHPYTVALLKAM 262
Cdd:TIGR02323 227 VVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-247 |
2.16e-26 |
|
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: 109.12 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLT---IEIEtpQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK----ENWkvsadrMRLGN-- 72
Cdd:TIGR03269 278 PIIKVRNVSkryISVD--RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsgEVN------VRVGDew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 73 IDLLQLTPKERRRViARDIAMIFQEPSscLDPSEKVGRQLIESIpshSFEgkwwQRFKWRKKQAITLIHKVGIKDHS--R 150
Cdd:TIGR03269 350 VDMTKPGPDGRGRA-KRYIGILHQEYD--LYPHRTVLDNLTEAI---GLE----LPDELARMKAVITLKMVGFDEEKaeE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQ----ILRLLSRMNQlnntTIVLIGHDLTTITQWA 226
Cdd:TIGR03269 420 ILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEMEQ----TFIIVSHDMDFVLDVC 495
|
250 260
....*....|....*....|.
gi 515624491 227 TRITVMYCGQSVESADTQKLL 247
Cdd:TIGR03269 496 DRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-236 |
2.79e-26 |
|
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: 104.06 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF----LRPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRviaRDIAMIFQEPS-----SCLDPSEkVGRQLIEsiPSHSFEGKWWQRFKWRKKQAITLIHKVGIkdhSRLMDSYSYE 158
Cdd:cd03219 73 AR---LGIGRTFQIPRlfpelTVLENVM-VAAQART--GSGLLLARARREEREARERAEELLERVGL---ADLADRPAGE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03219 144 LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-236 |
4.26e-26 |
|
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: 102.09 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKER 83
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL------LKPDS---GEIKVLGKDIKKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRVIARDIAMIFQEPSscLDPSEKVgRQLIEsipshsfegkwwqrfkwrkkqaitlihkvgikdhsrlmdsYSYeltdGQ 163
Cdd:cd03230 68 PEEVKRRIGYLPEEPS--LYENLTV-RENLK----------------------------------------LSG----GM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 164 CQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 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-26 |
|
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: 101.88 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckeNWKVSADrMRLGNIDLLQLTpkER 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---EEPDSGS-ILIDGEDLTDLE--DE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRVIARDIAMIFQEPssCLDPsekvgrqliesipshsfegkwwqrfkwrkkqaitlihkvgikdHSRLMDSYSYELTDGQ 163
Cdd:cd03229 71 LPPLRRRIGMVFQDF--ALFP-------------------------------------------HLTVLENIALGLSGGQ 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 164 CQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03229 106 QQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-238 |
9.50e-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: 103.69 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRvIARDIAMIFQEPss 100
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKP----TSGTVTIDGRDITAKKKKKLKD-LRKKVGLVFQFP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsEKvgrQLiesipshsFE---------GKwwQRFKWRKKQ----AITLIHKVGIKDHsrLMDSYSYELTDGQCQKV 167
Cdd:TIGR04521 92 -----EH---QL--------FEetvykdiafGP--KNLGLSEEEaeerVKEALELVGLDEE--YLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-232 |
1.05e-25 |
|
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: 102.16 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIdLLQLTPKER 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL------ERPTS---GEV-LVDGEPVTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRviaRDIAMIFQEPSscLDPsekvGRQLIESIpSHSFEGKWWQRfKWRKKQAITLIHKVGIKDHSrlmDSYSYELTDGQ 163
Cdd:cd03293 71 PG---PDRGYVFQQDA--LLP----WLTVLDNV-ALGLELQGVPK-AEARERAEELLELVGLSGFE---NAYPHQLSGGM 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 164 CQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-239 |
1.76e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKS----LVAKAIvgvckenwKVSADRMRLGNIDLLQLTPKE----RRRviardI 91
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKStllkLLYGEE--------RPTSGQVLVNGQDLSRLKRREipylRRR-----I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 92 AMIFQEPsscldpsekvgrQLIE--SIpshsFE---------GKwwqrfKWR--KKQAITLIHKVGIKDHsrlMDSYSYE 158
Cdd:COG2884 82 GVVFQDF------------RLLPdrTV----YEnvalplrvtGK-----SRKeiRRRVREVLDLVGLSDK---AKALPHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
.
gi 515624491 239 E 239
Cdd:COG2884 217 R 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
8.65e-25 |
|
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: 100.20 E-value: 8.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKS----LVAkaivGVckEnwKVSADRMRLGNIDLLQ 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKStllgLLA----GL--D--RPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 78 LTPKERRRVIARDIAMIFQE----PS-SCLD----PSEKVGRqliesipSHSFEgkwwqrfkwrkkQAITLIHKVGIKDh 148
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSfqllPTlTALEnvmlPLELAGR-------RDARA------------RARALLERVGLGH- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 149 srLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDL 219
Cdd:COG4181 139 --RLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP 207
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-232 |
9.91e-25 |
|
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: 98.22 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 16 PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIF 95
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL----YDPTSGEILIDGVDLRDLDLESLRKNIA----YVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPsscldpsekvgrqliesipsHSFEGkwwqrfkwrkkqaiTLIHKVgikdhsrlmdsysyeLTDGQCQKVMIAMAIAA 175
Cdd:cd03228 83 QDP--------------------FLFSG--------------TIRENI---------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMnqLNNTTIVLIGHDLTTITQwATRITVM 232
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-259 |
1.46e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGL-----VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMrlgnIDLLQ 77
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELL----IDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 78 LTPKERRRVIARdIAMIFQEPSSCLDPSEKVGrQLIEsIP---SHSFEGKWwqrfkwRKKQAITLIHKVGIK-DHSrlmD 153
Cdd:PRK15112 77 LHFGDYSYRSQR-IRMIFQDPSTSLNPRQRIS-QILD-FPlrlNTDLEPEQ------REKQIIETLRQVGLLpDHA---S 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 154 SYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
250 260
....*....|....*....|....*.
gi 515624491 234 CGQSVESADTQKLLDAPKHPYTVALL 259
Cdd:PRK15112 225 QGEVVERGSTADVLASPLHELTKRLI 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-246 |
1.51e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSAD--RMRLGNIDLLQL 78
Cdd:COG1129 2 EPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGV------YQPDsgEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 79 TPKErrrviARD--IAMIFQEPSSCLDPSekVGrqliESIpshsFEGKWWQRF---KWRK--KQAITLIHKVGIK-DHSR 150
Cdd:COG1129 72 SPRD-----AQAagIAIIHQELNLVPNLS--VA----ENI----FLGREPRRGgliDWRAmrRRARELLARLGLDiDPDT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 LMDsysyELTDGQCQKVMIAMAIAAKPKILIADEPTndlDPITQSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWATR 228
Cdd:COG1129 137 PVG----DLSVAQQQLVEIARALSRDARVLILDEPT---ASLTEREVERLFRIIRRLkaQGVAIIYISHRLDEVFEIADR 209
|
250
....*....|....*...
gi 515624491 229 ITVMYCGQSVESADTQKL 246
Cdd:COG1129 210 VTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-254 |
1.77e-24 |
|
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: 100.03 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:cd03294 18 FKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP----TSGKVLIDGQDIAAMSR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQepSSCLDPSEKVGRQL-----IESIPShsfegkwwqrfKWRKKQAITLIHKVGIKDHSrlmDSY 155
Cdd:cd03294 94 KELRELRRKKISMVFQ--SFALLPHRTVLENVafgleVQGVPR-----------AEREERAAEALELVGLEGWE---HKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 156 SYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPIT----QSQILRLLSRMNQlnntTIVLIGHDLTTITQWATRITV 231
Cdd:cd03294 158 PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIrremQDELLRLQAELQK----TIVFITHDLDEALRLGDRIAI 233
|
250 260
....*....|....*....|...
gi 515624491 232 MYCGQSVESADTQKLLDAPKHPY 254
Cdd:cd03294 234 MKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-246 |
2.14e-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: 98.79 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAD---RMRLGNIDLLQLTP 80
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRviarDIAMIFQEPSscldPSEKvgrqlieSIpshsFE----GKWWQRFKWRK------KQAITlihKVGIKD--H 148
Cdd:cd03260 77 LELRR----RVGMVFQKPN----PFPG-------SI----YDnvayGLRLHGIKLKEeldervEEALR---KAALWDevK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 149 SRLmdsYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQWATR 228
Cdd:cd03260 135 DRL---HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADR 209
|
250
....*....|....*...
gi 515624491 229 ITVMYCGQSVESADTQKL 246
Cdd:cd03260 210 TAFLLNGRLVEFGPTEQI 227
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-254 |
3.18e-24 |
|
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: 101.47 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQe 97
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEP----TAGQIFIDGENIMKQSPVELREVRRKKIGMVFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 pSSCLDPSEKVgRQLIESIPshsfEGKWWQRFKwRKKQAITLIHKVGIKDHsrlMDSYSYELTDGQCQKVMIAMAIAAKP 177
Cdd:TIGR01186 79 -QFALFPHMTI-LQNTSLGP----ELLGWPEQE-RKEKALELLKLVGLEEY---EHRYPDELSGGMQQRVGLARALAAEP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 178 KILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:TIGR01186 149 DILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEY 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
5.36e-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: 98.62 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIdllqLTP 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL------EKPTS---GEV----LVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPS-----SCLD----PSEKVGRQLIEsipshsfegkwwqrfkwRKKQAITLIHKVGIKDHsrl 151
Cdd:COG1116 72 GKPVTGPGPDRGVVFQEPAllpwlTVLDnvalGLELRGVPKAE-----------------RRERARELLELVGLAGF--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 152 MDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHD------Lttitqw 225
Cdd:COG1116 132 EDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvdeavfL------ 205
|
....*..
gi 515624491 226 ATRITVM 232
Cdd:COG1116 206 ADRVVVL 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-232 |
6.67e-24 |
|
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: 97.22 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIA-----RDIamifq 96
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL------LKPTS---GSIRVFGKPLEKERKRIGyvpqrRSI----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 97 EPSSCLDPSEKV--GRQliesipSHSFEGKWWQRFKWRKkqAITLIHKVGIKDHS-RLMDsysyELTDGQCQKVMIAMAI 173
Cdd:cd03235 80 DRDFPISVRDVVlmGLY------GHKGLFRRLSKADKAK--VDEALERVGLSELAdRQIG----ELSGGQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-236 |
5.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLlqlTPKE-RRRVIARDIAMIFQEPS 99
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP----TSGKIIIDGVDI---TDKKvKLSDIRKKVGLVFQYPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 SCLdpSEKVGRQLIESIPSHSFEGKwwQRFKWRKKQAITLihkVGIkDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPKI 179
Cdd:PRK13637 94 YQL--FEETIEKDIAFGPINLGLSE--EEIENRVKRAMNI---VGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 180 LIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-246 |
6.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP----TTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 CLDpSEKVGRQLIesipshsFEGKwwqRFKWR----KKQAITLIHKVGIkdhSR-LMDSYSYELTDGQCQKVMIAMAIAA 175
Cdd:PRK13646 97 QLF-EDTVEREII-------FGPK---NFKMNldevKNYAHRLLMDLGF---SRdVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-253 |
1.36e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.39 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQltPKERRRVIARDIAMIFQE 97
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--E--EITSGDLIVDGLKVND--PKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 ----PSscLDPSEKVGRQLIESIPSHSFEGKwwqrfkwrkKQAITLIHKVGIKDHsrlMDSYSYELTDGQCQKVMIAMAI 173
Cdd:PRK09493 86 fylfPH--LTALENVMFGPLRVRGASKEEAE---------KQARELLAKVGLAER---AHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLlsrMNQLNN--TTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKV---MQDLAEegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPP 228
|
..
gi 515624491 252 HP 253
Cdd:PRK09493 229 SQ 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-255 |
1.50e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.61 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGN-IDLLQLT 79
Cdd:PRK11701 4 QPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 80 PKERRRVIARDIAMIFQEPSSCLDPS----EKVGRQLIesipshsfeGKWWQRFKWRKKQAITLIHKVGIkDHSRLMD-- 153
Cdd:PRK11701 80 EAERRRLLRTEWGFVHQHPRDGLRMQvsagGNIGERLM---------AVGARHYGDIRATAGDWLERVEI-DAARIDDlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 154 -SYSyeltDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:PRK11701 150 tTFS----GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|...
gi 515624491 233 YCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYT 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-236 |
2.36e-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: 93.34 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTieiET-PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKE 82
Cdd:cd03263 1 LQIRNLT---KTyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGE------LRPTS---GTAYINGYSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RRRVIARDIAMIFQepSSCLDPsEKVGRQLIE------SIPSHSfegkwwqrfkwRKKQAITLIHKVGIKDHsrlMDSYS 156
Cdd:cd03263 69 DRKAARQSLGYCPQ--FDALFD-ELTVREHLRfyarlkGLPKSE-----------IKEEVELLLRVLGLTDK---ANKRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03263 132 RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-232 |
9.25e-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: 91.43 E-value: 9.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEietpQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03259 1 LELKGLSKT----YGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 rrviarDIAMIFQEPssCLDPSEKVgrqlIESIpshSFEGKwwqRFKWRKKQAITLIHK----VGIkdhSRLMDSYSYEL 159
Cdd:cd03259 73 ------NIGMVFQDY--ALFPHLTV----AENI---AFGLK---LRGVPKAEIRARVREllelVGL---EGLLNRYPHEL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-236 |
1.02e-21 |
|
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: 91.16 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERrrviarDIAMIFQe 97
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL----EEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 pSSCLDPSEKVGRQLIESIPSHSFegkwwqrfkwrKKQAITL-IHKVG-IKDHSRLMDSYSYELTDGQCQKVMIAMAIAA 175
Cdd:cd03301 80 -NYALYPHMTVYDNIAFGLKLRKV-----------PKDEIDErVREVAeLLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-238 |
1.32e-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: 89.80 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSAD--RMRLGNIDLLQLTPKERRRviaRDIAMIF 95
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL------YKPDsgEILVDGKEVSFASPRDARR---AGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QepsscldpsekvgrqliesipshsfegkwwqrfkwrkkqaitlihkvgikdhsrlmdsysyeLTDGQCQKVMIAMAIAA 175
Cdd:cd03216 82 Q--------------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 176 KPKILIADEPTNDLDPitqSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03216 100 NARLLILDEPTAALTP---AEVERLFKVIRRLraQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
27-257 |
1.82e-21 |
|
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: 91.24 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERrrviarDIAMIFQEpsSCLDPSE 106
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD----SGKILLNGKDITNLPPEKR------DISYVPQN--YALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 107 KVGRQlIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIkDHsrLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPT 186
Cdd:cd03299 87 TVYKN-IAYGLKKRKVDK-----KEIERKVLEIAEMLGI-DH--LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 187 NDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKhPYTVA 257
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK-NEFVA 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-218 |
3.90e-21 |
|
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: 89.77 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvCKENwKVSADRMRLGNIDLLQLtpkeRRRVIA---RDIAMIFQ 96
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLI---YKEE-LPTSGTIRVNGQDVSDL----RGRAIPylrRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 97 EpsSCLDPSEKVGRQLIESIPSHSFEGKWWQRfkwRKKQAITLihkVGIKDHSRlmdSYSYELTDGQCQKVMIAMAIAAK 176
Cdd:cd03292 86 D--FRLLPDRNVYENVAFALEVTGVPPREIRK---RVPAALEL---VGLSHKHR---ALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515624491 177 PKILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHD 218
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHA 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-239 |
5.35e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.84 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIetPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPK 81
Cdd:PRK13635 4 EIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLP----EAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRviarDIAMIFQEPSScldpsEKVGRQLIESIpSHSFEGKWWQRFKW--RKKQAItliHKVGIKDhsrLMDSYSYEL 159
Cdd:PRK13635 78 DVRR----QVGMVFQNPDN-----QFVGATVQDDV-AFGLENIGVPREEMveRVDQAL---RQVGMED---FLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVE 239
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-262 |
1.23e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQE 97
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 ----PSSCLDPSEKVGRQLiESIPSHSfegkwwqrfkwRKKQAITLIHKVGIKDHSRlmdSYSYELTDGQCQKVMIAMAI 173
Cdd:PRK10070 115 falmPHMTVLDNTAFGMEL-AGINAEE-----------RREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHP 253
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
....*....
gi 515624491 254 YTVALLKAM 262
Cdd:PRK10070 260 YVRTFFRGV 268
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
27-262 |
1.70e-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: 88.51 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLqLTPKERRRVIaRDIAMIFQepSSCLDP 104
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCI------NLleEPDSGTITVDGEDLT-DSKKDINKLR-RKVGMVFQ--QFNLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 105 SEKVGRQLIESiPSHSFegkwwqrfKWRKKQAI----TLIHKVGIKDHsrlMDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:COG1126 91 HLTVLENVTLA-PIKVK--------KMSKAEAEeramELLERVGLADK---ADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 181 IADEPTNDLDPITQSQILRLlsrMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDV---MRDLakEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
....
gi 515624491 259 LKAM 262
Cdd:COG1126 236 LSKV 239
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
238-305 |
1.81e-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: 1.81e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 238 VESADTQKLLDAPKHPYTVALLKAMPDFNdwiPHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC 305
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLD---PPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-232 |
1.92e-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: 88.20 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 13 IETpQGLVK------AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKERRRv 86
Cdd:cd03265 1 IEV-ENLVKkygdfeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK----PTSGRATVAGHDVVREPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 87 iardIAMIFQEPSscLDPsEKVGRqliESIPSHS-FEGKWWQRFKWRKKQAITLIHKVGIKDhsRLMDSYSyeltDGQCQ 165
Cdd:cd03265 75 ----IGIVFQDLS--VDD-ELTGW---ENLYIHArLYGVPGAERRERIDELLDFVGLLEAAD--RLVKTYS----GGMRR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03265 139 RLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII 205
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
236-323 |
2.18e-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: 83.95 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 236 QSVESADTQKLLDAPKHPYTVALLKAMPDFNDwipHKEKLQSLPGSIPPLQHLPIGCRLGPRCPYAQRQC-VEIPYTKRI 314
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKK---RDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECrKEPPALVEI 77
|
90
....*....|
gi 515624491 315 KS-HKFNCHF 323
Cdd:TIGR01727 78 AEgHRVACHL 87
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-236 |
6.99e-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: 85.56 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEietpqglvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL----RPPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrvIARDIAMIfqepsscldPSEkvgrqliesipshsfegkwwqrfkwRKKQAITLIHkvGIKDHSRLmdsySYELTD 161
Cdd:cd03215 71 DA---IRAGIAYV---------PED-------------------------RKREGLVLDL--SVAENIAL----SSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-238 |
8.81e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 85.77 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 5 DIRHLTIEIETPQGLVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDllqLTPKERR 84
Cdd:cd03226 1 RIENISFSYKKGTEILDDL---SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGKP---IKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RViardIAMIFQEPSSCLDpSEKVGRQLIESIPSHSFEgkwwqrfkwrKKQAITLIHKVGIkdhSRLMDSYSYELTDGQC 164
Cdd:cd03226 71 KS----IGYVMQDVDYQLF-TDSVREELLLGLKELDAG----------NEQAETVLKDLDL---YALKERHPLSLSGGQK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624491 165 QKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMnQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03226 133 QRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-244 |
1.88e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRViarDIAMIFQE 97
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGI----HEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 pSSCLDPSEKVGRQLIESIPSHSFEGKWWQRFKWRKKQAITLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAIAAKP 177
Cdd:PRK09700 89 -LSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLK---VDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 178 KILIADEPTNDLdpiTQSQILRLLSRMNQLNN--TTIVLIGHDLTTITQWATRITVMYCGQSVESADTQ 244
Cdd:PRK09700 165 KVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-232 |
1.97e-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: 87.06 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRviardIAMIFQE 97
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRP----TSGTARVAGYDVVREPRKVRRS-----IGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSscldPSEKV-GRQLIESIpshsfeGKWWQRFKW-RKKQAITLIHKVGIKDHS-RLMDSYSyeltDGQCQKVMIAMAIA 174
Cdd:TIGR01188 75 AS----VDEDLtGRENLEMM------GRLYGLPKDeAEERAEELLELFELGEAAdRPVGTYS----GGMRRRLDIAASLI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHDLTTITQWATRITVM 232
Cdd:TIGR01188 141 HQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAII 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-236 |
2.41e-19 |
|
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: 85.04 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIrGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLG---------NIDLlqltPKERRRviardIAMIFQE 97
Cdd:cd03297 18 DFDLNEEVT-GIFGASGAGKSTLLRCIAGLEK----PDGGTIVLNgtvlfdsrkKINL----PPQQRK-----IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSscLDPSEKVgRQLIEsipshsfegkWWQRFKWRKKQAITLIHKVGIKDHSRLMDSYSYELTDGQCQKVMIAMAIAAKP 177
Cdd:cd03297 84 YA--LFPHLNV-RENLA----------FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 178 KILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-244 |
2.47e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.93 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRrVIARDIAMIFQEPSS 100
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERP----SAGKIWFSGHDITRLKNREVP-FLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 CLDPS--EKVGRQLIesIPSHSFEgkwwqrfKWRKKQAITLiHKVGIKDHSRlmdSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:PRK10908 91 LMDRTvyDNVAIPLI--IAGASGD-------DIRRRVSAAL-DKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 179 ILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQ 244
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-255 |
4.65e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDR-MSLTLNEGEIRGLVGESGSGKSLVAKAI---VGVCKENWKVSADRMRLGNiDLLQLTPKERRRviarDIAMIFQ 96
Cdd:PRK14246 23 KAILKdITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKIKVDGKVLYFGK-DIFQIDAIKLRK----EVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 97 EPSSCldPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGI--KDHSRLmDSYSYELTDGQCQKVMIAMAIA 174
Cdd:PRK14246 98 QPNPF--PHLSIYDNIAYPLKSHGIKEK-----REIKKIVEECLRKVGLwkEVYDRL-NSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNqlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
.
gi 515624491 255 T 255
Cdd:PRK14246 248 T 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-247 |
5.17e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.04 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDLLQLT-PKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---------SGEIKIDGITiSKENLKEIRKKIGIIFQNPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsEKVGRQLIESIpSHSFEGKwwqRFKWRKKQAI--TLIHKVGIKDHsrlMDSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:PRK13632 95 -----QFIGATVEDDI-AFGLENK---KVPPKKMKDIidDLAKKVGMEDY---LDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 179 ILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLL 247
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
27-236 |
1.41e-18 |
|
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: 82.58 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLQltPKERRRVIARDIAMIFQepSSCLDP 104
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCI------NLleEPDSGTIIIDGLKLTD--DKKNINELRQKVGMVFQ--QFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 105 SEKVGRQLIESIPshsfegkwwQRFKWRKKQAIT----LIHKVGIKDHSrlmDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd03262 90 HLTVLENITLAPI---------KVKGMSKAEAEEraleLLEKVGLADKA---DAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 181 IADEPTNDLDPITQSQILRLlsrMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDV---MKDLaeEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-260 |
1.75e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.48 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGV---CKENWKVSADRMRL--GNIDLLQLTPKERRRVIARDIAMIFQEPS- 99
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLekpSEGSIVVNGQTINLvrDKDGQLKVADKNQLRLLRTRLTMVFQHFNl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 -SCLDPSEKVGRQLIESIPSHSFEGkwwqrfkwrKKQAITLIHKVGIKDHSRlmDSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:PRK10619 104 wSHMTVLENVMEAPIQVLGLSKQEA---------RERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 179 ILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPYTVAL 258
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQF 251
|
..
gi 515624491 259 LK 260
Cdd:PRK10619 252 LK 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-255 |
1.98e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.04 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKA------IVGVCKENWKVSADRMRLGNID 74
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLYPEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 75 LLQLtpkeRRRViardiAMIFQEPSSCLDPS--EKV--GRQLIESIPSHSfegKWWQRFKWRKKQAiTLIHKVgiKDHsr 150
Cdd:PRK14247 77 VIEL----RRRV-----QMVFQIPNPIPNLSifENValGLKLNRLVKSKK---ELQERVRWALEKA-QLWDEV--KDR-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 lMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK14247 140 -LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVA 216
|
250 260
....*....|....*....|....*
gi 515624491 231 VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK14247 217 FLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-248 |
2.55e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsadrmrL----GNIDLLQLTPKERRRVIARDIAMIF 95
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI-------------LvptsGEVRVLGYVPFKRRKEFARRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPSscldpsekvgrQLiesipshsfegkWW-----QRFKWRKKqaitlIHKVGIKDHSRLMDSYS--YELTD------- 161
Cdd:COG4586 102 GQRS-----------QL------------WWdlpaiDSFRLLKA-----IYRIPDAEYKKRLDELVelLDLGElldtpvr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 ----GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQS 237
Cdd:COG4586 154 qlslGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
250
....*....|.
gi 515624491 238 VESADTQKLLD 248
Cdd:COG4586 234 IYDGSLEELKE 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-255 |
3.38e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 19 LVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK--ENWKVSADRMRLG-NIDLLQLTPKERRRviarDIAMIF 95
Cdd:PRK14267 19 VIKGVD---LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEARVEGEVRLFGrNIYSPDVDPIEVRR----EVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPSS----CLDPSEKVGRQLIESIPShsfEGKWWQRFKWRKKQAiTLIHKVgiKDhsRLMDsYSYELTDGQCQKVMIAM 171
Cdd:PRK14267 92 QYPNPfphlTIYDNVAIGVKLNGLVKS---KKELDERVEWALKKA-ALWDEV--KD--RLND-YPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 172 AIAAKPKILIADEPTNDLDPITQSQILRLLSRMNqlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
....
gi 515624491 252 HPYT 255
Cdd:PRK14267 241 HELT 244
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-218 |
3.51e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MP---LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQ 77
Cdd:PRK10584 1 MPaenIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDG----SSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 78 LTPKERRRVIARDIAMIFQepSSCLDPS----EKVgrQLIESIPSHSFegkwwqrfKWRKKQAITLIHKVGIKDhsRLmD 153
Cdd:PRK10584 77 MDEEARAKLRAKHVGFVFQ--SFMLIPTlnalENV--ELPALLRGESS--------RQSRNGAKALLEQLGLGK--RL-D 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 154 SYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHD 218
Cdd:PRK10584 142 HLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
3.61e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIETpqglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAI----------------VGVCK--------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhVALCEkcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 59 ---ENWKVSADRMRLGNIDLLQLTPKERRRVIARdIAMIFQEpSSCLDPSEKVGRQLIESIPSHSFEGKWwqrfkwRKKQ 135
Cdd:TIGR03269 77 kvgEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKR-IAIMLQR-TFALYGDDTVLDNVLEALEEIGYEGKE------AVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 136 AITLIHKVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLI 215
Cdd:TIGR03269 149 AVDLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
250
....*....|....*.
gi 515624491 216 GH------DLTTITQW 225
Cdd:TIGR03269 226 SHwpevieDLSDKAIW 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-232 |
4.20e-18 |
|
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: 82.00 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 19 LVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKERRRVIARDIAMIFQEP 98
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL---------QPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 SscldpsekvgrQLIESIP---SHSFEGKWWQ----RFKWRKKQAITLIhkvgikDHSRLMDSYSYELTDGQCQKVMIAM 171
Cdd:cd03267 104 T-----------QLWWDLPvidSFYLLAAIYDlppaRFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 172 AIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-232 |
6.39e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 84.45 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPS- 99
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YDPTSGRILIDGVDIRDLTLESLRRQIG----VVPQDTFl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 -----------SCLDPSEKvgrQLIESIpshsfegkwwqrfkwRKKQAITLIHkvgikdhsRLMDSYSYELTD------- 161
Cdd:COG1132 426 fsgtireniryGRPDATDE---EVEEAA---------------KAAQAHEFIE--------ALPDGYDTVVGErgvnlsg 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQwATRITVM 232
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVL 547
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-236 |
7.49e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRMRLGNIDLLQLTPKERRRvIARDI-------AM 93
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTVQREGR-LARDIrksrantGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 94 IFQEPS--SCLDPSEKVgrqLIESIPSHSFegkWWQRFKW----RKKQAITLIHKVGIKD--HSRLMdsysyELTDGQCQ 165
Cdd:PRK09984 91 IFQQFNlvNRLSVLENV---LIGALGSTPF---WRTCFSWftreQKQRALQALTRVGMVHfaHQRVS-----TLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-260 |
7.55e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKErrrvIARDIAMIFQEPsscL 102
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP----QSGTVFLGDKPISMLSSRQ----LARRLALLPQHH---L 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 DPSEKVGRQLIE--SIPSHSFEGKWWQRFKWRKKQAITLIHKVGIKDHsRLMDsysyeLTDGQCQKVMIAMAIAAKPKIL 180
Cdd:PRK11231 87 TPEGITVRELVAygRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADR-RLTD-----LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAdtqklldAPKHPYTVALLK 260
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG-------TPEEVMTPGLLR 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-286 |
1.47e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQglvkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERrrviarDIAMIFQepSSCLDPSEKVGRQLIESIPSHSFEGKwwqRFKWRKKQAITLIHkvgikdhsrlMDSYS---- 156
Cdd:PRK11607 89 YQR------PINMMFQ--SYALFPHMTVEQNIAFGLKQDKLPKA---EIASRVNEMLGLVH----------MQEFAkrkp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPI----TQSQILRLLSRMnqlnNTTIVLIGHDLTTITQWATRITVM 232
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIM 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 233 YCGQSVESADTQKLLDAPKHPYTVALLKAMPDFNDWIPHKEK----LQSlPGSIPPLQ 286
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGVLKERQEdglvIDS-PGLVHPLK 280
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-249 |
2.04e-17 |
|
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: 80.22 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGV-CKENWKVSADRMRLGNIDLLQLtpkeRRRViardiAMIFQEpss 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWL----RRQV-----GVVLQE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpSEKVGRQLIESIPSHSfEGKWWQRFKWRKKQAitlihkvGIKDHSRLMDSySYE---------LTDGQCQKVMIAM 171
Cdd:cd03252 85 ----NVLFNRSIRDNIALAD-PGMSMERVIEAAKLA-------GAHDFISELPE-GYDtivgeqgagLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 172 AIAAKPKILIADEPTNDLDPITQSQILRLLSRMnqLNNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLLDA 249
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-247 |
2.29e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.91 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETpQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENW---KVSADRMRLGNIDLLQlt 79
Cdd:PRK13642 4 ILEVENLVFKYEK-ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEgkvKIDGELLTAENVWNLR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 80 pkerrrviaRDIAMIFQEPSScldpsEKVGrQLIESIPSHSFEGKWWQRFKWRKK--QAITLIHKVGIKDHSrlmdsySY 157
Cdd:PRK13642 81 ---------RKIGMVFQNPDN-----QFVG-ATVEDDVAFGMENQGIPREEMIKRvdEALLAVNMLDFKTRE------PA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQS 237
Cdd:PRK13642 140 RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
250
....*....|
gi 515624491 238 VESADTQKLL 247
Cdd:PRK13642 219 IKEAAPSELF 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-246 |
2.56e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPqglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:COG3845 256 VVLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL----RPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRviaRDIAMIfqepsscldPSEKVGRQLI-----------ESIPSHSFEGKWWQRFKWRKKQAITLIHKVGIK--DH 148
Cdd:COG3845 329 ERRR---LGVAYI---------PEDRLGRGLVpdmsvaenlilGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRtpGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 149 SRLMDSYSyeltdG--QcQKVMIAMAIAAKPKILIADEPTNDLDPITQSQIL-RLLSRMNQlnNTTIVLIGHDLTTITQW 225
Cdd:COG3845 397 DTPARSLS-----GgnQ-QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHqRLLELRDA--GAAVLLISEDLDEILAL 468
|
250 260
....*....|....*....|....*.
gi 515624491 226 ATRITVMYCGQ-----SVESADTQKL 246
Cdd:COG3845 469 SDRIAVMYEGRivgevPAAEATREEI 494
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-249 |
2.63e-17 |
|
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: 79.58 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvcKENWKVSADRMRLGNIDLLQLTPKERRR--------------V 86
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLI----PRFYDVDSGRILIDGHDVRDYTLASLRRqiglvsqdvflfndT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 87 IARDIAmiFQEPSSCLDPSEKVGR-----QLIESIPshsfegkwwqrfkwrkKQAITLIHKVGIKdhsrlmdsysyeLTD 161
Cdd:cd03251 92 VAENIA--YGRPGATREEVEEAARaanahEFIMELP----------------EGYDTVIGERGVK------------LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVlIGHDLTTITQwATRITVMYCGQSVESA 241
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
....*...
gi 515624491 242 DTQKLLDA 249
Cdd:cd03251 219 THEELLAQ 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-261 |
2.91e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.41 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERrrviarDIAMIFQE----PSS 100
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP----DSGRILWNGQDLTALPPAER------PVSMLFQEnnlfPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 C--------LDPSEKVGRQliesipshsfegkwwqrfkwRKKQAITLIHKVGIKDhsrLMDSYSYELTDGQCQKVMIAMA 172
Cdd:COG3840 87 TvaqniglgLRPGLKLTAE--------------------QRAQVEQALERVGLAG---LLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 173 IAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKH 252
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*....
gi 515624491 253 PYTVALLKA 261
Cdd:COG3840 224 PALAAYLGI 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
3.21e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.08 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPqglvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADrmrlGNIDLLQLTP 80
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVE----GRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERR---RVIARDIAMIFQEPS----SCLDpSEKVGRQLIesipshsfegkwwqrfKWRKKQAITLIHKVGIKDhSRLMD 153
Cdd:PRK14258 77 YERRvnlNRLRRQVSMVHPKPNlfpmSVYD-NVAYGVKIV----------------GWRPKLEIDDIVESALKD-ADLWD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 154 SYSY-------ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQwA 226
Cdd:PRK14258 139 EIKHkihksalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR-L 217
|
250 260 270
....*....|....*....|....*....|
gi 515624491 227 TRITVMY------CGQSVESADTQKLLDAP 250
Cdd:PRK14258 218 SDFTAFFkgnenrIGQLVEFGLTKKIFNSP 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-247 |
3.85e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKS-----LVAKAIVGVCKENW-------KVSADRMRLGNIDLLQLTPKERR---- 84
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEKLVIQKTRFKKikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 85 RVIARDIAMIFQEPSScldpsekvgrQLIESIPSH-------SFeGKWWQRFKWRKKQAITLihkVGIkDHSRLMDSySY 157
Cdd:PRK13651 101 KEIRRRVGVVFQFAEY----------QLFEQTIEKdiifgpvSM-GVSKEEAKKRAAKYIEL---VGL-DESYLQRS-PF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQS 237
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
250
....*....|
gi 515624491 238 VESADTQKLL 247
Cdd:PRK13651 244 IKDGDTYDIL 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
4.36e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETpQGLVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNW--KVSADRMRLGNIDLLQL 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHG-QTVLHGID---LEVKPGEVVAIIGPSGSGKTTLLRCI------NLleQPEAGTIRVGDITIDTA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 79 TP----KERRRVIARDIAMIFQepSSCLDPSekvgRQLIESIpshsFEGKWWQRfKWRKKQAIT----LIHKVGIKDHSr 150
Cdd:PRK11264 71 RSlsqqKGLIRQLRQHVGFVFQ--NFNLFPH----RTVLENI----IEGPVIVK-GEPKEEATArareLLAKVGLAGKE- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 lmDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11264 139 --TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAI 215
|
250 260
....*....|....*....|....*
gi 515624491 231 VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:PRK11264 216 FMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
4.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNidllQLTPKERRRVIARDIAMIFQEPSSc 101
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI----EKVKSGEIFYNN----QAITDDNFEKLRKHIGIVFQNPDN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 ldpsekvgrQLIESI---------PSHSFEGKWWQRfkwRKKQAITlihKVGIKDHSrlmDSYSYELTDGQCQKVMIAMA 172
Cdd:PRK13648 95 ---------QFVGSIvkydvafglENHAVPYDEMHR---RVSEALK---QVDMLERA---DYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515624491 173 IAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLT 220
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-247 |
8.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 8.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMrlgnIDLLQLTPkERRRVIARDIAMIFQEPSScl 102
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE---SGQII----IDGDLLTE-ENVWDIRHKIGMVFQNPDN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 dpsEKVGrQLIESIPSHSFEGKW--WQRFKWRKKQAITLihkVGIKDhsrLMDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:PRK13650 93 ---QFVG-ATVEDDVAFGLENKGipHEEMKERVNEALEL---VGMQD---FKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITqWATRITVMYCGQsVESADTQKLL 247
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTPREL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-250 |
9.79e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKaIVGvckENWKVSADRMRLGNIDLLQLTPKerrrVIARDIAMIFQEpsscLDPS 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLK-MLG---RHQPPSEGEILLDAQPLESWSSK----AFARKVAYLPQQ----LPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 106 EKVG-RQL--IESIPSHSFEGKWWQRFKWRKKQAITLihkVGIKD-HSRLMDSysyeLTDGQCQKVMIAMAIAAKPKILI 181
Cdd:PRK10575 98 EGMTvRELvaIGRYPWHGALGRFGAADREKVEEAISL---VGLKPlAHRLVDS----LSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 182 ADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-255 |
1.20e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvCKENWKVSADRMRlGNIDLLQLTPKERRRVIA--RDIAMIFQEPS- 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTL---NRMNDKVSGYRYS-GDVLLGGRSIFNYRDVLEfrRRVGMLFQRPNp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 ---SCLDpSEKVGRQLIESIPSHSFEGKWWQRfkwrkkqaitlIHKVGIKD--HSRLMDSySYELTDGQCQKVMIAMAIA 174
Cdd:PRK14271 113 fpmSIMD-NVLAGVRAHKLVPRKEFRGVAQAR-----------LTEVGLWDavKDRLSDS-PFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMnqLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
.
gi 515624491 255 T 255
Cdd:PRK14271 258 T 258
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-219 |
1.20e-16 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 79.76 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTI--------------------EIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeN 60
Cdd:COG4175 1 MPKIEVRNLYKifgkrperalklldqgkskdEILEKTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCL------N 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 61 --WKVSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQepsscldpsekvgrqliesipshSF----------------- 121
Cdd:COG4175 75 rlIEPTAGEVLIDGEDITKLSKKELRELRRKKMSMVFQ-----------------------HFallphrtvlenvafgle 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 122 ---EGKwwqrfKWRKKQAITLIHKVGIKDHSrlmDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPIT----Q 194
Cdd:COG4175 132 iqgVPK-----AERRERAREALELVGLAGWE---DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIrremQ 203
|
250 260
....*....|....*....|....*
gi 515624491 195 SQILRLLSRMNQlnntTIVLIGHDL 219
Cdd:COG4175 204 DELLELQAKLKK----TIVFITHDL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-243 |
1.38e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKS-LVaKAIVGVckenwkVSADRmrlGNIdLL--- 76
Cdd:COG3845 3 PPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKStLM-KILYGL------YQPDS---GEI-LIdgk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 77 QLTPKERRRVIARDIAMIFQEPSscLdpsekvgrqliesIPSHS--------FEGKWWQRFKWRK--KQAITLIHKVGIK 146
Cdd:COG3845 68 PVRIRSPRDAIALGIGMVHQHFM--L-------------VPNLTvaenivlgLEPTKGGRLDRKAarARIRELSERYGLD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 147 -DhsrlMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLdpiTQSQILRLLSRMNQL--NNTTIVLIGHDLTTIT 223
Cdd:COG3845 133 vD----PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRLaaEGKSIIFITHKLREVM 205
|
250 260
....*....|....*....|
gi 515624491 224 QWATRITVMYCGQSVESADT 243
Cdd:COG3845 206 AIADRVTVLRRGKVVGTVDT 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-232 |
1.67e-16 |
|
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: 77.82 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEietpQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckENWKVSADRM-----RLGNIDL 75
Cdd:COG1119 1 DPLLELRNVTVR----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---DLPPTYGNDVrlfgeRRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 76 LQLtpkeRRR--VIARDIAMIFQEPSSCLDpsekvgrqLIESipshsfeGKW-----WQRFKWR-KKQAITLIHKVGIKD 147
Cdd:COG1119 74 WEL----RKRigLVSPALQLRFPRDETVLD--------VVLS-------GFFdsiglYREPTDEqRERARELLELLGLAH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 148 hsrLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWAT 227
Cdd:COG1119 135 ---LADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGIT 211
|
....*
gi 515624491 228 RITVM 232
Cdd:COG1119 212 HVLLL 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-241 |
1.74e-16 |
|
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: 76.87 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsadrmrlgnidllqltpkerrrvIARDIAMIFQE 97
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL------------------------------IKPDSGEITFD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSSCLDPSEKVGR--QLIESipsHSFEG--------KWWQRFKWRKKQAI-TLIHKVGIKDH-SRLMDSYSYeltdGQCQ 165
Cdd:cd03268 61 GKSYQKNIEALRRigALIEA---PGFYPnltarenlRLLARLLGIRKKRIdEVLDVVGLKDSaKKKVKGFSL----GMKQ 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:cd03268 134 RLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-251 |
1.87e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.33 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP----SSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgrQLIESIPSHSFE------GKWWQRfkwRKKQAITLIHKVGIKDHsrLMDSYSYELTDGQCQKVMIAMAIA 174
Cdd:PRK13641 97 ----------QLFENTVLKDVEfgpknfGFSEDE---AKEKALKWLKKVGLSED--LISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMnQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-255 |
2.03e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAI--VGVCKENWKVSADRMRLG-NIdllqLTPKERRRVIARDIAMIFQE 97
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGhNI----YSPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSScldpsekvgrqliesIPSHSFEGKWWQ-RFKWRKKQAItLIHKVG-----------IKDhsRLMDSySYELTDGQCQ 165
Cdd:PRK14239 95 PNP---------------FPMSIYENVVYGlRLKGIKDKQV-LDEAVEkslkgasiwdeVKD--RLHDS-ALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQK 245
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQ 233
|
250
....*....|
gi 515624491 246 LLDAPKHPYT 255
Cdd:PRK14239 234 MFMNPKHKET 243
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-236 |
2.09e-16 |
|
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: 75.72 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPKERRRVI---ARDIamifqeps 99
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILG----LLRPTSGRVRLDGADISQWDPNELGDHVgylPQDD-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 scldpsekvgrQLiesipshsFEGkwwqrfkwrkkqaiTLIHKVgikdhsrlmdsysyeLTDGQCQKVMIAMAIAAKPKI 179
Cdd:cd03246 86 -----------EL--------FSG--------------SIAENI---------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 180 LIADEPTNDLDPITQSQILRLLSRMnQLNNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-238 |
2.68e-16 |
|
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: 76.17 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE---------NWKVSADRMRLGNIdllqltPKERRrvia 88
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdsgevlfdgKPLDIAARNRIGYL------PEERG---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 89 rdiamifqepsscLDPSEKVGRQLIesipshsfegkWWQRFKWRKKQAIT-----LIHKVGIKDH--SRLMdsysyELTD 161
Cdd:cd03269 81 -------------LYPKMKVIDQLV-----------YLAQLKGLKKEEARrrideWLERLELSEYanKRVE-----ELSK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQ---SQILRLLSRmnqlNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03269 132 GNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVellKDVIRELAR----AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-257 |
2.89e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTPKErrrviaRDIAMIFQEPS 99
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL--E--DPTSGEILIGGRDVTDLPPKD------RNIAMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 scLDPS-------------EKVGRQLIESipshsfegkwwqrfkwRKKQAITLihkVGIKDhsrLMDSYSYELTDGQCQK 166
Cdd:COG3839 86 --LYPHmtvyeniafplklRKVPKAEIDR----------------RVREAAEL---LGLED---LLDRKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 167 VMIAMAIAAKPKILIADEPTNDLDP----ITQSQILRLLSRMnqlnNTTIVLIGHDLT---TItqwATRITVMYCGQSVE 239
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL----GTTTIYVTHDQVeamTL---ADRIAVMNDGRIQQ 214
|
250
....*....|....*...
gi 515624491 240 SADTQKLLDAPKHPYtVA 257
Cdd:COG3839 215 VGTPEELYDRPANLF-VA 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-251 |
3.03e-16 |
|
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: 76.51 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRrviardIAMIFQepSSC 101
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPTSGEILLDGKDITNLPPHKRP------VNTVFQ--NYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LDPSEKVGRQLIESIpshsfegkwwqRFKWRKKQAIT-----LIHKVGIKDHSRLMDSysyELTDGQCQKVMIAMAIAAK 176
Cdd:cd03300 83 LFPHLTVFENIAFGL-----------RLKKLPKAEIKervaeALDLVQLEGYANRKPS---QLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 177 PKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-248 |
3.83e-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: 75.93 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERrrvIARDIAMIFQe 97
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL----LPPRSGSIRFDGRDITGLPPHER---ARAGIGYVPE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 psscldpsekvGRQLIesiPSHSFE--------GKWWQRFKWRKKQAITLIhkvgikdhSRL---MDSYSYELTDGQCQK 166
Cdd:cd03224 83 -----------GRRIF---PELTVEenlllgayARRRAKRKARLERVYELF--------PRLkerRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 167 VMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLnNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
..
gi 515624491 247 LD 248
Cdd:cd03224 220 LA 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-219 |
3.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIetPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLgNIDLLQLTPKER 83
Cdd:PRK13640 6 VEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPD---DNPNSKI-TVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRVIARdIAMIFQEPSScldpsEKVGRQLIESIpSHSFEGKWWQRfkwrkKQAITLIHK----VGIKDHsrlMDSYSYEL 159
Cdd:PRK13640 80 WDIREK-VGIVFQNPDN-----QFVGATVGDDV-AFGLENRAVPR-----PEMIKIVRDvladVGMLDY---IDSEPANL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDL 219
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-235 |
4.74e-16 |
|
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: 75.87 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQlTPKE 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEP----DAGFATVDGFDVVK-EPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 83 RRRVIArdiamiFQEPSSCLDPSEKVGRQLiesipshsfegKWWQRFKWRKKQAIT-----LIHKVGIKDhsrLMDSYSY 157
Cdd:cd03266 76 ARRRLG------FVSDSTGLYDRLTARENL-----------EYFAGLYGLKGDELTarleeLADRLGMEE---LLDRRVG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDpITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-242 |
6.78e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWK-------VSADRMRLGNIDLLQLTPKERR-RVIARDI 91
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiYIGDKKNNHELITNPYSKKIKNfKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 92 AMIFQEPSSCL--DPSEK--------VGRQLIESipshsfegkwwqrfkwrKKQAITLIHKVGIKDhsRLMDSYSYELTD 161
Cdd:PRK13631 119 SMVFQFPEYQLfkDTIEKdimfgpvaLGVKKSEA-----------------KKLAKFYLNKMGLDD--SYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESA 241
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
.
gi 515624491 242 D 242
Cdd:PRK13631 259 T 259
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-249 |
8.79e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 38 LVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTpkerRRVIARDIAMIFQEPSSCLDP---SEKVGRQLIE 114
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMG----YYPLTEGEIRLDGRPLSSLS----HSVLRQGVAMVQQDPVVLADTflaNVTLGRDISE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 115 SipshsfegKWWQRFKwrKKQAITLIHKV--GIkdHSRLMDSYSyELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPI 192
Cdd:PRK10790 444 E--------QVWQALE--TVQLAELARSLpdGL--YTPLGEQGN-NLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 193 TQSQILRLLSRMNQlnNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK10790 511 TEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-240 |
2.65e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.78 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP----TQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgrQLIES--IPSHSFEGkwwQRFKWRKKQAITL----IHKVGIKDHsrLMDSYSYELTDGQCQKVMIAMAIA 174
Cdd:PRK13649 97 ----------QLFEEtvLKDVAFGP---QNFGVSQEEAEALarekLALVGISES--LFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
2.74e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTP 80
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KErrrvIARDIAMIFQEPSSCLDPSekvGRQLIE--SIPSHSFEGKWWQRFKWRKKQAitlIHKVGIkdhSRLMDSYSYE 158
Cdd:PRK09536 73 RA----ASRRVASVPQDTSLSFEFD---VRQVVEmgRTPHRSRFDTWTETDRAAVERA---MERTGV---AQFADRPVTS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIgHDL 219
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDL 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-254 |
4.78e-15 |
|
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: 73.53 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKErrrviaRDIAMIFQEPS- 99
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD----SGTILFGGEDATDVPVQE------RNVGFVFQHYAl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 -SCLDPSEKVGRQLiESIPSHSFEGKwwQRFKWRKKQAITLIHKvgikdhSRLMDSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:cd03296 86 fRHMTVFDNVAFGL-RVKPRSERPPE--AEIRAKVHELLKLVQL------DWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 179 ILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPKHPY 254
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-238 |
6.26e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.27 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrviARDIAMIFQepSSCLD---PSEKV---GRqliesIPshsfegkwWQRFKWRKKQAI-TLIHKVGIkdhSRLMDS 154
Cdd:PRK13548 73 EL----ARRRAVLPQ--HSSLSfpfTVEEVvamGR-----AP--------HGLSRAEDDALVaAALAQVDL---AHLAGR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 155 YSYELTDGQCQKVMIAMAIA------AKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATR 228
Cdd:PRK13548 131 DYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADR 210
|
250
....*....|
gi 515624491 229 ITVMYCGQSV 238
Cdd:PRK13548 211 IVLLHQGRLV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-248 |
6.71e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.62 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQepss 100
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI----YLPQRGRVKVMGREVNAENEKWVRS----KVGLVFQ---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 clDPSEKVgrqliesipshsFEGKWWQ--------------RFKWRKKQAITLihkVGIKDhsrLMDSYSYELTDGQCQK 166
Cdd:PRK13647 87 --DPDDQV------------FSSTVWDdvafgpvnmgldkdEVERRVEEALKA---VRMWD---FRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 167 VMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
..
gi 515624491 247 LD 248
Cdd:PRK13647 226 TD 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-238 |
9.87e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSS 100
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP----TEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 CLdpsekvgrqLIESIPSHSFEGKwwQRFKWRKKQAITL----IHKVGIKdhSRLMDSYSYELTDGQCQKVMIAMAIAAK 176
Cdd:PRK13643 96 QL---------FEETVLKDVAFGP--QNFGIPKEKAEKIaaekLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 177 PKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-240 |
1.09e-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: 71.19 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSadrmrLGNIDLLQLTPKERRRVIARDIAMIFQEPss 100
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG----DLKPQ-----QGEITLDGVPVSDLEKALSSLISVLNQRP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgrqliesipsHSFEGkwwqrfkwrkkqaiTLIHKVGIKdhsrlmdsysyeLTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd03247 85 ------------------YLFDT--------------TLRNNLGRR------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 181 IADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVES 240
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-250 |
1.16e-14 |
|
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: 73.98 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkvsAD--RMRLGNiDLLQLT------PKERRRviardIAMIFQEP 98
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLER------PDsgRIRLGG-EVLQDSargiflPPHRRR-----IGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 SscLDPSEKVGRQLiesipshsfEGKWWQRFKWRKK----QAITLihkVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIA 174
Cdd:COG4148 87 R--LFPHLSVRGNL---------LYGRKRAPRAERRisfdEVVEL---LGI---GHLLDRRPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAP 250
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-255 |
1.18e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 72.76 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNwkvsadRM------------- 68
Cdd:COG1117 10 PKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL------N------RMndlipgarvegei 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 69 RLGNIDLLQLT---PKERRRViardiAMIFQEPSscldPSEKvgrqlieSIpshsFE---------GkwwqrfkWRKKQA 136
Cdd:COG1117 74 LLDGEDIYDPDvdvVELRRRV-----GMVFQKPN----PFPK-------SI----YDnvayglrlhG-------IKSKSE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 137 I-----TLIHKVGI----KDhsRLMDSySYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQL 207
Cdd:COG1117 127 LdeiveESLRKAALwdevKD--RLKKS-ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEEL---ILEL 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515624491 208 -NNTTIVLIGHDLttitQWATRIT----VMYCGQSVESADTQKLLDAPKHPYT 255
Cdd:COG1117 201 kKDYTIVIVTHNM----QQAARVSdytaFFYLGELVEFGPTEQIFTNPKDKRT 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-217 |
1.25e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 24 DRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwkvsadrmrlgnidllqltpkerrrviardiAMIFQEPSSCLD 103
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG------------------------------------ALKGTPVAGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 104 -PSEKVGRQ--LIESIPShsfegkwwqrfKWRKKQAITLIHKVGIKDHSRLMDSYSyELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:COG2401 91 vPDNQFGREasLIDAIGR-----------KGDFKDAVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGH 217
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-246 |
2.45e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWK----VSADRMRLGNIdl 75
Cdd:PRK13549 3 EYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgTYEgeiiFEGEELQASNI-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 76 lqltpkerRRVIARDIAMIFQEPSscLDPSEKVGrqliESIpshsFEGKWWQRFK---WRK--KQAITLIHKVG--IKDH 148
Cdd:PRK13549 77 --------RDTERAGIAIIHQELA--LVKELSVL----ENI----FLGNEITPGGimdYDAmyLRAQKLLAQLKldINPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 149 SRLMDsysyeLTDGQCQKVMIAMAIAAKPKILIADEPTNDLdpiTQSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWA 226
Cdd:PRK13549 139 TPVGN-----LGLGQQQLVEIAKALNKQARLLILDEPTASL---TESETAVLLDIIRDLkaHGIACIYISHKLNEVKAIS 210
|
250 260
....*....|....*....|
gi 515624491 227 TRITVMYCGQSVESADTQKL 246
Cdd:PRK13549 211 DTICVIRDGRHIGTRPAAGM 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-218 |
3.11e-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: 70.14 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 17 QGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRL--GNIDLLQLtpkeRRRViardiAM 93
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGEPLdySRKGLLER----RQRV-----GL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 94 IFQEPSSCL---DPSEKVG---RQLiesipshsfeGKWWQRFKWRKKQAITLIhkvgikDHSRLMDSYSYELTDGQCQKV 167
Cdd:TIGR01166 73 VFQDPDDQLfaaDVDQDVAfgpLNL----------GLSEAEVERRVREALTAV------GASGLRERPTHCLSGGEKKRV 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHD 218
Cdd:TIGR01166 137 AIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRA-EGMTVVISTHD 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-249 |
4.12e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEietpqGLVKAVdrmSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPK 81
Cdd:COG1129 255 VVLEVEGLSVG-----GVVRDV---SFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrvIARDIAMIfqepsscldPSEkvgRQ-----LIESI------PS-HSFEGKWWQRFKWRKKQAITLIHKVGIK--D 147
Cdd:COG1129 323 DA---IRAGIAYV---------PED---RKgeglvLDLSIrenitlASlDRLSRGGLLDRRRERALAEEYIKRLRIKtpS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 148 HSRLMDSYSyeltdG--QcQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQL--NNTTIVLIGHDLTTIT 223
Cdd:COG1129 388 PEQPVGNLS-----GgnQ-QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL---IRELaaEGKAVIVISSELPELL 458
|
250 260 270
....*....|....*....|....*....|.
gi 515624491 224 QWATRITVMYCGQSV-----ESADTQKLLDA 249
Cdd:COG1129 459 GLSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
27-257 |
4.13e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSADRMRLgNI-----DLLQLTPKERRRVIARDIAMIFQEPSsc 101
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVL------NLLEMPRSGTL-NIagnhfDFSKTPSDKAIRELRRNVGMVFQQYN-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LDPSEKVGRQLIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGIKDHSrlmDSYSYELTDGQCQKVMIAMAIAAKPKILI 181
Cdd:PRK11124 93 LWPHLTVQQNLIEAPCRVLGLSK-----DQALARAEKLLERLRLKPYA---DRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 182 ADEPTNDLDPITQSQIlrlLSRMNQLNNTTI--VLIGHDLTTITQWATRITVMYCGQSVESADTqkllDAPKHPYTVA 257
Cdd:PRK11124 165 FDEPTAALDPEITAQI---VSIIRELAETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDA----SCFTQPQTEA 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-236 |
6.97e-14 |
|
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: 69.53 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGeIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKERRRVIARDIAMIFQEPSs 100
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLT---------PPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cLDPSEKVGRQL-----IESIPShsfegkwwqrfKWRKKQAITLIHKVGIKDH-SRLMDSYSyeltDGQCQKVMIAMAIA 174
Cdd:cd03264 83 -VYPNFTVREFLdyiawLKGIPS-----------KEVKARVDEVLELVNLGDRaKKKIGSLS----GGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-237 |
1.04e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEietpqGLVKavdrMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK15439 267 PVLTVEDLTGE-----GFRN----ISLEVRAGEILGLAGVVGAGRTELAETLYGL----RPARGGRIMLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrvIARDIAMIFQEPSSC---LDPSekvgrqLIESIPSHSFEGK-WWQRfkwRKKQAITL---IHKVGIK-DHSrlmD 153
Cdd:PRK15439 334 QR---LARGLVYLPEDRQSSglyLDAP------LAWNVCALTHNRRgFWIK---PARENAVLeryRRALNIKfNHA---E 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 154 SYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMH 477
|
....
gi 515624491 234 CGQS 237
Cdd:PRK15439 478 QGEI 481
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-238 |
1.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.12 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG-VCKENWKVSADRMRLGNIdllqltpkERRRVIARDIAMIFQEPSS 100
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAlLIPSEGKVYVDGLDTSDE--------ENLWDIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgrQLIESIPSH--SF--EGKWWQRFKWRKKQAITLiHKVGI---KDHSRLMdsysyeLTDGQCQKVMIAMAI 173
Cdd:PRK13633 97 ----------QIVATIVEEdvAFgpENLGIPPEEIRERVDESL-KKVGMyeyRRHAPHL------LSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSV 238
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-236 |
1.31e-13 |
|
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: 69.11 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwKVSADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPSs 100
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKLPMHKRAR---LGIGYLPQEAS- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekVGRQL-----IESIpshsFEGKWWQRFKWRKKqAITLIHKVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIAA 175
Cdd:cd03218 86 -------IFRKLtveenILAV----LEIRGLSKKEREEK-LEELLEEFHI---THLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMNQLNnttI-VLIG----HDLTTITQwatRITVMYCGQ 236
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG---IgVLITdhnvRETLSITD---RAYIIYEGK 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-239 |
1.59e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETPQGLvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVG--VCKENWKVSADRMRLGNIDLLqltp 80
Cdd:PRK13645 8 ILDNVSYTYAKKTPFEF-KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliISETGQTIVGDYAIPANLKKI---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRvIARDIAMIFQEPSSCL--DPSEKVgrqlIESIPSHSFEGKwwqrfKWRKKQAITLIHKVGI-KDHSRlmdSYSY 157
Cdd:PRK13645 83 KEVKR-LRKEIGLVFQFPEYQLfqETIEKD----IAFGPVNLGENK-----QEAYKKVPELLKLVQLpEDYVK---RSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQS 237
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
..
gi 515624491 238 VE 239
Cdd:PRK13645 230 IS 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-247 |
1.67e-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: 69.11 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvcKENWKVSADRMRLGNIDLLQLTPKERRRviarDIAMIFQEP- 98
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL----ERFYDPTSGEILLDGVDIRDLNLRWLRS----QIGLVSQEPv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 ----------SSCLDPSEKVgrQLIESIpshsfegkwwqrfkwrkKQAitLIHKVGIKdhsrLMDSYSYE-------LTD 161
Cdd:cd03249 88 lfdgtiaeniRYGKPDATDE--EVEEAA-----------------KKA--NIHDFIMS----LPDGYDTLvgergsqLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMnQLNNTTIVlIGHDLTTItQWATRITVMYCGQSVESA 241
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIV-IAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
....*.
gi 515624491 242 DTQKLL 247
Cdd:cd03249 220 THDELM 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-243 |
1.78e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 9 LTIEIETPQ---GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRr 85
Cdd:PRK10851 1 MSIEIANIKksfGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRLHARDRK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 86 viardIAMIFQEPS---------------SCLDPSEKVGRQLIesipshsfegkwwqrfkwrKKQAITLIHKVGIkdhSR 150
Cdd:PRK10851 76 -----VGFVFQHYAlfrhmtvfdniafglTVLPRRERPNAAAI-------------------KAKVTQLLEMVQL---AH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK10851 129 LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
250
....*....|...
gi 515624491 231 VMYCGqSVESADT 243
Cdd:PRK10851 209 VMSQG-NIEQAGT 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-229 |
2.76e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckeNWKVSADRMRLGNiDLLQLTPK 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL---DTPTSGDVIFNGQ-PMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRVIARDIAMIFQEPSSCLDPSEkvgrqlIESIPSHSFEGKwwQRFKWRKKQAITLIHKVGIKDHSRLMDSysyELTD 161
Cdd:PRK11629 80 AKAELRNQKLGFIYQFHHLLPDFTA------LENVAMPLLIGK--KKPAEINSRALEMLAAVGLEHRANHRPS---ELSG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLttitQWATRI 229
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDL----QLAKRM 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-254 |
3.79e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIETpqglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckENWKVSADRMRLGNIDLLQLTPKER 83
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRviaRDIAMIFQEPsscldpsekvgrqlIEsipshsfegkwwqrfkwrkkqaitlIHKVGIKDHSRLMDsysYELTDGQ 163
Cdd:cd03217 75 AR---LGIFLAFQYP--------------PE-------------------------IPGVKNADFLRYVN---EGFSGGE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 164 CQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVlIGHD---LTTITqwATRITVMYCGQSVES 240
Cdd:cd03217 110 KKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLI-ITHYqrlLDYIK--PDRVHVLYDGRIVKS 186
|
250
....*....|....
gi 515624491 241 ADTQKLLDAPKHPY 254
Cdd:cd03217 187 GDKELALEIEKKGY 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-251 |
4.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.51 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNiDLLQLTPKERR-RVIARDIAMIFQEPSScldps 105
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP----TSGTVTIGE-RVITAGKKNKKlKPLRKKVGIVFQFPEH----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 106 ekvgrQLIESI--------PshsfegkwwQRF----KWRKKQAITLIHKVGIkDHSrLMDSYSYELTDGQCQKVMIAMAI 173
Cdd:PRK13634 97 -----QLFEETvekdicfgP---------MNFgvseEDAKQKAREMIELVGL-PEE-LLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES-------ADTQKL 246
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQgtpreifADPDEL 240
|
....*....
gi 515624491 247 ----LDAPK 251
Cdd:PRK13634 241 eaigLDLPE 249
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-236 |
4.76e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQltpKERRRVIARD-----IAMI 94
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGI------YTRDA---GSILYLG---KEVTFNGPKSsqeagIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 95 FQEPSscLDPsekvgrQLieSIPSHSFEGK----WWQRFKWRK--KQAITLIHKVGIKDHSRLMDSysyELTDGQCQKVM 168
Cdd:PRK10762 85 HQELN--LIP------QL--TIAENIFLGRefvnRFGRIDWKKmyAEADKLLARLNLRFSSDKLVG---ELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 169 IAMAIAAKPKILIADEPTndlDPITQSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPT---DALTDTETESLFRVIRELksQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-245 |
7.58e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADrmrlGNIDLlqlTPKERR-RVI----ARDIAMI 94
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHG---SYE----GEILF---DGEVCRfKDIrdseALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 95 FQEPSscLDPsekvgrQLieSIPSHSFEGKWWQRFK---WRK--KQAITLIHKVGIKDH--SRLMDsysyeLTDGQCQKV 167
Cdd:NF040905 84 HQELA--LIP------YL--SIAENIFLGNERAKRGvidWNEtnRRARELLAKVGLDESpdTLVTD-----IGVGKQQLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 168 MIAMAIAAKPKILIADEPT---NDLDpitqSQilRLLSRMNQLNN--TTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTaalNEED----SA--ALLDLLLELKAqgITSIIISHKLNEIRRVADSITVLRDGRTIETLD 222
|
...
gi 515624491 243 TQK 245
Cdd:NF040905 223 CRA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-232 |
1.36e-12 |
|
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: 65.98 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenWKVSAD-RMRLGNIDLLQLTPKERrrviarDIAMIFQEPS--SC 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAG-----FETPQSgRVLINGVDVTAAPPADR------PVSMLFQENNlfAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LDPSEKVGRQLIESIpshsfegkwwqRFKWRKKQAITLI-HKVGIKDhsrLMDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd03298 85 LTVEQNVGLGLSPGL-----------KLTAEDRQAIEVAlARVGLAG---LEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
157-240 |
1.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.02 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 157 YELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
....
gi 515624491 237 SVES 240
Cdd:PRK13639 215 IIKE 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-204 |
1.81e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPS- 99
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD----AGNIIIDDEDISLLPLHARAR---RGIGYLPQEASi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 ----SCLDPSEKVgRQLIESIPSHSfegkwwqrfkwRKKQAITLIHKVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIAA 175
Cdd:PRK10895 90 frrlSVYDNLMAV-LQIRDDLSAEQ-----------REDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180
....*....|....*....|....*....
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRM 204
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
22-235 |
2.05e-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: 65.50 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVC-KENWKVSAD-----RMRLGNIDLLQLTPKERRRVIARDiamif 95
Cdd:TIGR03740 15 AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILrPTSGEIIFDghpwtRKDLHKIGSLIESPPLYENLTARE----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 qepsscldpSEKVgRQLIESIPSHSFEgkwwqrfkwrkkqaiTLIHKVGIKDHSRlmdSYSYELTDGQCQKVMIAMAIAA 175
Cdd:TIGR03740 90 ---------NLKV-HTTLLGLPDSRID---------------EVLNIVDLTNTGK---KKAKQFSLGMKQRLGIAIALLN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 176 KPKILIADEPTNDLDPITqSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIG-IQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-242 |
2.36e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.80 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckeNWKVSADRMRLgNI-----DLLQLTPKERRRVIARDIA 92
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVL------NLLETPDSGQL-NIaghqfDFSQKPSEKAIRLLRQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 93 MIFQEPSscLDPSEKVGRQLIESiPShsfegkwwQRFKWRKKQAIT----LIHKVGIKDHSrlmDSYSYELTDGQCQKVM 168
Cdd:COG4161 86 MVFQQYN--LWPHLTVMENLIEA-PC--------KVLGLSKEQAREkamkLLARLRLTDKA---DRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 169 IAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrmNQLNNTTI--VLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEII---RELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-245 |
2.51e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKaIVGvCKEnwKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILG-CLD--KPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRVIARDIAMIFQEPS--SCLDPSEKVgrqlieSIPS-HSFEGKwwqrfKWRKKQAITLIHKVGIKDHsrlMDSYSYE 158
Cdd:PRK10535 79 ALAQLRREHFGFIFQRYHllSHLTAAQNV------EVPAvYAGLER-----KQRLLRAQELLQRLGLEDR---VEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVlIGHDlTTITQWATRITVMYCGQSV 238
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGEIV 222
|
....*..
gi 515624491 239 ESADTQK 245
Cdd:PRK10535 223 RNPPAQE 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-239 |
2.54e-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: 65.21 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 17 QGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLQLTPKE-RRRviardIAMIF 95
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDlRSR-----ISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEP-------SSCLDPSEKvgrqliesipsHSfEGKWWQrfkwrkkqaitLIHKVGIKDH-SRLMDSYSYELTD------ 161
Cdd:cd03244 85 QDPvlfsgtiRSNLDPFGE-----------YS-DEELWQ-----------ALERVGLKEFvESLPGGLDTVVEEggenls 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 162 -GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVE 239
Cdd:cd03244 142 vGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-238 |
3.94e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.64 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGN--IDLLQLTPKERRRviarDIAMIFQEPS 99
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP----SSGRILFDGkpIDYSRKGLMKLRE----SVGMVFQDPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 SCLDpSEKVGRQLIESIPSHSFEGKWWQRfkwRKKQAITlihKVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIAAKPKI 179
Cdd:PRK13636 93 NQLF-SASVYQDVSFGAVNLKLPEDEVRK---RVDNALK---RTGI---EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 180 LIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-200 |
5.56e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEIETpQGLVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAdRMRLGNIDLLQLtPKER 83
Cdd:COG4136 2 LSLENLTITLGG-RPLLAPLS---LTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASG-EVLLNGRRLTAL-PAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRviardIAMIFQEPssCLDPSEKVGRQLIESIPSHsfegkwWQRfKWRKKQAITLIHKVGIKDHSrlmDSYSYELTDGQ 163
Cdd:COG4136 76 RR-----IGILFQDD--LLFPHLSVGENLAFALPPT------IGR-AQRRARVEQALEEAGLAGFA---DRDPATLSGGQ 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 515624491 164 CQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRL 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 |
7.18e-12 |
|
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: 64.22 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRviaRDIAMIFQEPSs 100
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPD----AGKILIDGQDITHLPMHERAR---LGIGYLPQEAS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekVGRQL-----IESIPSHSFEGKWWQRfkwrKKQAITLIHKVGIkdhSRLMDSYSYELTDGQCQKVMIAMAIAA 175
Cdd:TIGR04406 87 -------IFRKLtveenIMAVLEIRKDLDRAER----EERLEALLEEFQI---SHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMNQLNnttI-VLI-GHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERG---IgVLItDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEK 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-236 |
1.26e-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: 63.26 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIvgvckEN-WKVSADRMRLGNIDLLQLTPKERRRVIArdiaMIFQEPSScldp 104
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALL-----ENfYQPQGGQVLLDGKPISQYEHKYLHSKVS----LVGQEPVL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 105 sekVGRQLIESIpSHSFEGKWWQRFK--WRKKQAITLIhkvgikdhSRLMDSYSYE-------LTDGQCQKVMIAMAIAA 175
Cdd:cd03248 100 ---FARSLQDNI-AYGLQSCSFECVKeaAQKAHAHSFI--------SELASGYDTEvgekgsqLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 176 KPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-219 |
1.32e-11 |
|
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: 65.07 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQglvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:TIGR02868 333 PTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL----LDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRVI---ARDiAMIFqepSSCLDPSEKVGRqliesiPSHSFEGKWWqrfkwrkkqaitLIHKVGIKDHSR-LMDSYSY 157
Cdd:TIGR02868 406 EVRRRVsvcAQD-AHLF---DTTVRENLRLAR------PDATDEELWA------------ALERVGLADWLRaLPDGLDT 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 158 ELTD-------GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDL 219
Cdd:TIGR02868 464 VLGEggarlsgGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-239 |
4.62e-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: 61.27 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 19 LVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCK-ENWKVSADRMRLGNIDLLQLtpkeRRRviardIAMIFQE 97
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL----RSS-----LTIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PS-------SCLDP-SEKVGRQLIESIpshsfegkwwqrfkwrkkqaitlihkvgikdhsRLMDSYSyELTDGQCQKVMI 169
Cdd:cd03369 91 PTlfsgtirSNLDPfDEYSDEEIYGAL---------------------------------RVSEGGL-NLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 170 AMAIAAKPKILIADEPTNDLDPITQSQILRLLSRmnQLNNTTIVLIGHDLTTITQWAtRITVMYCGQSVE 239
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKE 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-249 |
6.44e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRViarDIAMIFQEPss 100
Cdd:PRK15439 28 KGID---FTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD----SGTLEIGGNPCARLTPAKAHQL---GIYLVPQEP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 CLDPSEKVGRQLIESIPSHsfegkwwQRFKWRKKQaitLIHKVGIkdHSRL-MDSYSYELTDGQCQKVMIAMAIAAKpkI 179
Cdd:PRK15439 96 LLFPNLSVKENILFGLPKR-------QASMQKMKQ---LLAALGC--QLDLdSSAGSLEVADRQIVEILRGLMRDSR--I 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 180 LIADEPTNDLDPITQSqilRLLSRMNQLNNTT--IVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK15439 162 LILDEPTASLTPAETE---RLFSRIRELLAQGvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-231 |
8.69e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 19 LVKAVDRMSLTLNEGEIR-----GLVGESGSGKSLVAKAIVGVCKenwkvsADRmrlGNIDLlqltpkerrrviARDIAM 93
Cdd:COG1245 347 LTKSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLK------PDE---GEVDE------------DLKISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 94 IFQEPSSclDPSEKVgRQLIESIPSHSFEGKWWQrfkwrkkqaITLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAI 173
Cdd:COG1245 406 KPQYISP--DYDGTV-EEFLRSANTDDFGSSYYK---------TEIIKPLGLE---KLLDKNVKDLSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITV 231
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-219 |
1.06e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.25 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKenwkVSADRMRLGNIDLLqlTPKERRRVIARDIAMIfqePSSC 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP----YQHGSITLDGKPVE--GPGAERGVVFQNEGLL---PWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LDPSEKVGRQLiESIPSHSfegkwwqrfkwRKKQAITLIHKVGIKD-HSRlmdsYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:PRK11248 87 VQDNVAFGLQL-AGVEKMQ-----------RLEIAHQMLKKVGLEGaEKR----YIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDL 219
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
27-253 |
1.07e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 60.97 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAI----------VGVCKENWKVSADRmrlgnidLLQLTPKERRRV--IARDIAMI 94
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCInlletpdsgeIRVGGEEIRLKPDR-------DGELVPADRRQLqrIRTRLGMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 95 FQepSSCLDPSEKVGRQLIESiPSHSFegkwwqrfKWRKKQAIT----LIHKVGIKDhsrLMDSYSYELTDGQCQKVMIA 170
Cdd:COG4598 101 FQ--SFNLWSHMTVLENVIEA-PVHVL--------GRPKAEAIEraeaLLAKVGLAD---KRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 171 MAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQLNNT--TIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKV---MRDLAEEgrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
....*
gi 515624491 249 APKHP 253
Cdd:COG4598 244 NPKSE 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-260 |
1.12e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQLTPKErrrvIARDIAMIFQEPSSCLDPS 105
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP----AHGHVWLDGEHIQHYASKE----VARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 106 --EKVGRQLIESIPSHSfegkwwqrfKWRKKQAITLIHKVGIKDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIAD 183
Cdd:PRK10253 98 vqELVARGRYPHQPLFT---------RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 184 EPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESAdtqklldAPKHPYTVALLK 260
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIE 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-248 |
1.14e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLLQLTPKERRRVIARDIAMIFQEPSscL 102
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGM------TSPDA---GKITVLGVPVPARARLARARIGVVPQFDN--L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 DPSEKVGRQLIesipshsFEGKWWqRFKWRKKQAITlihkVGIKDHSRL---MDSYSYELTDGQCQKVMIAMAIAAKPKI 179
Cdd:PRK13536 126 DLEFTVRENLL-------VFGRYF-GMSTREIEAVI----PSLLEFARLeskADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 180 LIADEPTNDLDPITQSQI---LR-LLSRmnqlnNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIwerLRsLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-249 |
1.26e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkvsadRMRLGNIDLLQLTPKE--RRRVIArdiamiFQEPS 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV---------RLASGKISILGQPTRQalQKNLVA------YVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 SCLDPSEKVgrqLIESIPSHSFEGK--WWQRFKWRKKQAIT-LIHKVGIKDHSRLMDSysyELTDGQCQKVMIAMAIAAK 176
Cdd:PRK15056 87 EEVDWSFPV---LVEDVVMMGRYGHmgWLRRAKKRDRQIVTaALARVDMVEFRHRQIG---ELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 177 PKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIgHDLTTITQWATrITVMYCGQSVESADTQKLLDA 249
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVST-HNLGSVTEFCD-YTVMVKGTVLASGPTETTFTA 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-251 |
1.36e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRlgnIDLLQLTpkeRRRVIARDIAMIFQepSSCL 102
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP----TEGQIF---IDGEDVT---HRSIQQRDICMVFQ--SYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 DP----SEKVGRQL-IESIPShsfegkwwQRFKWRKKQAITLIHKVGIKDhsRLMDSYSyeltDGQCQKVMIAMAIAAKP 177
Cdd:PRK11432 90 FPhmslGENVGYGLkMLGVPK--------EERKQRVKEALELVDLAGFED--RYVDQIS----GGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624491 178 KILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDAPK 251
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-249 |
1.79e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLGNIDLLQLTPK 81
Cdd:PRK10762 247 PRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGA----LPRTSGYVTLDGHEVVTRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERrrvIARDIAMIfqepsscldpSEK-------VGRQLIE--SIPSHSFEGKWWQRFK-WRKKQAIT-LIHKVGIKDHSr 150
Cdd:PRK10762 323 DG---LANGIVYI----------SEDrkrdglvLGMSVKEnmSLTALRYFSRAGGSLKhADEQQAVSdFIRLFNIKTPS- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 lMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK10762 389 -MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRIL 466
|
250 260
....*....|....*....|....
gi 515624491 231 VMYCGQ-----SVESADTQKLLDA 249
Cdd:PRK10762 467 VMHEGRisgefTREQATQEKLMAA 490
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
162-215 |
2.17e-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: 59.10 E-value: 2.17e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLI 215
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSI 168
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-250 |
3.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTieiETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGNidllQLTp 80
Cdd:PRK13652 1 MHLIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT---SGSVLIRGE----PIT- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIFQEPS-SCLDPSEKvgrQLIESIPSHSfeGKWWQRFKWRKKQAItliHKVGIKDhsrLMDSYSYEL 159
Cdd:PRK13652 70 KENIREVRKFVGLVFQNPDdQIFSPTVE---QDIAFGPINL--GLDEETVAHRVSSAL---HMLGLEE---LRDRVPHHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 TDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250
....*....|.
gi 515624491 240 SADTQKLLDAP 250
Cdd:PRK13652 219 YGTVEEIFLQP 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-276 |
4.36e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADRmrlGNIDLL--QLTPKERRRviardIAMIFQE 97
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI------LAPDS---GEVLWDgePLDPEDRRR-----IGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PSscLDPSEKVGRQLI--------------ESIPshsfegKWWQRFK---WRKKqaitlihKVGikdhsrlmdsysyELT 160
Cdd:COG4152 80 RG--LYPKMKVGEQLVylarlkglskaeakRRAD------EWLERLGlgdRANK-------KVE-------------ELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 515624491 241 ADTQKLLDA-PKHPYTV------ALLKAMPDFNDWIPHKEKLQ 276
Cdd:COG4152 211 GSVDEIRRQfGRNTLRLeadgdaGWLRALPGVTVVEEDGDGAE 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-245 |
4.83e-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: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTI-EIETPQglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSAdrmrlgNIDLLQLTPK 81
Cdd:TIGR02633 257 ILEARNLTCwDVINPH--RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNV------FINGKPVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 82 ERRRVIARDIAMIFQE-PSSCLDPSEKVGRQL-IESIPSHSFEGkwwqRFKWRKKQAITL--IHKVGIKDHSRLMDSYSy 157
Cdd:TIGR02633 329 NPAQAIRAGIAMVPEDrKRHGIVPILGVGKNItLSVLKSFCFKM----RIDAAAELQIIGsaIQRLKVKTASPFLPIGR- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 158 eLTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQL--NNTTIVLIGHDLTTITQWATRITVMY-- 233
Cdd:TIGR02633 404 -LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKL---INQLaqEGVAIIVVSSELAEVLGLSDRVLVIGeg 479
|
250
....*....|....
gi 515624491 234 --CGQSVESADTQK 245
Cdd:TIGR02633 480 klKGDFVNHALTQE 493
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-248 |
6.18e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 25 RMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkVSADR--MRLGNIDLlQLTPKERRRViardiAMIFQEP---- 98
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGF------LTPASgsLTLNGQDH-TTTPPSRRPV-----SMLFQENnlfs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 --------SSCLDPSEKVGRQliesipshsfegkwwQRfkwRKKQAITliHKVGIKDH-SRLmdsySYELTDGQCQKVMI 169
Cdd:PRK10771 85 hltvaqniGLGLNPGLKLNAA---------------QR---EKLHAIA--RQMGIEDLlARL----PGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 170 AMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-255 |
6.32e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.03 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKA------IVGVCKENWKVSadrMRLGNIDLLQLTPKERRRviarDIAMIF 95
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVEGKVT---FHGKNLYAPDVDPVEVRR----RIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 QEPssclDPSEKVGRQLIESIPS-HSFEGKWWQRFKWRKKQAItLIHKVgiKDhsRLMDSySYELTDGQCQKVMIAMAIA 174
Cdd:PRK14243 98 QKP----NPFPKSIYDNIAYGARiNGYKGDMDELVERSLRQAA-LWDEV--KD--KLKQS-GLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 175 AKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLttitQWATRITVMYC-------------GQSVESA 241
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNM----QQAARVSDMTAffnveltegggryGYLVEFD 241
|
250
....*....|....
gi 515624491 242 DTQKLLDAPKHPYT 255
Cdd:PRK14243 242 RTEKIFNSPQQQAT 255
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-217 |
6.78e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLTIEieTPQG--LVKAVdrmSLTLNEGEiRGLV-GESGSGKSLVAKAIVGVckenWKVSAdrmrlGNIDLlqltP 80
Cdd:COG4178 363 LALEDLTLR--TPDGrpLLEDL---SLSLKPGE-RLLItGPSGSGKSTLLRAIAGL----WPYGS-----GRIAR----P 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRrviardiaMIF--QEP---SSCLdpsekvgRQLI---ESIPSHSFEgkwwqrfkwrkkQAITLIHKVGIKDHSRLM 152
Cdd:COG4178 424 AGAR--------VLFlpQRPylpLGTL-------REALlypATAEAFSDA------------ELREALEAVGLGHLAERL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 153 D---SYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRmnQLNNTTIVLIGH 217
Cdd:COG4178 477 DeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-231 |
7.47e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 19 LVKAVDRMSLTLNEGEIR-----GLVGESGSGKSLVAKAIVGVckenwkvsadrmrlgnidllqLTPKERRRVIARDIAM 93
Cdd:PRK13409 346 LTKKLGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGV---------------------LKPDEGEVDPELKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 94 IFQEPSSclDPSEKVgRQLIESIPShSFEGKWWQrfkwrkkqaITLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAI 173
Cdd:PRK13409 405 KPQYIKP--DYDGTV-EDLLRSITD-DLGSSYYK---------SEIIKPLQLE---RLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITV 231
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-246 |
1.40e-09 |
|
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: 59.07 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIetpqGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWKvsadrmrlGNI--DLLQLT 79
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgTWD--------GEIywSGSPLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 80 PKERRRVIARDIAMIFQEPSscLDPSEKVGRQLIESIPSHSFEGKWWQRFKWRKKQAITLIHKVGIKDHSRLMDSYSYel 159
Cdd:TIGR02633 69 ASNIRDTERAGIVIIHQELT--LVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGG-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 160 tdGQCQKVMIAMAIAAKPKILIADEPTNDLDPiTQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVE 239
Cdd:TIGR02633 145 --GQQQLVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
....*..
gi 515624491 240 SADTQKL 246
Cdd:TIGR02633 222 TKDMSTM 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-252 |
2.01e-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: 59.15 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLtpKERRRVIARDIAMIFQEPSSCLDPS 105
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTW--RKAFGVIPQKVFIFSGTFRKNLDPY 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 106 EKVGRQLIesipshsfegkwwqrfkWRKKQAITL---IHKVGIKDHSRLMDSySYELTDGQCQKVMIAMAIAAKPKILIA 182
Cdd:TIGR01271 1316 EQWSDEEI-----------------WKVAEEVGLksvIEQFPDKLDFVLVDG-GYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 183 DEPTNDLDPITQSQILRLLSRmnQLNNTTIVLIGHDLTTITQWATRITVMycGQSVESADT-QKLLDAPKH 252
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIE--GSSVKQYDSiQKLLNETSL 1444
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-242 |
2.66e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEN-----WKVSA-DRMRLGNIDLLQltpkerrrviarDIAMIFQeps 99
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkgavlWQGKPlDYSKRGLLALRQ------------QVATVFQ--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 sclDPSEKVGRQLIESIPSHSFE--GKWWQRFKWRKKQAITLIhkvgikDHSRLMDSYSYELTDGQCQKVMIAMAIAAKP 177
Cdd:PRK13638 85 ---DPEQQIFYTDIDSDIAFSLRnlGVPEAEITRRVDEALTLV------DAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 178 KILIADEPTNDLDPITQSQILRLLSRMNQLNNtTIVLIGHDLTTITQWATRITVMYCGQSVESAD 242
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
145-229 |
2.89e-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: 54.76 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 145 IKDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnntTIVLIGHDLTTITQ 224
Cdd:cd03221 57 VTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQ 132
|
....*
gi 515624491 225 WATRI 229
Cdd:cd03221 133 VATKI 137
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-232 |
2.91e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 21 KAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsaDRMRLGNIDL--LQLTPKERRRVIARDIAMIFQE- 97
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---------DKRAGGEIRLngKDISPRSPLDAVKKGMAYITESr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 ------PSSCLDPSEKVGRQLIESipshSFEGKWwQRFKWRKKQAITLIHK--VGIKDHSrlMDSYSYELTDGQCQKVMI 169
Cdd:PRK09700 348 rdngffPNFSIAQNMAISRSLKDG----GYKGAM-GLFHEVDEQRTAENQRelLALKCHS--VNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 170 AMAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQLNNT--TIVLIGHDLTTITQWATRITVM 232
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKV---MRQLADDgkVILMVSSELPEIITVCDRIAVF 482
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-235 |
7.45e-09 |
|
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: 55.35 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRMRLGNI--DLLQLTPKERRRVIArdiamiFQEPSSCLDP 104
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISG------RVEGGGTTSGQIlfNGQPRKPDQFQKCVA------YVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 105 SEKVGRQL----IESIPSHSFEGkwwQRfkwRKKQAITLIHKVGikdHSRLMDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd03234 95 GLTVRETLtytaILRLPRKSSDA---IR---KKRVEDVLLRDLA---LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVM------YCG 235
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLssgeivYSG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
33-236 |
7.70e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.45 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 33 GEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDLLQltpkerrrviAR-DIAMIFQEPSscLDPSEKVgrq 111
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETP----SAGELLAGTAPLAE----------AReDTRLMFQDAR--LLPWKKV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 112 lIESIpSHSFEGKWwqrfkwrKKQAITLIHKVGIKDHSrlmDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDP 191
Cdd:PRK11247 99 -IDNV-GLGLKGQW-------RDAALQALAAVGLADRA---NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515624491 192 ITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-257 |
1.12e-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: 56.49 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 26 MSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKE-NWKVSADRMRLGNIDLLQLTPKerrrviardIAMIFQEP---SSC 101
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFK---------ITIIPQDPvlfSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LdpsekvgRQLIESIPSHSFEGKWWqrfkwrkkqAITLIHkvgIKDH-SRLMDSYSYE-------LTDGQCQKVMIAMAI 173
Cdd:TIGR00957 1376 L-------RMNLDPFSQYSDEEVWW---------ALELAH---LKTFvSALPDKLDHEcaeggenLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 174 AAKPKILIADEPTNDLDPITQSQILRLLSrmNQLNNTTIVLIGHDLTTITQWaTRITVMYCGQSVESADTQKLLDAPKHP 253
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
....
gi 515624491 254 YTVA 257
Cdd:TIGR00957 1514 YSMA 1517
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-290 |
1.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVG---------VCKEN--WKVS--------ADRMRLGNIDLLQLTPKERRRVI 87
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerQSQFShiTRLSfeqlqklvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 88 ARDIAMIFQEPSSCLDPSEKVGrqlIESIPShsfegkwwQRFKWrkkqaitlihkvgikdhsrlmdsysyeLTDGQCQKV 167
Cdd:PRK10938 103 AEIIQDEVKDPARCEQLAQQFG---ITALLD--------RRFKY---------------------------LSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLL 247
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515624491 248 -DApkhpyTVALLKampdfndwipHKEKLQ--SLPGSIPPLQHLPI 290
Cdd:PRK10938 224 qQA-----LVAQLA----------HSEQLEgvQLPEPDEPSARHAL 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-235 |
1.54e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 28 LTLNEGEIRGLVGESGSGKSLVAKAIVGVckENwkVSADRMRLGNIDLLQLTPKERrrviarDIAMIFQepSSCLDPSEK 107
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGL--ED--ITSGDLFIGEKRMNDVPPAER------GVGMVFQ--SYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 108 VGRQLiesipshSFEGKWWQRFKWRKKQAITLIHKVGIKDHsrLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTN 187
Cdd:PRK11000 92 VAENM-------SFGLKLAGAKKEEINQRVNQVAEVLQLAH--LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515624491 188 DLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCG 235
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-232 |
1.67e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.70 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKS----LVAKAIvgvckenwKVSADRMRLGNIDLLQlTPKerrRVIARDIAMIFQEP 98
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKStllsMISRLL--------PPDSGEVLVDGLDVAT-TPS---RELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 99 SscLDPSEKVgRQLIesipshSFeGkwwqRFKWRK-----------KQAITLIHKVGIKDhsRLMDsysyELTDGQCQKV 167
Cdd:COG4604 85 H--INSRLTV-RELV------AF-G----RFPYSKgrltaedreiiDEAIAYLDLEDLAD--RYLD----ELSGGQRQRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRM-NQLNNTTIVLIgHDLTTITQWATRITVM 232
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVL-HDINFASCYADHIVAM 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-246 |
1.73e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvSADRMRLGNidllQLTPKERRRVIARDIAMIFQEPS 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGK----EIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 SCLDpsekvgRQLIESIpshsfegkWWQRFKwrkKQAITLIHKVGIKDHSRLMDSYSYE---------LTDGQCQKVMIA 170
Cdd:PRK10982 84 LVLQ------RSVMDNM--------WLGRYP---TKGMFVDQDKMYRDTKAIFDELDIDidprakvatLSVSQMQMIEIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 171 MAIAAKPKILIADEPTNDLdpiTQSQILRLLSRMNQLNNT--TIVLIGHDLTTITQWATRITVMYCGQSVESADTQKL 246
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-247 |
2.60e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.22 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 16 PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVgvckENWKVSADRMRLGNIDLLQLtpkerrrviardiamif 95
Cdd:PRK11160 349 PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT----RAWDPQQGEILLNGQPIADY----------------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 96 qepsscldpSEKVGRQLIESIPS--HSFEGKWWQRFKWRKKQA-----ITLIHKVG----IKDHSRLmDSYSYE----LT 160
Cdd:PRK11160 408 ---------SEAALRQAISVVSQrvHLFSATLRDNLLLAAPNAsdealIEVLQQVGleklLEDDKGL-NAWLGEggrqLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 161 DGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQWaTRITVMYCGQSVES 240
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
....*..
gi 515624491 241 ADTQKLL 247
Cdd:PRK11160 555 GTHQELL 561
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-219 |
3.06e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.00 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEietpQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRmrlGNI--DLLQLTP 80
Cdd:PRK11831 7 LVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG------QIAPDH---GEIlfDGENIPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIA--RDIAMIFQEPSSCLDPS--EKVGRQLIE--SIPS---HSfegkwwqrfkwrkkqaiTLIHK---VGIKDH 148
Cdd:PRK11831 74 MSRSRLYTvrKRMSMLFQSGALFTDMNvfDNVAYPLREhtQLPApllHS-----------------TVMMKleaVGLRGA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 149 SRLMDSysyELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDL 219
Cdd:PRK11831 137 AKLMPS---ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-232 |
3.51e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIetpQGLVkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenWKVSADRMRLG---------- 71
Cdd:PRK11300 4 PLLSVSGLMMRF---GGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF----YKPTGGTILLRgqhieglpgh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 72 ------------NIDLL-QLTPKE------RRRVIARDIAMIFQEPSSCLDPSEKVGRqliesipshsfegkwwqrfkwr 132
Cdd:PRK11300 76 qiarmgvvrtfqHVRLFrEMTVIEnllvaqHQQLKTGLFSGLLKTPAFRRAESEALDR---------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 133 kkqAITLIHKVGIKDHS-RLMDSYSYeltdGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTT 211
Cdd:PRK11300 134 ---AATWLERVGLLEHAnRQAGNLAY----GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVT 206
|
250 260
....*....|....*....|.
gi 515624491 212 IVLIGHDLTTITQWATRITVM 232
Cdd:PRK11300 207 VLLIEHDMKLVMGISDRIYVV 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-257 |
4.54e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwkvsADRMRLGNIDL--LQLTPKERRRVIARDIAMifqepssCLDP 104
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYG---------ATRRTAGQVYLdgKPIDIRSPRDAIRAGIML-------CPED 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 105 SEKVGrqlIesIPSHSFE-------------GKWWQRFKWRKKQAITLIHKVGIKDHSRlmDSYSYELTDGQCQKVMIAM 171
Cdd:PRK11288 337 RKAEG---I--IPVHSVAdninisarrhhlrAGCLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 172 AIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQSV-----ESADTQKL 246
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQA 488
|
250
....*....|...
gi 515624491 247 LDA--PKHPYTVA 257
Cdd:PRK11288 489 LSLalPRTSAAVA 501
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-232 |
5.92e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTIEIETPQglvkAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckENwkVSADRMRLGNIDLLQLtP 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ET--PDSGRIMLDGQDITHV-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRrviarDIAMIFQepSSCLDPS-------------EKVGRQLIESipshsfegkwwqrfkwRKKQAITLIHKVGIKD 147
Cdd:PRK09452 83 AENR-----HVNTVFQ--SYALFPHmtvfenvafglrmQKTPAAEITP----------------RVMEALRMVQLEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 148 HSrlmdsySYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQI---LRLLSRmnQLnNTTIVLIGHDLTTITQ 224
Cdd:PRK09452 140 RK------PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQR--KL-GITFVFVTHDQEEALT 210
|
....*...
gi 515624491 225 WATRITVM 232
Cdd:PRK09452 211 MSDRIVVM 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-250 |
7.91e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTItQWATRIT 230
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIF 650
|
90 100
....*....|....*....|
gi 515624491 231 VMYCGQSVESADTQKLLDAP 250
Cdd:PTZ00265 651 VLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-231 |
8.70e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.41 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 29 TLNEGEIRGLVGESGSGKSLVAKAIVGVCK--------ENWKVSADRMrlgnidllQLTPKERRRViardiamifqepss 100
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpdegdieiELDTVSYKPQ--------YIKADYEGTV-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 101 cldpsekvgRQLIESIPSHSFEGKWWQrfkwrkkqaITLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAIAAKPKIL 180
Cdd:cd03237 79 ---------RDLLSSITKDFYTHPYFK---------TEIAKPLQIE---QILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515624491 181 IADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITV 231
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-280 |
1.11e-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: 52.16 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADRMRLGNIDLLQLtpKERRRVIARDIaMIFQEP-SSC 101
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKW--RKAFGVIPQKV-FIFSGTfRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 LDPSekvgrqliesipshsfeGKWWQRFKWRKKQAI---TLIHKVGIKDHSRLMDSySYELTDGQCQKVMIAMAIAAKPK 178
Cdd:cd03289 97 LDPY-----------------GKWSDEEIWKVAEEVglkSVIEQFPGQLDFVLVDG-GCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 179 ILIADEPTNDLDPITqSQILRLLSRmNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLLDAPKHpytval 258
Cdd:cd03289 159 ILLLDEPSAHLDPIT-YQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSH------ 229
|
250 260
....*....|....*....|..
gi 515624491 259 lkampdFNDWIPHKEKLQSLPG 280
Cdd:cd03289 230 ------FKQAISPSDRLKLFPR 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-247 |
1.16e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 18 GLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwKVSADRMRLGNIDLLQLTPKERRRViardIAMIFQE 97
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 98 PsscLDPSEKVgRQLIESIPSHSFEGKWwqrfkwrkkQAITLIH-KVGIKDHSRLMDSYSYE----LTDGQCQKVMIAMA 172
Cdd:PLN03232 1319 P---VLFSGTV-RFNIDPFSEHNDADLW---------EALERAHiKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARA 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 173 IAAKPKILIADEPTNDLDPITQSQILRLLSRmnQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVESADTQKLL 247
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-250 |
1.18e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 9 LTIEIET---PQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIvgvcKENWKVSADRMRLGNIDLLQLTPKERRr 85
Cdd:PRK10789 314 LDVNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI----QRHFDVSEGDIRFHDIPLTKLQLDSWR- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 86 viARdIAMIFQEPsscLDPSEKVGRQLIESIPSHSFEgkwwqrfkwRKKQAITL--IHKvgikDHSRLMDSYSYE----- 158
Cdd:PRK10789 389 --SR-LAVVSQTP---FLFSDTVANNIALGRPDATQQ---------EIEHVARLasVHD----DILRLPQGYDTEvgerg 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 --LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlnNTTIVLIGHDLTTITQwATRITVMYCGQ 236
Cdd:PRK10789 450 vmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGH 526
|
250
....*....|....
gi 515624491 237 SVESADTQKLLDAP 250
Cdd:PRK10789 527 IAQRGNHDQLAQQS 540
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-98 |
1.21e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 2 PLLDIRHLTIEIETPQgLVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGvcKENWKVSADRMRLGNIDLLQLTPK 81
Cdd:CHL00131 6 PILEIKNLHASVNENE-ILKGLN---LSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEGDILFKGESILDLEPE 79
|
90
....*....|....*..
gi 515624491 82 ERRRviaRDIAMIFQEP 98
Cdd:CHL00131 80 ERAH---LGIFLAFQYP 93
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-229 |
2.93e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 24 DRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwKVSADRMRLgNID-------LLQLTPKERRRVIARDIAMIFQ 96
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNG------EVLLDDGRI-IYEqdlivarLQQDPPRNVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 97 EPSSCL------------DPSEKVGRQL--IESIPSHsfEGKWwqRFKWRKKQAITLIhkvGIKDHSRLMdsysyELTDG 162
Cdd:PRK11147 93 EQAEYLkryhdishlvetDPSEKNLNELakLQEQLDH--HNLW--QLENRINEVLAQL---GLDPDAALS-----SLSGG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 163 QCQKVMIAMAIAAKPKILIADEPTNDLDpITQSQILR--LLSRmnqlnNTTIVLIGHDLTTITQWATRI 229
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLD-IETIEWLEgfLKTF-----QGSIIFISHDRSFIRNMATRI 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-98 |
4.64e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 3 LLDIRHLTIEIETpQGLVKAVDrmsLTLNEGEIRGLVGESGSGKSLVAKAIVGvcKENWKVSADRMRLGNIDLLQLTPKE 82
Cdd:PRK09580 1 MLSIKDLHVSVED-KAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90
....*....|....*.
gi 515624491 83 RrrvIARDIAMIFQEP 98
Cdd:PRK09580 75 R---AGEGIFMAFQYP 87
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-238 |
5.49e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRhltiEIETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckenwkvsADRMRLGNI--DLLQL 78
Cdd:PRK11614 3 KVMLSFD----KVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG---------DPRATSGRIvfDGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 79 TPKERRRVIARDIAMIFQepsscldpsekvGRQLI------ESIPSHSFEGKWwQRFKWRKKQAITLIHKVGIKDHSRlm 152
Cdd:PRK11614 70 TDWQTAKIMREAVAIVPE------------GRRVFsrmtveENLAMGGFFAER-DQFQERIKWVYELFPRLHERRIQR-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 153 dsySYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVM 232
Cdd:PRK11614 135 ---AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVL 210
|
....*.
gi 515624491 233 YCGQSV 238
Cdd:PRK11614 211 ENGHVV 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-243 |
6.25e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGvckeNWKVSADRMRlgnIDLLQLTPKERRRVIARDIAMIFQEPS 99
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG----NYQPDAGSIL---IDGQEMRFASTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 scLDPSEKVGRQLiesipshsFEGKWWQRFKWRKKQaiTLIHKVG---------IKDHSRLMdsysyELTDGQCQKVMIA 170
Cdd:PRK11288 90 --LVPEMTVAENL--------YLGQLPHKGGIVNRR--LLNYEAReqlehlgvdIDPDTPLK-----YLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 171 MAIAAKPKILIADEPTNDLdpiTQSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQSVESADT 243
Cdd:PRK11288 153 KALARNARVIAFDEPTSSL---SAREIEQLFRVIRELraEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
27-218 |
9.26e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.06 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVG---------VCKENWKVS--------------ADRMRLGNIDLLQLtpKER 83
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGelepdsgevSIPKGLRIGylpqeppldddltvLDTVLDGDAELRAL--EAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 84 RRVIARDIAMIFQEPsscldpsEKVGR--QLIESIPSHSFEGKwwqrfkwrkkqAITLIHKVGIK--DHSRLMDSYSyel 159
Cdd:COG0488 96 LEELEAKLAEPDEDL-------ERLAElqEEFEALGGWEAEAR-----------AEEILSGLGFPeeDLDRPVSELS--- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 160 tDGQCQKVMIAMAIAAKPKILIADEPTNDLDpiTQSqILRLLSRMNQLNNtTIVLIGHD 218
Cdd:COG0488 155 -GGWRRRVALARALLSEPDLLLLDEPTNHLD--LES-IEWLEEFLKNYPG-TVLVVSHD 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-236 |
1.04e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 4 LDIRHLT-IEIETPQglVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKvsadrmrlGNI--DLLQLTP 80
Cdd:PRK13549 260 LEVRNLTaWDPVNPH--IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWE--------GEIfiDGKPVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KERRRVIARDIAMIfqepsscldpSEKVGRQLIesIPSHSFegkwwqrfkwrkKQAITL-----IHKVGIKDHSRLMDSY 155
Cdd:PRK13549 330 RNPQQAIAQGIAMV----------PEDRKRDGI--VPVMGV------------GKNITLaaldrFTGGSRIDDAAELKTI 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 156 SYE-----------------LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLlsrMNQL--NNTTIVLIG 216
Cdd:PRK13549 386 LESiqrlkvktaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKL---INQLvqQGVAIIVIS 462
|
250 260
....*....|....*....|
gi 515624491 217 HDLTTITQWATRITVMYCGQ 236
Cdd:PRK13549 463 SELPEVLGLSDRVLVMHEGK 482
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
10-238 |
1.28e-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: 48.41 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 10 TIEIETPQGLVKA--VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENWKVSADrMRLGNIDllqltPKERRRVI 87
Cdd:cd03233 8 NISFTTGKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIP-----YKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 88 ARDIAMIFQEPSSclDPSEKVgRQLIEsipshsfegkwwqrFKWRKKQaitlihkvgikdhsrlmDSYSYELTDGQCQKV 167
Cdd:cd03233 82 PGEIIYVSEEDVH--FPTLTV-RETLD--------------FALRCKG-----------------NEFVRGISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 168 MIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRM-NQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMaDVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-247 |
3.45e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.48 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 10 TIEIETPQGLVK--------------AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVgvckENWKVSADRMRLGNIDL 75
Cdd:PRK11176 332 KRVIERAKGDIEfrnvtftypgkevpALRNINFKIPAGKTVALVGRSGSGKSTIANLLT----RFYDIDEGEILLDGHDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 76 LQLTPKERRR--------------VIARDIAMIFQEPSScldpsekvgRQLIESIP--SHSFEgkwwqrFKWRKKQAI-T 138
Cdd:PRK11176 408 RDYTLASLRNqvalvsqnvhlfndTIANNIAYARTEQYS---------REQIEEAArmAYAMD------FINKMDNGLdT 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 139 LIHKVGIKdhsrlmdsysyeLTDGQCQKVMIAMAIAAKPKILIADEPTNDLDpiTQSQILrLLSRMNQLN-NTTIVLIGH 217
Cdd:PRK11176 473 VIGENGVL------------LSGGQRQRIAIARALLRDSPILILDEATSALD--TESERA-IQAALDELQkNRTSLVIAH 537
|
250 260 270
....*....|....*....|....*....|
gi 515624491 218 DLTTITQwATRITVMYCGQSVESADTQKLL 247
Cdd:PRK11176 538 RLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-222 |
5.17e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 5.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 155 YSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTI 222
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-233 |
7.56e-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: 46.59 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 32 EGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIARDIAMIFQE-----PSSCLDPSE 106
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPN---------LGKFD----DPPDWDEILDEFRGSELQNyftklLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 107 KVgrQLIESIPShSFEGKWWQRFKWRKKQAI--TLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADE 184
Cdd:cd03236 92 KP--QYVDLIPK-AVKGKVGELLKKKDERGKldELVDQLELR---HVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515624491 185 PTNDLDPITQSQILRLLSRMNQLNNTTIVlIGHDLTTITQWATRITVMY 233
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCLY 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-234 |
8.24e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.70 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 11 IEIETPQGLvKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKEnwkvSADRMRLGNIDllqltpkerrrvIARD 90
Cdd:TIGR01257 935 VKIFEPSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKD------------IETN 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 91 IAMIFQEPSSCldPSEKVGRQLIeSIPSHSFegkWWQRFKWRKKQAITLIHKVGIKD----HSRlmDSYSYELTDGQCQK 166
Cdd:TIGR01257 998 LDAVRQSLGMC--PQHNILFHHL-TVAEHIL---FYAQLKGRSWEEAQLEMEAMLEDtglhHKR--NEEAQDLSGGMQRK 1069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624491 167 VMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDLTTITQWATRITV-----MYC 234
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIisqgrLYC 1140
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-250 |
9.07e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 27 SLTLNEGEIRGLVGESGSGKSLVAKAIVGVCkenwkVSADRMRLGNIDLLQLTPKE---RRRVIARD----IAM-IFQ-- 96
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-----PGSGSIQFAGQPLEAWSAAElarHRAYLSQQqtppFAMpVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 97 ---EPSSC-LDPSEKVGRQLIESI--------PSHSFEGKWWQRFkwRKKQAITLIHKVgIKDHSRLmdsysyeltdgqc 164
Cdd:PRK03695 91 tlhQPDKTrTEAVASALNEVAEALglddklgrSVNQLSGGEWQRV--RLAAVVLQVWPD-INPAGQL------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 165 qkvmiamaiaakpkiLIADEPTNDLDpITQSQIL-RLLSRMNQLnNTTIVLIGHDLTTITQWATRITVMYCGQSVESADT 243
Cdd:PRK03695 155 ---------------LLLDEPMNSLD-VAQQAALdRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
....*..
gi 515624491 244 QKLLDAP 250
Cdd:PRK03695 218 DEVLTPE 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-236 |
9.17e-06 |
|
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: 45.99 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 20 VKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckenwkvsadrmrlgnidllqLTPKERRRVIARDIAMIFqEPS 99
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI---------------------YPPDSGTVTVRGRVSSLL-GLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 100 SCLDPsEKVGRQLIEsipshsFEGKWWqrfKWRKKQAITLIHKvgIKDHSRLMDSYSY---ELTDGQCQKVMIAMAIAAK 176
Cdd:cd03220 93 GGFNP-ELTGRENIY------LNGRLL---GLSRKEIDEKIDE--IIEFSELGDFIDLpvkTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 177 PKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQ 236
Cdd:cd03220 161 PDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
159-222 |
5.10e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 5.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 159 LTDGQCQKVMIA--MAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNtTIVLIGHDLTTI 222
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVL 152
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-236 |
5.39e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 1 MPLLDIRHLTieiETPQGLVKAVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVckEnwKVSADRMRLGNIDLLQLTP 80
Cdd:PRK11650 1 MAGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--E--RITSGEIWIGGRVVNELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 81 KErrrviaRDIAMIFQepSSCLDP-------------SEKVGRQLIEsipshsfegkwwQRFkwrKKQAITLihkvGIKD 147
Cdd:PRK11650 74 AD------RDIAMVFQ--NYALYPhmsvrenmayglkIRGMPKAEIE------------ERV---AEAARIL----ELEP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 148 hsrLMDSYSYELTDGQCQKVmiAM--AIAAKPKILIADEPTNDLDPITQSQ----ILRLLSRMnqlnNTTIVLIGHDLTT 221
Cdd:PRK11650 127 ---LLDRKPRELSGGQRQRV--AMgrAIVREPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRL----KTTSLYVTHDQVE 197
|
250
....*....|....*
gi 515624491 222 ITQWATRITVMYCGQ 236
Cdd:PRK11650 198 AMTLADRVVVMNGGV 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-233 |
6.77e-05 |
|
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: 44.39 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 32 EGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIAR----DIAMIFQEPSSC-LDPSE 106
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPN---------LGDYD----EEPSWDEVLKRfrgtELQDYFKKLANGeIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 107 KVgrQLIESIPShSFEGKWWQ-------RFKWRKkqaitLIHKVGIKDhsrLMDSYSYELTDGQCQKVMIAMAIAAKPKI 179
Cdd:COG1245 165 KP--QYVDLIPK-VFKGTVREllekvdeRGKLDE-----LAEKLGLEN---ILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515624491 180 LIADEPTNDLDpITQ----SQILRLLSRMnqlnNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:COG1245 234 YFFDEPSSYLD-IYQrlnvARLIRELAEE----GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
159-248 |
8.43e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMYCGQSV 238
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
90
....*....|
gi 515624491 239 ESADTQKLLD 248
Cdd:TIGR00955 247 YLGSPDQAVP 256
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-249 |
1.11e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 43.26 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 23 VDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsADRMRLGNIDLLQLTPKERRRViarDIAMIFQEpsscL 102
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD----AGSISLCGEPVPSRARHARQRV---GVVPQFDN----L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 103 DPSEKVGRQLIesipshsFEGKWwqrFKWRKKQAITLIHkvGIKDHSRL---MDSYSYELTDGQCQKVMIAMAIAAKPKI 179
Cdd:PRK13537 92 DPDFTVRENLL-------VFGRY---FGLSAAAARALVP--PLLEFAKLenkADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624491 180 LIADEPTNDLDPITQSQI---LR-LLSRmnqlnNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLDA 249
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMwerLRsLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
166-218 |
1.40e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515624491 166 KVMIAMAIAAKPKILIADEPTNDLDPITqsqiLRLLSrmNQLN--NTTIVLIGHD 218
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINT----IRWLE--DVLNerNSTMIIISHD 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
151-236 |
1.94e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.55 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRIT 230
Cdd:PRK11144 121 LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVV 200
|
....*.
gi 515624491 231 VMYCGQ 236
Cdd:PRK11144 201 VLEQGK 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
158-233 |
2.56e-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: 41.02 E-value: 2.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-248 |
3.26e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 22 AVDRMSLTLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDLlqltpKERRRVIArdiamifqepssc 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN---------KGTVDI-----KGSAALIA------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 102 ldPSEKVGRQL--IESIPSHSFegkwwqRFKWRKKQAITLIHKV-GIKDHSRLMDSYSYELTDGQCQKVMIAMAIAAKPK 178
Cdd:PRK13545 92 --ISSGLNGQLtgIENIELKGL------MMGLTKEKIKEIIPEIiEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515624491 179 ILIADEPTNDLDpitQSQILRLLSRMNQL--NNTTIVLIGHDLTTITQWATRITVMYCGQSVESADTQKLLD 248
Cdd:PRK13545 164 ILVIDEALSVGD---QTFTKKCLDKMNEFkeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
151-219 |
6.30e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.87 E-value: 6.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGHDL 219
Cdd:PRK09544 113 LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
151-222 |
7.58e-04 |
|
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: 39.28 E-value: 7.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515624491 151 LMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQIL-----RLLSRMNQLNNTTIVLIGHDLTTI 222
Cdd:smart00382 53 IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNLTVILTTNDEKDL 129
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
159-248 |
1.52e-03 |
|
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: 40.31 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQIL-RLLSRMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQS 237
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 839
|
90
....*....|.
gi 515624491 238 VESADTQKLLD 248
Cdd:TIGR00957 840 SEMGSYQELLQ 850
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
167-218 |
1.67e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 40.05 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515624491 167 VMIAMAIAAKPKILIADEPTNDLDPITqsqiLRLLsrMNQLNNT--TIVLIGHD 218
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIET----LEAL--EEALDDFpgTVLLVSHD 488
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-233 |
2.34e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 29 TLNEGEIRGLVGESGSGKSLVAKAIVGVCKENwkvsadrmrLGNIDllqlTPKERRRVIAR----DIAMIFQEPSSC-LD 103
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN---------LGDYE----EEPSWDEVLKRfrgtELQNYFKKLYNGeIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 104 PSEKVgrQLIESIPShSFEGKWWQ-------RFKWRKkqaitLIHKVGIKdhsRLMDSYSYELTDGQCQKVMIAMAIAAK 176
Cdd:PRK13409 162 VVHKP--QYVDLIPK-VFKGKVREllkkvdeRGKLDE-----VVERLGLE---NILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624491 177 PKILIADEPTNDLDpITQ----SQILRLLSRmnqlnNTTIVLIGHDLTTITQWATRITVMY 233
Cdd:PRK13409 231 ADFYFFDEPTSYLD-IRQrlnvARLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
159-243 |
2.97e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 159 LTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQlNNTTIVLIGHDLTTITQWATRITVMYCGQS- 237
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLVa 470
|
....*...
gi 515624491 238 --VESADT 243
Cdd:PRK10982 471 giVDTKTT 478
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
162-255 |
3.15e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.74 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLsrMNQLNNTTIVLIGHDLTTITQwATRITVMYCGQSVESA 241
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECD 236
|
90
....*....|....
gi 515624491 242 DTQKLLDAPKHPYT 255
Cdd:cd03288 237 TPENLLAQEDGVFA 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
162-245 |
4.34e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624491 162 GQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRM-NQLNNTTIVLIGHDLTTITQWATRITVMYCGQSVES 240
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYF 292
|
....*
gi 515624491 241 ADTQK 245
Cdd:TIGR00956 293 GPADK 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
149-217 |
5.11e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.46 E-value: 5.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624491 149 SRLMDSYSYELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSRMNQLNNTTIVLIGH 217
Cdd:PRK10938 392 KRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
158-203 |
8.46e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 36.84 E-value: 8.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515624491 158 ELTDGQCQKVMIAMAIAAKPKILIADEPTNDLDPITQSQILRLLSR 203
Cdd:cd03232 108 GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| |
